Year |
Citation |
Score |
2023 |
Nieweglowska ES, Brilot AF, Méndez-Moran M, Kokontis C, Baek M, Li J, Cheng Y, Baker D, Bondy-Denomy J, Agard DA. The ϕPA3 phage nucleus is enclosed by a self-assembling 2D crystalline lattice. Nature Communications. 14: 927. PMID 36807264 DOI: 10.1038/s41467-023-36526-9 |
0.367 |
|
2023 |
Chen Z, Greenan GA, Shiozaki M, Liu Y, Skinner WM, Zhao X, Zhao S, Yan R, Yu Z, Lishko PV, Agard DA, Vale RD. In situ cryo-electron tomography reveals the asymmetric architecture of mammalian sperm axonemes. Nature Structural & Molecular Biology. PMID 36593309 DOI: 10.1038/s41594-022-00861-0 |
0.407 |
|
2022 |
Diwanji D, Trenker R, Thaker TM, Wang F, Agard DA, Verba KA, Jura N. Author Correction: Structures of the HER2-HER3-NRG1β complex reveal a dynamic dimer interface. Nature. PMID 35132240 DOI: 10.1038/s41586-021-04299-0 |
0.782 |
|
2022 |
Wang RY, Noddings CM, Kirschke E, Myasnikov AG, Johnson JL, Agard DA. Structure of Hsp90-Hsp70-Hop-GR reveals the Hsp90 client-loading mechanism. Nature. 601: 460-464. PMID 34937942 DOI: 10.1038/s41586-021-04252-1 |
0.787 |
|
2022 |
Noddings CM, Wang RY, Johnson JL, Agard DA. Structure of Hsp90-p23-GR reveals the Hsp90 client-remodelling mechanism. Nature. 601: 465-469. PMID 34937936 DOI: 10.1038/s41586-021-04236-1 |
0.577 |
|
2021 |
Croxford M, Elbaum M, Arigovindan M, Kam Z, Agard D, Villa E, Sedat J. Entropy-regularized deconvolution of cellular cryotransmission electron tomograms. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 34876518 DOI: 10.1073/pnas.2108738118 |
0.493 |
|
2021 |
Diwanji D, Trenker R, Thaker TM, Wang F, Agard DA, Verba KA, Jura N. Structures of the HER2-HER3-NRG1β complex reveal a dynamic dimer interface. Nature. PMID 34759323 DOI: 10.1038/s41586-021-04084-z |
0.789 |
|
2021 |
Verba K, Gupta M, Azumaya C, Moritz M, Pourmal S, Diallo A, Merz G, Jang G, Bouhaddou M, Fossati A, Brilot A, Diwanji D, Hernandez E, Herrera N, Kratochvil H, ... ... Agard D, et al. CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes. Research Square. PMID 34031651 DOI: 10.21203/rs.3.rs-515215/v1 |
0.784 |
|
2021 |
Gupta M, Azumaya CM, Moritz M, Pourmal S, Diallo A, Merz GE, Jang G, Bouhaddou M, Fossati A, Brilot AF, Diwanji D, Hernandez E, Herrera N, Kratochvil HT, Lam VL, ... ... Agard DA, et al. CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes. Biorxiv : the Preprint Server For Biology. PMID 34013269 DOI: 10.1101/2021.05.10.443524 |
0.784 |
|
2021 |
Sun M, Azumaya C, Tse E, Frost A, Southworth D, Verba KA, Cheng Y, Agard DA. Practical considerations for using K3 cameras in CDS mode for high-resolution and high-throughput single particle cryo-EM. Journal of Structural Biology. 107745. PMID 33984504 DOI: 10.1016/j.jsb.2021.107745 |
0.726 |
|
2021 |
Rice LM, Moritz M, Agard DA. Microtubules form by progressively faster tubulin accretion, not by nucleation-elongation. The Journal of Cell Biology. 220. PMID 33734292 DOI: 10.1083/jcb.202012079 |
0.624 |
|
2020 |
Gordon DE, Hiatt J, Bouhaddou M, Rezelj VV, Ulferts S, Braberg H, Jureka AS, Obernier K, Guo JZ, Batra J, Kaake RM, Weckstein AR, Owens TW, Gupta M, Pourmal S, ... ... Agard DA, et al. Comparative host-coronavirus protein interaction networks reveal pan-viral disease mechanisms. Science (New York, N.Y.). PMID 33060197 DOI: 10.1126/science.abe9403 |
0.753 |
|
2020 |
Wang F, Liu Y, Yu Z, Li S, Feng S, Cheng Y, Agard DA. General and robust covalently linked graphene oxide affinity grids for high-resolution cryo-EM. Proceedings of the National Academy of Sciences of the United States of America. PMID 32913054 DOI: 10.1073/Pnas.2009707117 |
0.42 |
|
2020 |
Wolff G, Limpens RWAL, Zevenhoven-Dobbe JC, Laugks U, Zheng S, de Jong AWM, Koning RI, Agard DA, Grünewald K, Koster AJ, Snijder EJ, Bárcena M. A molecular pore spans the double membrane of the coronavirus replication organelle. Science (New York, N.Y.). PMID 32763915 DOI: 10.1126/Science.Abd3629 |
0.303 |
|
2020 |
King BR, Moritz M, Kim H, Agard DA, Asbury CL, Davis TN. XMAP215 and γ-tubulin additively promote microtubule nucleation in purified solutions. Molecular Biology of the Cell. mbcE20020160. PMID 32726183 DOI: 10.1091/Mbc.E20-02-0160 |
0.31 |
|
2020 |
Gordon DE, Jang GM, Bouhaddou M, Xu J, Obernier K, O'Meara MJ, Guo JZ, Swaney DL, Tummino TA, Hüttenhain R, Kaake RM, Richards AL, Tutuncuoglu B, Foussard H, Batra J, ... ... Agard D, et al. A SARS-CoV-2-Human Protein-Protein Interaction Map Reveals Drug Targets and Potential Drug-Repurposing. Biorxiv : the Preprint Server For Biology. PMID 32511329 DOI: 10.1101/2020.03.22.002386 |
0.55 |
|
2020 |
Gordon DE, Jang GM, Bouhaddou M, Xu J, Obernier K, White KM, O'Meara MJ, Rezelj VV, Guo JZ, Swaney DL, Tummino TA, Huettenhain R, Kaake RM, Richards AL, Tutuncuoglu B, ... ... Agard DA, et al. A SARS-CoV-2 protein interaction map reveals targets for drug repurposing. Nature. PMID 32353859 DOI: 10.1038/S41586-020-2286-9 |
0.781 |
|
2020 |
Joshi A, Dai L, Liu Y, Lee J, Ghahhari NM, Segala G, Beebe K, Jenkins LM, Lyons GC, Bernasconi L, Tsai FTF, Agard DA, Neckers L, Picard D. The mitochondrial HSP90 paralog TRAP1 forms an OXPHOS-regulated tetramer and is involved in mitochondrial metabolic homeostasis. Bmc Biology. 18: 10. PMID 31987035 DOI: 10.1186/S12915-020-0740-7 |
0.376 |
|
2020 |
Greenan GA, Vale RD, Agard DA. Electron cryotomography of intact motile cilia defines the basal body to axoneme transition. The Journal of Cell Biology. 219. PMID 31874113 DOI: 10.1083/Jcb.201907060 |
0.361 |
|
2019 |
Wolff G, Limpens RWAL, Zheng S, Snijder EJ, Agard DA, Koster AJ, Bárcena M. Mind the gap: micro-expansion joints drastically decrease the bending of FIB-milled cryo-lamellae. Journal of Structural Biology. PMID 31536774 DOI: 10.1016/J.Jsb.2019.09.006 |
0.32 |
|
2019 |
Chaikeeratisak V, Khanna K, Nguyen KT, Sugie J, Egan ME, Erb ML, Vavilina A, Nonejuie P, Nieweglowska E, Pogliano K, Agard DA, Villa E, Pogliano J. Viral Capsid Trafficking along Treadmilling Tubulin Filaments in Bacteria. Cell. 177: 1771-1780.e12. PMID 31199917 DOI: 10.1016/J.Cell.2019.05.032 |
0.309 |
|
2019 |
Li S, Fernandez JJ, Marshall WF, Agard DA. Electron cryo-tomography provides insight into procentriole architecture and assembly mechanism. Elife. 8. PMID 30741631 DOI: 10.7554/Elife.43434 |
0.572 |
|
2019 |
Li S, Fernandez J, Marshall WF, Agard DA. Author response: Electron cryo-tomography provides insight into procentriole architecture and assembly mechanism Elife. DOI: 10.7554/Elife.43434.060 |
0.511 |
|
2018 |
Freilich R, Betegon M, Tse E, Mok SA, Julien O, Agard DA, Southworth DR, Takeuchi K, Gestwicki JE. Competing protein-protein interactions regulate binding of Hsp27 to its client protein tau. Nature Communications. 9: 4563. PMID 30385828 DOI: 10.1038/S41467-018-07012-4 |
0.33 |
|
2018 |
Greenan GA, Keszthelyi B, Vale RD, Agard DA. Insights into centriole geometry revealed by cryoTomography of doublet and triplet centrioles. Elife. 7. PMID 30080137 DOI: 10.7554/Elife.36851 |
0.364 |
|
2018 |
Elnatan D, Agard DA. Calcium binding to a remote site can replace magnesium as cofactor for mitochondrial Hsp90 (TRAP1) ATPase activity. The Journal of Biological Chemistry. PMID 29991590 DOI: 10.1074/Jbc.Ra118.003562 |
0.303 |
|
2018 |
Kalia R, Wang RY, Yusuf A, Thomas PV, Agard DA, Shaw JM, Frost A. Structural basis of mitochondrial receptor binding and constriction by DRP1. Nature. PMID 29899447 DOI: 10.1038/S41586-018-0211-2 |
0.606 |
|
2018 |
Moroni E, Agard DA, Colombo G. The Structural Asymmetry of Mitochondrial Hsp90 (Trap1) Determines Fine Tuning of Functional Dynamics. Journal of Chemical Theory and Computation. PMID 29320629 DOI: 10.1021/Acs.Jctc.7B00766 |
0.383 |
|
2018 |
Citron YR, Fagerstrom CJ, Keszthelyi B, Huang B, Rusan NM, Kelly MJS, Agard DA. The centrosomin CM2 domain is a multi-functional binding domain with distinct cell cycle roles. Plos One. 13: e0190530. PMID 29315319 DOI: 10.1371/Journal.Pone.0190530 |
0.392 |
|
2018 |
Liu Y, Agard DA. Structural Insights into the Regulation Mechanism of HSP90 by Co-chaperone AHA1 Biophysical Journal. 114: 162a. DOI: 10.1016/J.Bpj.2017.11.907 |
0.455 |
|
2017 |
Verba KA, Agard DA. Protein Expression and Purification of the Hsp90-Cdc37-Cdk4 Kinase Complex from Saccharomyces cerevisiae. Bio-Protocol. 7. PMID 29104897 DOI: 10.21769/BioProtoc.2563 |
0.739 |
|
2017 |
Verba KA, Agard DA. How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches. Trends in Biochemical Sciences. PMID 28784328 DOI: 10.1016/J.Tibs.2017.07.002 |
0.74 |
|
2017 |
Elnatan D, Betegon M, Liu Y, Ramelot T, Kennedy MA, Agard DA. Symmetry broken and rebroken during the ATP hydrolysis cycle of the mitochondrial Hsp90 TRAP1. Elife. 6. PMID 28742020 DOI: 10.7554/Elife.25235 |
0.464 |
|
2017 |
Pederson K, Chalmers GR, Gao Q, Elnatan D, Ramelot TA, Ma LC, Montelione GT, Kennedy MA, Agard DA, Prestegard JH. NMR characterization of HtpG, the E. coli Hsp90, using sparse labeling with (13)C-methyl alanine. Journal of Biomolecular Nmr. PMID 28653216 DOI: 10.1007/S10858-017-0123-8 |
0.344 |
|
2017 |
Larson AG, Elnatan D, Keenen MM, Trnka MJ, Johnston JB, Burlingame AL, Agard DA, Redding S, Narlikar GJ. Liquid droplet formation by HP1α suggests a role for phase separation in heterochromatin. Nature. PMID 28636604 DOI: 10.1038/Nature22822 |
0.32 |
|
2017 |
Zheng SQ, Palovcak E, Armache JP, Verba KA, Cheng Y, Agard DA. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy. Nature Methods. PMID 28250466 DOI: 10.1038/Nmeth.4193 |
0.72 |
|
2017 |
Chaikeeratisak V, Nguyen K, Khanna K, Brilot AF, Erb ML, Coker JK, Vavilina A, Newton GL, Buschauer R, Pogliano K, Villa E, Agard DA, Pogliano J. Assembly of a nucleus-like structure during viral replication in bacteria. Science (New York, N.Y.). 355: 194-197. PMID 28082593 DOI: 10.1126/Science.Aal2130 |
0.358 |
|
2017 |
Elnatan D, Betegon M, Liu Y, Ramelot T, Kennedy MA, Agard DA. Author response: Symmetry broken and rebroken during the ATP hydrolysis cycle of the mitochondrial Hsp90 TRAP1 Elife. DOI: 10.7554/Elife.25235.016 |
0.38 |
|
2017 |
Verba KA, Agard DA. Kinase Regulation Through Dramatic Unfolding, as Told by Hsp90:Cdc37:Cdk4 Atomic Cryoem Structure Biophysical Journal. 112: 14a. DOI: 10.1016/J.Bpj.2016.11.108 |
0.313 |
|
2016 |
Duan D, Torosyan H, Elnatan D, McLaughlin CK, Logie J, Shoichet MS, Agard DA, Shoichet BK. Internal Structure and Preferential Protein Binding of Colloidal Aggregates. Acs Chemical Biology. PMID 27983786 DOI: 10.1021/Acschembio.6B00791 |
0.796 |
|
2016 |
Verba KA, Wang RY, Arakawa A, Liu Y, Shirouzu M, Yokoyama S, Agard DA. Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase. Science (New York, N.Y.). 352: 1542-7. PMID 27339980 DOI: 10.1126/Science.Aaf5023 |
0.787 |
|
2016 |
Lyon AS, Morin G, Moritz M, Yabut KC, Vojnar T, Zelter A, Muller E, Davis TN, Agard DA. Higher-order oligomerization of Spc110p drives γ-tubulin ring complex assembly. Molecular Biology of the Cell. 27: 2245-58. PMID 27226487 DOI: 10.1091/Mbc.E16-02-0072 |
0.331 |
|
2016 |
Vettoretti G, Moroni E, Sattin S, Tao J, Agard DA, Bernardi A, Colombo G. Molecular Dynamics Simulations Reveal the Mechanisms of Allosteric Activation of Hsp90 by Designed Ligands. Scientific Reports. 6: 23830. PMID 27032695 DOI: 10.1038/Srep23830 |
0.346 |
|
2016 |
Greenberg CH, Kollman J, Zelter A, Johnson R, MacCoss MJ, Davis TN, Agard DA, Sali A. Structure of γ-tubulin small complex based on a cryo-EM map, chemical cross-links, and a remotely related structure. Journal of Structural Biology. PMID 26968363 DOI: 10.1016/J.Jsb.2016.03.006 |
0.669 |
|
2016 |
Sattin S, Panza M, Vasile F, Berni F, Goti G, Tao J, Moroni E, Agard D, Colombo G, Bernardi A. Synthesis of Functionalized 2-(4-Hydroxyphenyl)-3-methylbenzofuran Allosteric Modulators of Hsp90 Activity European Journal of Organic Chemistry. 2016: 3349-3364. DOI: 10.1002/Ejoc.201600420 |
0.356 |
|
2015 |
Pimentel-Elardo SM, Sørensen D, Ho L, Ziko M, Bueler SA, Lu S, Tao J, Moser A, Lee R, Agard D, Fairn G, Rubinstein JL, Shoichet BK, Nodwell JR. Activity-Independent Discovery of Secondary Metabolites Using Chemical Elicitation and Cheminformatic Inference. Acs Chemical Biology. PMID 26352211 DOI: 10.1021/Acschembio.5B00612 |
0.544 |
|
2015 |
Chiu PL, Li X, Li Z, Beckett B, Brilot AF, Grigorieff N, Agard DA, Cheng Y, Walz T. Evaluation of super-resolution performance of the K2 electron-counting camera using 2D crystals of aquaporin-0. Journal of Structural Biology. PMID 26318383 DOI: 10.1016/J.Jsb.2015.08.015 |
0.576 |
|
2015 |
Sattin S, Tao J, Vettoretti G, Moroni E, Pennati M, Lopergolo A, Morelli L, Bugatti A, Zuehlke A, Moses M, Prince T, Kijima T, Beebe K, Rusnati M, Neckers L, ... ... Agard DA, et al. Activation of Hsp90 Enzymatic Activity and Conformational Dynamics through Rationally Designed Allosteric Ligands. Chemistry (Weinheim An Der Bergstrasse, Germany). 21: 13598-608. PMID 26286886 DOI: 10.1002/Chem.201502211 |
0.327 |
|
2015 |
Peng Y, Moritz M, Han X, Giddings TH, Lyon A, Kollman J, Winey M, Yates J, Agard DA, Drubin DG, Barnes G. Interaction of CK1δ with γTuSC ensures proper microtubule assembly and spindle positioning. Molecular Biology of the Cell. 26: 2505-18. PMID 25971801 DOI: 10.1091/Mbc.E14-12-1627 |
0.649 |
|
2015 |
Morgner N, Schmidt C, Beilsten-Edmands V, Ebong IO, Patel NA, Clerico EM, Kirschke E, Daturpalli S, Jackson SE, Agard D, Robinson CV. Hsp70 forms antiparallel dimers stabilized by post-translational modifications to position clients for transfer to Hsp90. Cell Reports. 11: 759-69. PMID 25921532 DOI: 10.1016/J.Celrep.2015.03.063 |
0.782 |
|
2015 |
Cheng A, Henderson R, Mastronarde D, Ludtke SJ, Schoenmakers RH, Short J, Marabini R, Dallakyan S, Agard D, Winn M. MRC2014: Extensions to the MRC format header for electron cryo-microscopy and tomography. Journal of Structural Biology. PMID 25882513 DOI: 10.1016/J.Jsb.2015.04.002 |
0.505 |
|
2015 |
Kollman JM, Greenberg CH, Li S, Moritz M, Zelter A, Fong KK, Fernandez JJ, Sali A, Kilmartin J, Davis TN, Agard DA. Ring closure activates yeast γTuRC for species-specific microtubule nucleation. Nature Structural & Molecular Biology. 22: 132-7. PMID 25599398 DOI: 10.1038/Nsmb.2953 |
0.649 |
|
2014 |
Partridge JR, Lavery LA, Elnatan D, Naber N, Cooke R, Agard DA. A novel N-terminal extension in mitochondrial TRAP1 serves as a thermal regulator of chaperone activity. Elife. 3. PMID 25531069 DOI: 10.7554/Elife.03487 |
0.584 |
|
2014 |
Erb ML, Kraemer JA, Coker JK, Chaikeeratisak V, Nonejuie P, Agard DA, Pogliano J. A bacteriophage tubulin harnesses dynamic instability to center DNA in infected cells. Elife. 3. PMID 25429514 DOI: 10.7554/Elife.03197 |
0.792 |
|
2014 |
Kirschke E, Goswami D, Southworth D, Griffin PR, Agard DA. Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cycles. Cell. 157: 1685-97. PMID 24949977 DOI: 10.1016/J.Cell.2014.04.038 |
0.781 |
|
2014 |
Street TO, Zeng X, Pellarin R, Bonomi M, Sali A, Kelly MJ, Chu F, Agard DA. Elucidating the mechanism of substrate recognition by the bacterial Hsp90 molecular chaperone. Journal of Molecular Biology. 426: 2393-404. PMID 24726919 DOI: 10.1016/J.Jmb.2014.04.001 |
0.377 |
|
2014 |
Schax E, Walter JG, Märzhäuser H, Stahl F, Scheper T, Agard DA, Eichner S, Kirschning A, Zeilinger C. Microarray-based screening of heat shock protein inhibitors. Journal of Biotechnology. 180: 1-9. PMID 24667540 DOI: 10.1016/J.Jbiotec.2014.03.006 |
0.33 |
|
2014 |
Prestegard JH, Agard DA, Moremen KW, Lavery LA, Morris LC, Pederson K. Sparse labeling of proteins: structural characterization from long range constraints. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 241: 32-40. PMID 24656078 DOI: 10.1016/J.Jmr.2013.12.012 |
0.585 |
|
2014 |
Zehr EA, Kraemer JA, Erb ML, Coker JK, Montabana EA, Pogliano J, Agard DA. The structure and assembly mechanism of a novel three-stranded tubulin filament that centers phage DNA. Structure (London, England : 1993). 22: 539-48. PMID 24631461 DOI: 10.1016/J.Str.2014.02.006 |
0.805 |
|
2014 |
Montabana EA, Agard DA. Bacterial tubulin TubZ-Bt transitions between a two-stranded intermediate and a four-stranded filament upon GTP hydrolysis. Proceedings of the National Academy of Sciences of the United States of America. 111: 3407-12. PMID 24550513 DOI: 10.1073/Pnas.1318339111 |
0.791 |
|
2014 |
Peng LX, Hsu MT, Bonomi M, Agard DA, Jacobson MP. The free energy profile of tubulin straight-bent conformational changes, with implications for microtubule assembly and drug discovery. Plos Computational Biology. 10: e1003464. PMID 24516374 DOI: 10.1371/Journal.Pcbi.1003464 |
0.342 |
|
2014 |
Lavery LA, Partridge JR, Ramelot TA, Elnatan D, Kennedy MA, Agard DA. Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism. Molecular Cell. 53: 330-43. PMID 24462206 DOI: 10.1016/J.Molcel.2013.12.023 |
0.603 |
|
2014 |
Mennella V, Agard DA, Huang B, Pelletier L. Amorphous no more: subdiffraction view of the pericentriolar material architecture. Trends in Cell Biology. 24: 188-97. PMID 24268653 DOI: 10.1016/J.Tcb.2013.10.001 |
0.346 |
|
2014 |
Partridge JR, Lavery LA, Elnatan D, Naber N, Cooke R, Agard DA. Author response: A novel N-terminal extension in mitochondrial TRAP1 serves as a thermal regulator of chaperone activity Elife. DOI: 10.7554/Elife.03487.021 |
0.515 |
|
2014 |
Erb ML, Kraemer JA, Coker JKC, Chaikeeratisak V, Nonejuie P, Agard DA, Pogliano J. Author response: A bacteriophage tubulin harnesses dynamic instability to center DNA in infected cells Elife. DOI: 10.7554/Elife.03197.021 |
0.762 |
|
2013 |
Miao Y, Wong CC, Mennella V, Michelot A, Agard DA, Holt LJ, Yates JR, Drubin DG. Cell-cycle regulation of formin-mediated actin cable assembly. Proceedings of the National Academy of Sciences of the United States of America. 110: E4446-55. PMID 24133141 DOI: 10.1073/Pnas.1314000110 |
0.318 |
|
2013 |
Arigovindan M, Fung JC, Elnatan D, Mennella V, Chan YH, Pollard M, Branlund E, Sedat JW, Agard DA. High-resolution restoration of 3D structures from widefield images with extreme low signal-to-noise-ratio. Proceedings of the National Academy of Sciences of the United States of America. 110: 17344-9. PMID 24106307 DOI: 10.1073/Pnas.1315675110 |
0.581 |
|
2013 |
Li X, Mooney P, Zheng S, Booth CR, Braunfeld MB, Gubbens S, Agard DA, Cheng Y. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nature Methods. 10: 584-90. PMID 23644547 DOI: 10.1038/Nmeth.2472 |
0.339 |
|
2013 |
Genest O, Reidy M, Street TO, Hoskins JR, Camberg JL, Agard DA, Masison DC, Wickner S. Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast. Molecular Cell. 49: 464-73. PMID 23260660 DOI: 10.1016/J.Molcel.2012.11.017 |
0.33 |
|
2013 |
Abrahamsson S, Chen J, Hajj B, Stallinga S, Katsov AY, Wisniewski J, Mizuguchi G, Soule P, Mueller F, Dugast Darzacq C, Darzacq X, Wu C, Bargmann CI, Agard DA, Dahan M, et al. Fast multicolor 3D imaging using aberration-corrected multifocus microscopy. Nature Methods. 10: 60-3. PMID 23223154 DOI: 10.1038/Nmeth.2277 |
0.723 |
|
2013 |
Ozyamak E, Kollman J, Agard DA, Komeili A. The bacterial actin MamK: in vitro assembly behavior and filament architecture. The Journal of Biological Chemistry. 288: 4265-77. PMID 23204522 DOI: 10.1074/Jbc.M112.417030 |
0.659 |
|
2013 |
Jaswal SS, Fuhrmann CN, Ota N, Rader SD, Agard DA. α-Lytic Protease Handbook of Proteolytic Enzymes. 3: 2558-2565. DOI: 10.1016/B978-0-12-382219-2.00567-6 |
0.484 |
|
2012 |
Schneidman-Duhovny D, Rossi A, Avila-Sakar A, Kim SJ, Velázquez-Muriel J, Strop P, Liang H, Krukenberg KA, Liao M, Kim HM, Sobhanifar S, Dötsch V, Rajpal A, Pons J, Agard DA, et al. A method for integrative structure determination of protein-protein complexes. Bioinformatics (Oxford, England). 28: 3282-9. PMID 23093611 DOI: 10.1093/Bioinformatics/Bts628 |
0.767 |
|
2012 |
Mennella V, Keszthelyi B, McDonald KL, Chhun B, Kan F, Rogers GC, Huang B, Agard DA. Subdiffraction-resolution fluorescence microscopy reveals a domain of the centrosome critical for pericentriolar material organization. Nature Cell Biology. 14: 1159-68. PMID 23086239 DOI: 10.1038/Ncb2597 |
0.36 |
|
2012 |
Kraemer JA, Erb ML, Waddling CA, Montabana EA, Zehr EA, Wang H, Nguyen K, Pham DS, Agard DA, Pogliano J. A phage tubulin assembles dynamic filaments by an atypical mechanism to center viral DNA within the host cell. Cell. 149: 1488-99. PMID 22726436 DOI: 10.1016/J.Cell.2012.04.034 |
0.798 |
|
2012 |
Cunningham CN, Southworth DR, Krukenberg KA, Agard DA. The conserved arginine 380 of Hsp90 is not a catalytic residue, but stabilizes the closed conformation required for ATP hydrolysis. Protein Science : a Publication of the Protein Society. 21: 1162-71. PMID 22653663 DOI: 10.1002/Pro.2103 |
0.807 |
|
2012 |
Kelch BA, Salimi NL, Agard DA. Functional modulation of a protein folding landscape via side-chain distortion. Proceedings of the National Academy of Sciences of the United States of America. 109: 9414-9. PMID 22635267 DOI: 10.1073/Pnas.1119274109 |
0.786 |
|
2012 |
Shao L, Winoto L, Agard DA, Gustafsson MG, Sedat JW. Interferometer-based structured-illumination microscopy utilizing complementary phase relationship through constructive and destructive image detection by two cameras. Journal of Microscopy. 246: 229-36. PMID 22472010 DOI: 10.1111/J.1365-2818.2012.03604.X |
0.663 |
|
2012 |
Arigovindan M, Sedat JW, Agard DA. Effect of depth dependent spherical aberrations in 3D structured illumination microscopy. Optics Express. 20: 6527-41. PMID 22418536 DOI: 10.1364/Oe.20.006527 |
0.563 |
|
2012 |
Li S, Fernandez JJ, Marshall WF, Agard DA. Three-dimensional structure of basal body triplet revealed by electron cryo-tomography. The Embo Journal. 31: 552-62. PMID 22157822 DOI: 10.1038/Emboj.2011.460 |
0.564 |
|
2012 |
Street TO, Lavery LA, Verba KA, Lee CT, Mayer MP, Agard DA. Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activity. Journal of Molecular Biology. 415: 3-15. PMID 22063096 DOI: 10.1016/J.Jmb.2011.10.038 |
0.8 |
|
2012 |
Agard D. Conformational Dynamics, Structure & Substrate Protein Interactions of Hsp90 Chaperones Biophysical Journal. 102: 428a. DOI: 10.1016/J.Bpj.2011.11.2341 |
0.363 |
|
2011 |
Alexander LD, Partridge JR, Agard DA, McAlpine SR. A small molecule that preferentially binds the closed conformation of Hsp90. Bioorganic & Medicinal Chemistry Letters. 21: 7068-71. PMID 22014826 DOI: 10.1016/J.Bmcl.2011.09.096 |
0.302 |
|
2011 |
Kollman JM, Merdes A, Mourey L, Agard DA. Microtubule nucleation by γ-tubulin complexes. Nature Reviews. Molecular Cell Biology. 12: 709-21. PMID 21993292 DOI: 10.1038/Nrm3209 |
0.673 |
|
2011 |
Zheng SQ, Branlund E, Kesthelyi B, Braunfeld MB, Cheng Y, Sedat JW, Agard DA. A distributed multi-GPU system for high speed electron microscopic tomographic reconstruction. Ultramicroscopy. 111: 1137-43. PMID 21741915 DOI: 10.1016/J.Ultramic.2011.03.015 |
0.544 |
|
2011 |
Guillet V, Knibiehler M, Gregory-Pauron L, Remy MH, Chemin C, Raynaud-Messina B, Bon C, Kollman JM, Agard DA, Merdes A, Mourey L. Crystal structure of γ-tubulin complex protein GCP4 provides insight into microtubule nucleation. Nature Structural & Molecular Biology. 18: 915-9. PMID 21725292 DOI: 10.1038/Nsmb.2083 |
0.686 |
|
2011 |
Southworth DR, Agard DA. Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex. Molecular Cell. 42: 771-81. PMID 21700222 DOI: 10.1016/J.Molcel.2011.04.023 |
0.37 |
|
2011 |
Gopalakrishnan J, Mennella V, Blachon S, Zhai B, Smith AH, Megraw TL, Nicastro D, Gygi SP, Agard DA, Avidor-Reiss T. Sas-4 provides a scaffold for cytoplasmic complexes and tethers them in a centrosome. Nature Communications. 2: 359. PMID 21694707 DOI: 10.1038/Ncomms1367 |
0.339 |
|
2011 |
Street TO, Lavery LA, Agard DA. Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone. Molecular Cell. 42: 96-105. PMID 21474071 DOI: 10.1016/J.Molcel.2011.01.029 |
0.605 |
|
2011 |
Krukenberg KA, Street TO, Lavery LA, Agard DA. Conformational dynamics of the molecular chaperone Hsp90. Quarterly Reviews of Biophysics. 44: 229-55. PMID 21414251 DOI: 10.1017/S0033583510000314 |
0.803 |
|
2011 |
Rivera CR, Kollman JM, Polka JK, Agard DA, Mullins RD. Architecture and assembly of a divergent member of the ParM family of bacterial actin-like proteins. The Journal of Biological Chemistry. 286: 14282-90. PMID 21339292 DOI: 10.1074/Jbc.M110.203828 |
0.652 |
|
2011 |
Kner P, Kam Z, Agard D, Sedat J. Adaptive optics in wide-field microscopy Proceedings of Spie - the International Society For Optical Engineering. 7931. DOI: 10.1117/12.876500 |
0.688 |
|
2011 |
Street TO, Lavery L, Agard DA. Elucidating the Mechanism of Protein Remodeling by the Hsp90 Molecular Chaperone Biophysical Journal. 100: 390a. DOI: 10.1016/J.Bpj.2010.12.2318 |
0.615 |
|
2010 |
Kner P, Winoto L, Agard DA, Sedat JW. Closed loop adaptive optics for microscopy without a wavefront sensor. Proceedings of Spie--the International Society For Optical Engineering. 7570. PMID 24392198 DOI: 10.1117/12.840943 |
0.731 |
|
2010 |
Zheng SQ, Sedat JW, Agard DA. Automated data collection for electron microscopic tomography. Methods in Enzymology. 481: 283-315. PMID 20887862 DOI: 10.1016/S0076-6879(10)81012-2 |
0.551 |
|
2010 |
Matsuda A, Shao L, Boulanger J, Kervrann C, Carlton PM, Kner P, Agard D, Sedat JW. Condensed mitotic chromosome structure at nanometer resolution using PALM and EGFP- histones. Plos One. 5: e12768. PMID 20856676 DOI: 10.1371/Journal.Pone.0012768 |
0.782 |
|
2010 |
Vasko RC, Rodriguez RA, Cunningham CN, Ardi VC, Agard DA, McAlpine SR. Mechanistic studies of Sansalvamide A-amide: an allosteric modulator of Hsp90. Acs Medicinal Chemistry Letters. 1: 4-8. PMID 20730035 DOI: 10.1021/Ml900003T |
0.751 |
|
2010 |
Carlton PM, Boulanger J, Kervrann C, Sibarita JB, Salamero J, Gordon-Messer S, Bressan D, Haber JE, Haase S, Shao L, Winoto L, Matsuda A, Kner P, Uzawa S, Gustafsson M, ... ... Agard DA, et al. Fast live simultaneous multiwavelength four-dimensional optical microscopy. Proceedings of the National Academy of Sciences of the United States of America. 107: 16016-22. PMID 20705899 DOI: 10.1073/Pnas.1004037107 |
0.795 |
|
2010 |
Kollman JM, Polka JK, Zelter A, Davis TN, Agard DA. Microtubule nucleating gamma-TuSC assembles structures with 13-fold microtubule-like symmetry. Nature. 466: 879-82. PMID 20631709 DOI: 10.1038/Nature09207 |
0.667 |
|
2010 |
Arigovindan M, Shaevitz J, McGowan J, Sedat JW, Agard DA. A Parallel Product-Convolution approach for representing the depth varying Point Spread Functions in 3D widefield microscopy based on principal component analysis. Optics Express. 18: 6461-76. PMID 20389670 DOI: 10.1364/Oe.18.006461 |
0.568 |
|
2010 |
Xu W, Xu F, Jones M, Keszthelyi B, Sedat J, Agard D, Mueller K. High-performance iterative electron tomography reconstruction with long-object compensation using graphics processing units (GPUs). Journal of Structural Biology. 171: 142-53. PMID 20371381 DOI: 10.1016/J.Jsb.2010.03.018 |
0.533 |
|
2010 |
Salimi NL, Ho B, Agard DA. Unfolding simulations reveal the mechanism of extreme unfolding cooperativity in the kinetically stable alpha-lytic protease. Plos Computational Biology. 6: e1000689. PMID 20195497 DOI: 10.1371/Journal.Pcbi.1000689 |
0.794 |
|
2010 |
Kner P, Sedat JW, Agard DA, Kam Z. High-resolution wide-field microscopy with adaptive optics for spherical aberration correction and motionless focusing. Journal of Microscopy. 237: 136-47. PMID 20096044 DOI: 10.1111/J.1365-2818.2009.03315.X |
0.74 |
|
2010 |
Gopalakrishnan J, Guichard P, Smith AH, Schwarz H, Agard DA, Marco S, Avidor-Reiss T. Self-assembling SAS-6 multimer is a core centriole building block. The Journal of Biological Chemistry. 285: 8759-70. PMID 20083610 DOI: 10.1074/Jbc.M109.092627 |
0.342 |
|
2010 |
Ho BK, Agard DA. Conserved tertiary couplings stabilize elements in the PDZ fold, leading to characteristic patterns of domain conformational flexibility. Protein Science : a Publication of the Protein Society. 19: 398-411. PMID 20052683 DOI: 10.1002/Pro.318 |
0.334 |
|
2010 |
Street TO, Krukenberg KA, Rosgen J, Bolen DW, Agard DA. Osmolyte-induced conformational changes in the Hsp90 molecular chaperone. Protein Science : a Publication of the Protein Society. 19: 57-65. PMID 19890989 DOI: 10.1002/Pro.282 |
0.765 |
|
2010 |
Xu F, Xu W, Jones M, Keszthelyi B, Sedat J, Agard D, Mueller K. On the efficiency of iterative ordered subset reconstruction algorithms for acceleration on GPUs. Computer Methods and Programs in Biomedicine. 98: 261-70. PMID 19850372 DOI: 10.1016/J.Cmpb.2009.09.003 |
0.527 |
|
2009 |
Choy RM, Kollman JM, Zelter A, Davis TN, Agard DA. Localization and orientation of the gamma-tubulin small complex components using protein tags as labels for single particle EM. Journal of Structural Biology. 168: 571-4. PMID 19723581 DOI: 10.1016/J.Jsb.2009.08.012 |
0.795 |
|
2009 |
Polka JK, Kollman JM, Agard DA, Mullins RD. The structure and assembly dynamics of plasmid actin AlfA imply a novel mechanism of DNA segregation. Journal of Bacteriology. 191: 6219-30. PMID 19666709 DOI: 10.1128/Jb.00676-09 |
0.665 |
|
2009 |
Krukenberg KA, Böttcher UM, Southworth DR, Agard DA. Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide. Protein Science : a Publication of the Protein Society. 18: 1815-27. PMID 19554567 DOI: 10.1002/Pro.191 |
0.758 |
|
2009 |
Zheng SQ, Matsuda A, Braunfeld MB, Sedat JW, Agard DA. Dual-axis target mapping and automated sequential acquisition of dual-axis EM tomographic data. Journal of Structural Biology. 168: 323-31. PMID 19545637 DOI: 10.1016/J.Jsb.2009.06.010 |
0.547 |
|
2009 |
Krukenberg KA, Southworth DR, Street TO, Agard DA. pH-dependent conformational changes in bacterial Hsp90 reveal a Grp94-like conformation at pH 6 that is highly active in suppression of citrate synthase aggregation. Journal of Molecular Biology. 390: 278-91. PMID 19427321 DOI: 10.1016/J.Jmb.2009.04.080 |
0.753 |
|
2009 |
Ho BK, Agard DA. Probing the flexibility of large conformational changes in protein structures through local perturbations. Plos Computational Biology. 5: e1000343. PMID 19343225 DOI: 10.1371/Journal.Pcbi.1000343 |
0.366 |
|
2009 |
Sedat J, Agard D, Kam Z, Boulange J, Carlton P, Shao L, Kner P, Matsuda A. S09-04 OMX, a new microscope platform for increased time and spatial resolution Mechanisms of Development. 126: S36. DOI: 10.1016/J.Mod.2009.06.1036 |
0.748 |
|
2008 |
Southworth DR, Agard DA. Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle. Molecular Cell. 32: 631-40. PMID 19061638 DOI: 10.1016/J.Molcel.2008.10.024 |
0.347 |
|
2008 |
Förster F, Webb B, Krukenberg KA, Tsuruta H, Agard DA, Sali A. Integration of small-angle X-ray scattering data into structural modeling of proteins and their assemblies. Journal of Molecular Biology. 382: 1089-106. PMID 18694757 DOI: 10.1016/J.Jmb.2008.07.074 |
0.765 |
|
2008 |
Schermelleh L, Carlton PM, Haase S, Shao L, Winoto L, Kner P, Burke B, Cardoso MC, Agard DA, Gustafsson MG, Leonhardt H, Sedat JW. Subdiffraction multicolor imaging of the nuclear periphery with 3D structured illumination microscopy. Science (New York, N.Y.). 320: 1332-6. PMID 18535242 DOI: 10.1126/Science.1156947 |
0.797 |
|
2008 |
Nölting B, Agard DA. How general is the nucleation-condensation mechanism? Proteins. 73: 754-64. PMID 18498109 DOI: 10.1002/Prot.22099 |
0.391 |
|
2008 |
Cunningham CN, Krukenberg KA, Agard DA. Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90. The Journal of Biological Chemistry. 283: 21170-8. PMID 18492664 DOI: 10.1074/Jbc.M800046200 |
0.806 |
|
2008 |
Krukenberg KA, Förster F, Rice LM, Sali A, Agard DA. Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90. Structure (London, England : 1993). 16: 755-65. PMID 18462680 DOI: 10.1016/J.Str.2008.01.021 |
0.8 |
|
2008 |
Trammell MA, Mahoney NM, Agard DA, Vale RD. Mob4 plays a role in spindle focusing in Drosophila S2 cells. Journal of Cell Science. 121: 1284-92. PMID 18388316 DOI: 10.1242/Jcs.017210 |
0.79 |
|
2008 |
Rice LM, Montabana EA, Agard DA. The lattice as allosteric effector: structural studies of alphabeta- and gamma-tubulin clarify the role of GTP in microtubule assembly. Proceedings of the National Academy of Sciences of the United States of America. 105: 5378-83. PMID 18388201 DOI: 10.1073/Pnas.0801155105 |
0.806 |
|
2008 |
Gustafsson MG, Shao L, Carlton PM, Wang CJ, Golubovskaya IN, Cande WZ, Agard DA, Sedat JW. Three-dimensional resolution doubling in wide-field fluorescence microscopy by structured illumination. Biophysical Journal. 94: 4957-70. PMID 18326650 DOI: 10.1529/Biophysj.107.120345 |
0.759 |
|
2008 |
Shao L, Isaac B, Uzawa S, Agard DA, Sedat JW, Gustafsson MG. I5S: wide-field light microscopy with 100-nm-scale resolution in three dimensions. Biophysical Journal. 94: 4971-83. PMID 18326649 DOI: 10.1529/Biophysj.107.120352 |
0.746 |
|
2008 |
Kollman JM, Zelter A, Muller EG, Fox B, Rice LM, Davis TN, Agard DA. The structure of the gamma-tubulin small complex: implications of its architecture and flexibility for microtubule nucleation. Molecular Biology of the Cell. 19: 207-15. PMID 17978090 DOI: 10.1091/Mbc.E07-09-0879 |
0.768 |
|
2008 |
Kner P, Sedat J, Agard D, Kam Z. Applying adaptive optics to three-dimensional wide-field microscopy Proceedings of Spie - the International Society For Optical Engineering. 6888. DOI: 10.1117/12.773731 |
0.695 |
|
2008 |
Zheng SQ, Braunfeld MB, Sedat JW, Agard DA. Serial acquisition of dual axis EM tomographic data Microscopy and Microanalysis. 14: 1320-1321. DOI: 10.1017/S1431927608083530 |
0.526 |
|
2007 |
Kelch BA, Agard DA. Mesophile versus thermophile: insights into the structural mechanisms of kinetic stability. Journal of Molecular Biology. 370: 784-95. PMID 17543987 DOI: 10.1016/J.Jmb.2007.04.078 |
0.735 |
|
2007 |
Hom EF, Marchis F, Lee TK, Haase S, Agard DA, Sedat JW. AIDA: an adaptive image deconvolution algorithm with application to multi-frame and three-dimensional data. Journal of the Optical Society of America. a, Optics, Image Science, and Vision. 24: 1580-600. PMID 17491626 DOI: 10.1364/Josaa.24.001580 |
0.776 |
|
2007 |
Kelch BA, Eagen KP, Erciyas FP, Humphris EL, Thomason AR, Mitsuiki S, Agard DA. Structural and mechanistic exploration of acid resistance: kinetic stability facilitates evolution of extremophilic behavior. Journal of Molecular Biology. 368: 870-83. PMID 17382344 DOI: 10.1016/J.Jmb.2007.02.032 |
0.716 |
|
2007 |
Kam Z, Kner P, Agard D, Sedat JW. Modelling the application of adaptive optics to wide-field microscope live imaging. Journal of Microscopy. 226: 33-42. PMID 17381707 DOI: 10.1111/J.1365-2818.2007.01751.X |
0.732 |
|
2007 |
König P, Braunfeld MB, Sedat JW, Agard DA. The three-dimensional structure of in vitro reconstituted Xenopus laevis chromosomes by EM tomography. Chromosoma. 116: 349-72. PMID 17333236 DOI: 10.1007/S00412-007-0101-0 |
0.565 |
|
2007 |
Zheng SQ, Kollman JM, Braunfeld MB, Sedat JW, Agard DA. Automated acquisition of electron microscopic random conical tilt sets. Journal of Structural Biology. 157: 148-55. PMID 17169745 DOI: 10.1016/J.Jsb.2006.10.026 |
0.725 |
|
2007 |
Zheng SQ, Keszthelyi B, Branlund E, Lyle JM, Braunfeld MB, Sedat JW, Agard DA. UCSF tomography: an integrated software suite for real-time electron microscopic tomographic data collection, alignment, and reconstruction. Journal of Structural Biology. 157: 138-47. PMID 16904341 DOI: 10.1016/J.Jsb.2006.06.005 |
0.555 |
|
2007 |
Moss WC, Haase S, Lyle JM, Agard DA, Sedat JW. Reply to letter to the editor Journal of Microscopy. 225: 108. DOI: 10.1111/j.1365-2818.2007.01734.x |
0.418 |
|
2006 |
Shiau AK, Harris SF, Southworth DR, Agard DA. Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements. Cell. 127: 329-40. PMID 17055434 DOI: 10.1016/J.Cell.2006.09.027 |
0.387 |
|
2006 |
Zheng SQ, Braunfeld MB, Keszthelyi B, Branlund E, Kollman JM, Sedat JW, Agard DA. Automated acquisition of tomographic and random conical tilt series and real-time reconstruction using UCSF tmography Microscopy and Microanalysis. 12: 88-89. DOI: 10.1017/S1431927606065871 |
0.691 |
|
2005 |
Moss WC, Haase S, Lyle JM, Agard DA, Sedat JW. A novel 3D wavelet-based filter for visualizing features in noisy biological data. Journal of Microscopy. 219: 43-9. PMID 16159339 DOI: 10.1111/J.1365-2818.2005.01492.X |
0.533 |
|
2005 |
Truhlar SM, Agard DA. The folding landscape of an alpha-lytic protease variant reveals the role of a conserved beta-hairpin in the development of kinetic stability. Proteins. 61: 105-14. PMID 16044461 DOI: 10.1002/Prot.20525 |
0.783 |
|
2005 |
Ota N, Agard DA. Intramolecular signaling pathways revealed by modeling anisotropic thermal diffusion. Journal of Molecular Biology. 351: 345-54. PMID 16005893 DOI: 10.1016/J.Jmb.2005.05.043 |
0.303 |
|
2005 |
Aldaz H, Rice LM, Stearns T, Agard DA. Insights into microtubule nucleation from the crystal structure of human gamma-tubulin. Nature. 435: 523-7. PMID 15917813 DOI: 10.1038/Nature03586 |
0.789 |
|
2005 |
Jaswal SS, Truhlar SM, Dill KA, Agard DA. Comprehensive analysis of protein folding activation thermodynamics reveals a universal behavior violated by kinetically stable proteases. Journal of Molecular Biology. 347: 355-66. PMID 15740746 DOI: 10.1016/J.Jmb.2005.01.032 |
0.786 |
|
2004 |
Hanser BM, Gustafsson MG, Agard DA, Sedat JW. Phase-retrieved pupil functions in wide-field fluorescence microscopy. Journal of Microscopy. 216: 32-48. PMID 15369481 DOI: 10.1111/J.0022-2720.2004.01393.X |
0.78 |
|
2004 |
Harris SF, Shiau AK, Agard DA. The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site. Structure (London, England : 1993). 12: 1087-97. PMID 15274928 DOI: 10.1016/J.Str.2004.03.020 |
0.385 |
|
2004 |
Zheng QS, Braunfeld MB, Sedat JW, Agard DA. An improved strategy for automated electron microscopic tomography. Journal of Structural Biology. 147: 91-101. PMID 15193638 DOI: 10.1016/J.Jsb.2004.02.005 |
0.561 |
|
2004 |
Fuhrmann CN, Kelch BA, Ota N, Agard DA. The 0.83 A resolution crystal structure of alpha-lytic protease reveals the detailed structure of the active site and identifies a source of conformational strain. Journal of Molecular Biology. 338: 999-1013. PMID 15111063 DOI: 10.1016/J.Jmb.2004.03.018 |
0.725 |
|
2004 |
Cunningham EL, Agard DA. Disabling the folding catalyst is the last critical step in alpha-lytic protease folding. Protein Science : a Publication of the Protein Society. 13: 325-31. PMID 14739318 DOI: 10.1110/Ps.03389704 |
0.725 |
|
2004 |
Truhlar SM, Cunningham EL, Agard DA. The folding landscape of Streptomyces griseus protease B reveals the energetic costs and benefits associated with evolving kinetic stability. Protein Science : a Publication of the Protein Society. 13: 381-90. PMID 14718653 DOI: 10.1110/Ps.03336804 |
0.781 |
|
2004 |
Bailey B, Agard DA, Sedat JW, Barfels M, Chao H, Mooney PE. Performance evaluation of a transmission scintillator-based lens-coupled 4K CCD camera for use in low-dose electron cryo-microscopy Microscopy and Microanalysis. 10: 1204-1205. DOI: 10.1017/S1431927604886458 |
0.525 |
|
2004 |
Gustafsson MGL, Shao L, Agard DA, Sedat JW. Fluorescence microscopy without resolution limit Leos Summer Topical Meeting. 25-26. |
0.492 |
|
2003 |
Cunningham EL, Agard DA. Interdependent folding of the N- and C-terminal domains defines the cooperative folding of alpha-lytic protease. Biochemistry. 42: 13212-9. PMID 14609332 DOI: 10.1021/Bi035409Q |
0.73 |
|
2003 |
Hanser BM, Gustafsson MG, Agard DA, Sedat JW. Phase retrieval for high-numerical-aperture optical systems. Optics Letters. 28: 801-3. PMID 12779151 DOI: 10.1364/Ol.28.000801 |
0.775 |
|
2002 |
Chen CY, Reese ML, Hwang PK, Ota N, Agard D, Brodsky FM. Clathrin light and heavy chain interface: alpha-helix binding superhelix loops via critical tryptophans. The Embo Journal. 21: 6072-82. PMID 12426379 DOI: 10.1093/Emboj/Cdf594 |
0.352 |
|
2002 |
Rice LM, Agard DA. Centriole duplication: centrin in on answers? Current Biology : Cb. 12: R618-9. PMID 12372266 DOI: 10.1016/S0960-9822(02)01133-8 |
0.636 |
|
2002 |
Cunningham EL, Mau T, Truhlar SM, Agard DA. The pro region N-terminal domain provides specific interactions required for catalysis of alpha-lytic protease folding. Biochemistry. 41: 8860-7. PMID 12102628 DOI: 10.1021/Bi020214O |
0.78 |
|
2002 |
Wille H, Michelitsch MD, Guenebaut V, Supattapone S, Serban A, Cohen FE, Agard DA, Prusiner SB. Structural studies of the scrapie prion protein by electron crystallography. Proceedings of the National Academy of Sciences of the United States of America. 99: 3563-8. PMID 11891310 DOI: 10.1073/Pnas.052703499 |
0.366 |
|
2002 |
Jaswal SS, Sohl JL, Davis JH, Agard DA. Energetic landscape of alpha-lytic protease optimizes longevity through kinetic stability. Nature. 415: 343-6. PMID 11797014 DOI: 10.1038/415343A |
0.609 |
|
2002 |
Hanser BM, Gustafsson MGL, Agard DA, Sedat JW. Application of phase retrieved pupil functions in wide-field fluorescence microscopy Proceedings of Spie - the International Society For Optical Engineering. 4621: 40-46. DOI: 10.1117/12.467844 |
0.77 |
|
2001 |
Ota N, Agard DA. Binding mode prediction for a flexible ligand in a flexible pocket using multi-conformation simulated annealing pseudo crystallographic refinement. Journal of Molecular Biology. 314: 607-17. PMID 11846570 DOI: 10.1006/Jmbi.2001.5147 |
0.314 |
|
2001 |
Tonelli M, Peters RJ, James TL, Agard DA. The solution structure of the viral binding domain of Tva, the cellular receptor for subgroup A avian leukosis and sarcoma virus. Febs Letters. 509: 161-8. PMID 11768384 DOI: 10.1016/S0014-5793(01)03086-1 |
0.314 |
|
2001 |
Murphy SM, Preble AM, Patel UK, O'Connell KL, Dias DP, Moritz M, Agard D, Stults JT, Stearns T. GCP5 and GCP6: two new members of the human gamma-tubulin complex. Molecular Biology of the Cell. 12: 3340-52. PMID 11694571 DOI: 10.1091/Mbc.12.11.3340 |
0.313 |
|
2001 |
Moritz M, Braunfeld MB, Alberts BM, Agard DA. Reconstitution of centrosome microtubule nucleation in Drosophila. Methods in Cell Biology. 67: 141-8. PMID 11550465 DOI: 10.1016/S0091-679X(01)67010-9 |
0.357 |
|
2001 |
Ota N, Agard DA. Enzyme specificity under dynamic control II: Principal component analysis of alpha-lytic protease using global and local solvent boundary conditions. Protein Science : a Publication of the Protein Society. 10: 1403-14. PMID 11420442 DOI: 10.1110/Ps.800101 |
0.311 |
|
2001 |
Marshall WF, Marko JF, Agard DA, Sedat JW. Chromosome elasticity and mitotic polar ejection force measured in living Drosophila embryos by four-dimensional microscopy-based motion analysis. Current Biology : Cb. 11: 569-78. PMID 11369201 DOI: 10.1016/S0960-9822(01)00180-4 |
0.667 |
|
2001 |
Moritz M, Agard DA. Gamma-tubulin complexes and microtubule nucleation. Current Opinion in Structural Biology. 11: 174-81. PMID 11297925 DOI: 10.1016/S0959-440X(00)00187-1 |
0.32 |
|
2001 |
Kam Z, Hanser B, Gustafsson MG, Agard DA, Sedat JW. Computational adaptive optics for live three-dimensional biological imaging. Proceedings of the National Academy of Sciences of the United States of America. 98: 3790-5. PMID 11274396 DOI: 10.1073/Pnas.071275698 |
0.785 |
|
2001 |
Hanser BM, Gustafsson MGL, Agard DA, Sedat JW. Phase retrieval of widefield microscopy point spread functions Proceedings of Spie - the International Society For Optical Engineering. 4261: 60-68. DOI: 10.1117/12.424520 |
0.768 |
|
2000 |
Moritz M, Braunfeld MB, Guénebaut V, Heuser J, Agard DA. Structure of the gamma-tubulin ring complex: a template for microtubule nucleation. Nature Cell Biology. 2: 365-70. PMID 10854328 DOI: 10.1038/35014058 |
0.347 |
|
2000 |
Bass HW, Riera-Lizarazu O, Ananiev EV, Bordoli SJ, Rines HW, Phillips RL, Sedat JW, Agard DA, Cande WZ. Evidence for the coincident initiation of homolog pairing and synapsis during the telomere-clustering (bouquet) stage of meiotic prophase. Journal of Cell Science. 113: 1033-42. PMID 10683151 |
0.521 |
|
2000 |
Gustafsson MGL, Agard DA, Sedat JW. Doubling the lateral resolution of wide-field fluorescence microscopy using structured illumination Proceedings of Spie - the International Society For Optical Engineering. 3919: 141-150. |
0.691 |
|
1999 |
Cunningham EL, Jaswal SS, Sohl JL, Agard DA. Kinetic stability as a mechanism for protease longevity. Proceedings of the National Academy of Sciences of the United States of America. 96: 11008-14. PMID 10500115 DOI: 10.1073/Pnas.96.20.11008 |
0.79 |
|
1999 |
Gustafsson MG, Agard DA, Sedat JW. I5M: 3D widefield light microscopy with better than 100 nm axial resolution. Journal of Microscopy. 195: 10-6. PMID 10444297 DOI: 10.1046/J.1365-2818.1999.00576.X |
0.554 |
|
1998 |
Sauter NK, Mau T, Rader SD, Agard DA. Structure of alpha-lytic protease complexed with its pro region. Nature Structural Biology. 5: 945-50. PMID 9808037 DOI: 10.1038/2919 |
0.348 |
|
1998 |
Sohl JL, Jaswal SS, Agard DA. Unfolded conformations of alpha-lytic protease are more stable than its native state. Nature. 395: 817-9. PMID 9796818 DOI: 10.1038/27470 |
0.596 |
|
1998 |
Davis JH, Agard DA. Relationship between enzyme specificity and the backbone dynamics of free and inhibited alpha-lytic protease. Biochemistry. 37: 7696-707. PMID 9601029 DOI: 10.1021/Bi972963P |
0.31 |
|
1998 |
Fung JC, Marshall WF, Dernburg A, Agard DA, Sedat JW. Homologous chromosome pairing in Drosophila melanogaster proceeds through multiple independent initiations. The Journal of Cell Biology. 141: 5-20. PMID 9531544 DOI: 10.1083/Jcb.141.1.5 |
0.664 |
|
1997 |
Han KF, Sedat JW, Agard DA. Practical image restoration of thick biological specimens using multiple focus levels in transmission electron microscopy. Journal of Structural Biology. 120: 237-44. PMID 9441929 DOI: 10.1006/Jsbi.1997.3914 |
0.576 |
|
1997 |
Marshall WF, Straight A, Marko JF, Swedlow J, Dernburg A, Belmont A, Murray AW, Agard DA, Sedat JW. Interphase chromosomes undergo constrained diffusional motion in living cells. Current Biology : Cb. 7: 930-9. PMID 9382846 DOI: 10.1016/S0960-9822(06)00412-X |
0.785 |
|
1997 |
Davis JH, Agard DA, Handel TM, Basus VJ. Alterations in chemical shifts and exchange broadening upon peptide boronic acid inhibitor binding to alpha-lytic protease. Journal of Biomolecular Nmr. 10: 21-7. PMID 9335113 DOI: 10.1023/A:1018314808361 |
0.338 |
|
1997 |
Rader SD, Agard DA. Conformational substates in enzyme mechanism: the 120 K structure of alpha-lytic protease at 1.5 A resolution. Protein Science : a Publication of the Protein Society. 6: 1375-86. PMID 9232638 DOI: 10.1002/Pro.5560060701 |
0.329 |
|
1997 |
Bass HW, Marshall WF, Sedat JW, Agard DA, Cande WZ. Telomeres cluster de novo before the initiation of synapsis: a three-dimensional spatial analysis of telomere positions before and during meiotic prophase. The Journal of Cell Biology. 137: 5-18. PMID 9105032 DOI: 10.1083/Jcb.137.1.5 |
0.773 |
|
1997 |
Fung JC, Kane L, Smith SD, Sedat JW, Agard DA, Spontak RJ. Phase behavior of complex diblock copolymer blends: A transmission electron microscopy study Materials Science Forum. 239: 179-184. DOI: 10.4028/Www.Scientific.Net/Msf.239-241.179 |
0.538 |
|
1997 |
Laurer JH, Hajduk DA, Fung JC, Sedat JW, Smith SD, Gruner SM, Agard DA, Spontak RJ. Microstructural analysis of a cubic bicontinuous morphology in a neat SIS triblock copolymer Macromolecules. 30: 3938-3941. DOI: 10.1021/Ma970449L |
0.498 |
|
1997 |
Laurer JH, Fung JC, Sedat JW, Smith SD, Samseth J, Mortensen K, Agard DA, Spontak RJ. From micelles to randomly connected, bilayered membranes in dilute block copolymer blends Langmuir. 13: 2177-2180. DOI: 10.1021/La9608876 |
0.547 |
|
1997 |
Agard DA, Braunfeld MB, Chen H, McQuitty R, Sedat J. Approaches for High Resolution Cryo-Electron Tomography of Biological Specimens Microscopy and Microanalysis. 3: 1111-1112. DOI: 10.1017/S1431927600012447 |
0.541 |
|
1997 |
Gustafsson MGL, Agard DA, Sedat JW. Sub-100nm Axial Resolution in 3D Widefield Optical Microscopy Using Two Opposing Objective Lenses Microscopy and Microanalysis. 3: 801-802. DOI: 10.1017/S1431927600010898 |
0.528 |
|
1997 |
Agard DA, Guenbaut V, Moritz M, Braunfeld MB, Zhang G, Sedat JW. Structure of Centrosomes and Chromosomes Through IVEM Tomography Microscopy and Microanalysis. 3: 223-224. DOI: 10.1017/S143192760000800X |
0.554 |
|
1997 |
Sedat J, Marshall W, Dernburg A, Fung J, Agard D. New Insights Into the Three-Dimensional Structure of the Nucleus and Chromosomes Microscopy and Microanalysis. 3: 213-214. DOI: 10.1017/S1431927600007959 |
0.562 |
|
1997 |
Hiraoka Y, Agard DA, Sedat JW. Spatial arrangement of homologous chromosomes during anaphase in early embryos of Drosophila melanogaster studied by three-dimensional fluorescence microscopy Bioimaging. 5: 183-193. DOI: 10.1002/1361-6374(199712)5:4<183::Aid-Bio2>3.3.Co;2-1 |
0.553 |
|
1997 |
Kam Z, Agard DA, Sedat JW. Three-dimensional microscopy in thick biological samples: A fresh approach for adjusting focus and correcting spherical aberration Bioimaging. 5: 40-49. DOI: 10.1002/1361-6374(199703)5:1<40::Aid-Bio4>3.3.Co;2-N |
0.564 |
|
1996 |
Paddy MR, Saumweber H, Agard DA, Sedat JW. Time-resolved, in vivo studies of mitotic spindle formation and nuclear lamina breakdown in Drosophila early embryos. Journal of Cell Science. 109: 591-607. PMID 8907705 |
0.553 |
|
1996 |
Han KF, Gubbens AJ, Sedat JW, Agard DA. Optimal strategies for imaging thick biological specimens: exit wavefront reconstruction and energy-filtered imaging. Journal of Microscopy. 183: 124-32. PMID 8805824 DOI: 10.1046/J.1365-2818.1996.810640.X |
0.556 |
|
1996 |
Marshall WF, Dernburg AF, Harmon B, Agard DA, Sedat JW. Specific interactions of chromatin with the nuclear envelope: positional determination within the nucleus in Drosophila melanogaster. Molecular Biology of the Cell. 7: 825-42. PMID 8744953 DOI: 10.1091/Mbc.7.5.825 |
0.787 |
|
1996 |
Fung JC, Liu W, de Ruijter WJ, Chen H, Abbey CK, Sedat JW, Agard DA. Toward fully automated high-resolution electron tomography. Journal of Structural Biology. 116: 181-9. PMID 8742742 DOI: 10.1006/Jsbi.1996.0029 |
0.552 |
|
1996 |
Chen H, Hughes DD, Chan TA, Sedat JW, Agard DA. IVE (Image Visualization Environment): a software platform for all three-dimensional microscopy applications. Journal of Structural Biology. 116: 56-60. PMID 8742723 DOI: 10.1006/Jsbi.1996.0010 |
0.542 |
|
1996 |
Dernburg AF, Broman KW, Fung JC, Marshall WF, Philips J, Agard DA, Sedat JW. Perturbation of nuclear architecture by long-distance chromosome interactions. Cell. 85: 745-59. PMID 8646782 DOI: 10.1016/S0092-8674(00)81240-4 |
0.657 |
|
1996 |
Scalettar BA, Swedlow JR, Sedat JW, Agard DA. Dispersion, aberration and deconvolution in multi-wavelength fluorescence images. Journal of Microscopy. 182: 50-60. PMID 8632447 DOI: 10.1046/J.1365-2818.1996.122402.X |
0.576 |
|
1996 |
Spontak RJ, Fung JC, Braunfeld MB, Sedat JW, Agard DA, Ashraf A, Smith SD. Architecture-induced phase immiscibility in a diblock/multiblock copolymer blend Macromolecules. 29: 2850-2856. DOI: 10.1021/Ma9515691 |
0.52 |
|
1996 |
Spontak RJ, Fung JC, Braunfeld MB, Sedat JW, Agard DA, Kane L, Smith SD, Satkowski MM, Ashraf A, Hajduk DA, Grüner SM. Phase behavior of ordered diblock copolymer blends: Effect of compositional heterogeneity Macromolecules. 29: 4494-4507. DOI: 10.1021/Ma9515689 |
0.548 |
|
1996 |
Gustafsson MG, Agard DA, Sedat JW. 3D widefield microscopy with two objective lenses: experimental verification of improved axial resolution Proceedings of Spie - the International Society For Optical Engineering. 2655: 62-66. |
0.665 |
|
1996 |
Marshall WF, Agard DA, Sedat JW. Chromosome mechanics in vivo: quantitative analysis of nonrigid 3D chromosome motion in Drosophila embryos Proceedings of Spie - the International Society For Optical Engineering. 2678: 142-150. |
0.611 |
|
1995 |
Moritz M, Braunfeld MB, Sedat JW, Alberts B, Agard DA. Microtubule nucleation by gamma-tubulin-containing rings in the centrosome. Nature. 378: 638-40. PMID 8524401 DOI: 10.1038/378638A0 |
0.579 |
|
1995 |
Han KF, Sedat JW, Agard DA. Mechanism of image formation for thick biological specimens: exit wavefront reconstruction and electron energy-loss spectroscopic imaging. Journal of Microscopy. 178: 107-19. PMID 7783184 DOI: 10.1111/J.1365-2818.1995.Tb03586.X |
0.565 |
|
1995 |
Moritz M, Braunfeld MB, Fung JC, Sedat JW, Alberts BM, Agard DA. Three-dimensional structural characterization of centrosomes from early Drosophila embryos. The Journal of Cell Biology. 130: 1149-59. PMID 7657699 DOI: 10.1083/Jcb.130.5.1149 |
0.59 |
|
1995 |
Mace JE, Wilk BJ, Agard DA. Functional linkage between the active site of alpha-lytic protease and distant regions of structure: scanning alanine mutagenesis of a surface loop affects activity and substrate specificity. Journal of Molecular Biology. 251: 116-34. PMID 7643381 DOI: 10.1006/Jmbi.1995.0420 |
0.304 |
|
1995 |
Urata Y, Parmelee SJ, Agard DA, Sedat JW. A three-dimensional structural dissection of Drosophila polytene chromosomes. The Journal of Cell Biology. 131: 279-95. PMID 7593159 DOI: 10.1083/Jcb.131.2.279 |
0.547 |
|
1995 |
Mace JE, Agard DA. Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity. Journal of Molecular Biology. 254: 720-36. PMID 7500345 DOI: 10.1006/Jmbi.1995.0650 |
0.302 |
|
1995 |
Gustafsson MG, Agard DA, Sedat JW. Sevenfold improvement of axial resolution in 3D wide-field microscopy using two objective-lenses Proceedings of Spie - the International Society For Optical Engineering. 2412: 147-156. |
0.665 |
|
1995 |
Marshall WF, Agard DA, Sedat JW. Quantitative analysis of chromosome motion in Drosophila melanogaster Proceedings of Spie - the International Society For Optical Engineering. 2412: 33-42. |
0.602 |
|
1994 |
Horowitz RA, Agard DA, Sedat JW, Woodcock CL. The three-dimensional architecture of chromatin in situ: electron tomography reveals fibers composed of a continuously variable zig-zag nucleosomal ribbon. The Journal of Cell Biology. 125: 1-10. PMID 8138564 DOI: 10.1083/Jcb.125.1.1 |
0.558 |
|
1994 |
Dawe RK, Sedat JW, Agard DA, Cande WZ. Meiotic chromosome pairing in maize is associated with a novel chromatin organization. Cell. 76: 901-12. PMID 8124724 DOI: 10.1016/0092-8674(94)90364-6 |
0.543 |
|
1994 |
Braunfeld MB, Koster AJ, Sedat JW, Agard DA. Cryo automated electron tomography: towards high-resolution reconstructions of plastic-embedded structures. Journal of Microscopy. 174: 75-84. PMID 8051698 DOI: 10.1111/J.1365-2818.1994.Tb03451.X |
0.548 |
|
1994 |
Baker D, Agard DA. Kinetics versus thermodynamics in protein folding. Biochemistry. 33: 7505-9. PMID 8011615 DOI: 10.1021/Bi00190A002 |
0.441 |
|
1994 |
Baker D, Agard DA. Influenza hemagglutinin: kinetic control of protein function. Structure (London, England : 1993). 2: 907-10. PMID 7866741 DOI: 10.1016/S0969-2126(94)00091-3 |
0.377 |
|
1994 |
Braunfeld MB, Moritz M, Alberts BM, Sedat JW, Agard DA. Three-dimensional reconstruction of isolated centrosomes by automated electron tomography Proceedings - Annual Meeting, Microscopy Society of America. 310-311. |
0.477 |
|
1993 |
Baker D, Krukowski AE, Agard DA. Uniqueness and the ab initio phase problem in macromolecular crystallography. Acta Crystallographica. Section D, Biological Crystallography. 49: 186-92. PMID 15299560 DOI: 10.1107/S0907444992008801 |
0.374 |
|
1993 |
Bystroff C, Baker D, Fletterick RJ, Agard DA. PRISM: application to the solution of two protein structures. Acta Crystallographica. Section D, Biological Crystallography. 49: 440-8. PMID 15299503 DOI: 10.1107/S0907444993004020 |
0.687 |
|
1993 |
Baker D, Bystroff C, Fletterick RJ, Agard DA. PRISM: topologically constrained phased refinement for macromolecular crystallography. Acta Crystallographica. Section D, Biological Crystallography. 49: 429-39. PMID 15299502 DOI: 10.1107/S0907444993004032 |
0.665 |
|
1993 |
Wilson C, Gregoret LM, Agard DA. Modeling side-chain conformation for homologous proteins using an energy-based rotamer search. Journal of Molecular Biology. 229: 996-1006. PMID 8445659 DOI: 10.1006/Jmbi.1993.1100 |
0.334 |
|
1993 |
Hiraoka Y, Dernburg AF, Parmelee SJ, Rykowski MC, Agard DA, Sedat JW. The onset of homologous chromosome pairing during Drosophila melanogaster embryogenesis. The Journal of Cell Biology. 120: 591-600. PMID 8425892 DOI: 10.1083/Jcb.120.3.591 |
0.557 |
|
1993 |
Swedlow JR, Sedat JW, Agard DA. Multiple chromosomal populations of topoisomerase II detected in vivo by time-lapse, three-dimensional wide-field microscopy. Cell. 73: 97-108. PMID 8384932 DOI: 10.1016/0092-8674(93)90163-K |
0.555 |
|
1993 |
Swedlow JR, Agard DA, Sedat JW. Chromosome structure inside the nucleus. Current Opinion in Cell Biology. 5: 412-6. PMID 8352957 DOI: 10.1016/0955-0674(93)90005-B |
0.584 |
|
1993 |
Baker D, Shiau AK, Agard DA. The role of pro regions in protein folding. Current Opinion in Cell Biology. 5: 966-70. PMID 8129949 DOI: 10.1016/0955-0674(93)90078-5 |
0.421 |
|
1993 |
Baker D, Bystroff C, Krukowski A, Wilson C, Agard D. Connectivity and the phase problem in macromolecular crystallography Acta Crystallographica Section a Foundations of Crystallography. 49: c50-c50. DOI: 10.1107/S0108767378098566 |
0.623 |
|
1993 |
Kam Z, Jones MO, Chen H, Agard DA, Sedat JW. Design and construction of an optimal illumination system for quantitative wide‐field multi‐dimensional microscopy Bioimaging. 1: 71-81. DOI: 10.1002/1361-6374(199306)1:2<71::Aid-Bio2>3.3.Co;2-R |
0.513 |
|
1993 |
Braunfeld MB, Koster AJ, Sedat JW, Agard DA. Properties and dose dependence of embedding media for cryo-automated electron tomography Proceedings - Annual Meeting, Microscopy Society of America. 436-437. |
0.466 |
|
1993 |
Koster AJ, Chen H, Clyborne W, Sedat JW, Agard DA. Design and performance of instrumentation for automated single-tilt-axis electron tomography Proceedings - Annual Meeting, Microscopy Society of America. 448-449. |
0.471 |
|
1992 |
Baker D, Silen JL, Agard DA. Protease pro region required for folding is a potent inhibitor of the mature enzyme. Proteins. 12: 339-44. PMID 1579568 DOI: 10.1002/Prot.340120406 |
0.431 |
|
1992 |
Baker D, Sohl JL, Agard DA. A protein-folding reaction under kinetic control. Nature. 356: 263-5. PMID 1552947 DOI: 10.1038/356263A0 |
0.408 |
|
1992 |
Koster AJ, Chen H, Sedat JW, Agard DA. Automated microscopy for electron tomography. Ultramicroscopy. 46: 207-27. PMID 1481272 DOI: 10.1016/0304-3991(92)90016-D |
0.554 |
|
1992 |
Paddy MR, Agard DA, Sedat JW. An extended view of nuclear lamin structure, function, and dynamics. Seminars in Cell Biology. 3: 255-66. PMID 1421171 DOI: 10.1016/1043-4682(92)90027-S |
0.577 |
|
1991 |
Wilson C, Wardell MR, Weisgraber KH, Mahley RW, Agard DA. Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E. Science (New York, N.Y.). 252: 1817-22. PMID 2063194 DOI: 10.1126/Science.2063194 |
0.313 |
|
1991 |
Bone R, Fujishige A, Kettner CA, Agard DA. Structural basis for broad specificity in alpha-lytic protease mutants. Biochemistry. 30: 10388-98. PMID 1931963 DOI: 10.1021/Bi00107A005 |
0.346 |
|
1991 |
Kam Z, Minden JS, Agard DA, Sedat JW, Leptin M. Drosophila gastrulation: analysis of cell shape changes in living embryos by three-dimensional fluorescence microscopy. Development (Cambridge, England). 112: 365-70. PMID 1794308 |
0.496 |
|
1991 |
Bone R, Agard DA. Mutational remodeling of enzyme specificity. Methods in Enzymology. 202: 643-71. PMID 1784192 DOI: 10.1016/0076-6879(91)02030-D |
0.341 |
|
1991 |
Hiraoka Y, Swedlow JR, Paddy MR, Agard DA, Sedat JW. Three-dimensional multiple-wavelength fluorescence microscopy for the structural analysis of biological phenomena. Seminars in Cell Biology. 2: 153-65. PMID 1720334 |
0.569 |
|
1991 |
HIRAOKA Y, CHEN H, SEDAT JW, AGARD DA. Three-dimensional fluorescence microscopy for the analysis of spatial arrangement of chromosomes. Acta Histochemica Et Cytochemica. 24: 357-365. DOI: 10.1267/Ahc.24.357 |
0.566 |
|
1991 |
Paddy MR, Swedlow JR, Hiraoka Y, Sedat JW, Agard DA. Time-resolved, multi-wavelength 3-D fluorescence microscopy of nuclear structures Scanning. 13: I2. |
0.51 |
|
1990 |
Hiraoka Y, Sedat JW, Agard DA. Determination of three-dimensional imaging properties of a light microscope system. Partial confocal behavior in epifluorescence microscopy. Biophysical Journal. 57: 325-33. PMID 2317554 DOI: 10.1016/S0006-3495(90)82534-0 |
0.572 |
|
1990 |
Paddy MR, Belmont AS, Saumweber H, Agard DA, Sedat JW. Interphase nuclear envelope lamins form a discontinuous network that interacts with only a fraction of the chromatin in the nuclear periphery. Cell. 62: 89-106. PMID 2194675 DOI: 10.1016/0092-8674(90)90243-8 |
0.683 |
|
1990 |
Hiraoka Y, Agard DA, Sedat JW. Temporal and spatial coordination of chromosome movement, spindle formation, and nuclear envelope breakdown during prometaphase in Drosophila melanogaster embryos. The Journal of Cell Biology. 111: 2815-28. PMID 2125300 DOI: 10.1083/Jcb.111.6.2815 |
0.568 |
|
1990 |
Koshy M, Agard DA, Sedat JW. Solution of Toeplitz systems for the restoration of 3-D optical sectioning microscopy data Proceedings of Spie - the International Society For Optical Engineering. 1205: 64-71. |
0.467 |
|
1989 |
Bone R, Silen JL, Agard DA. Structural plasticity broadens the specificity of an engineered protease. Nature. 339: 191-5. PMID 2716847 DOI: 10.1038/339191A0 |
0.307 |
|
1989 |
Aikens RS, Agard DA, Sedat JW. Solid-state imagers for microscopy. Methods in Cell Biology. 29: 291-313. PMID 2643764 DOI: 10.1016/S0091-679X(08)60199-5 |
0.551 |
|
1989 |
Hiraoka Y, Minden JS, Swedlow JR, Sedat JW, Agard DA. Focal points for chromosome condensation and decondensation revealed by three-dimensional in vivo time-lapse microscopy. Nature. 342: 293-6. PMID 2509947 DOI: 10.1038/342293A0 |
0.565 |
|
1989 |
Silen JL, Agard DA. The alpha-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo. Nature. 341: 462-4. PMID 2507926 DOI: 10.1038/341462A0 |
0.319 |
|
1989 |
Minden JS, Agard DA, Sedat JW, Alberts BM. Direct cell lineage analysis in Drosophila melanogaster by time-lapse, three-dimensional optical microscopy of living embryos. The Journal of Cell Biology. 109: 505-16. PMID 2503522 DOI: 10.1083/Jcb.109.2.505 |
0.554 |
|
1989 |
Shaw PJ, Agard DA, Hiraoka Y, Sedat JW. Tilted view reconstruction in optical microscopy. Three-dimensional reconstruction of Drosophila melanogaster embryo nuclei. Biophysical Journal. 55: 101-10. PMID 2495031 DOI: 10.1016/S0006-3495(89)82783-3 |
0.574 |
|
1989 |
Agard DA, Hiraoka Y, Shaw P, Sedat JW. Fluorescence microscopy in three dimensions. Methods in Cell Biology. 30: 353-77. PMID 2494418 DOI: 10.1016/S0091-679X(08)60986-3 |
0.578 |
|
1989 |
Belmont AS, Braunfeld MB, Sedat JW, Agard DA. Large-scale chromatin structural domains within mitotic and interphase chromosomes in vivo and in vitro. Chromosoma. 98: 129-43. PMID 2476279 DOI: 10.1007/Bf00291049 |
0.694 |
|
1989 |
Chen H, Sedat JW, Agard DA. Software and hardware for 3-d gray level image analysis and quantization Proceedings of Spie - the International Society For Optical Engineering. 1161: 31-41. DOI: 10.1117/12.962685 |
0.476 |
|
1989 |
Agard DA, Hiraoka Y, Sedat JW. Three-dimensional microscopy: Image processing for high resolution subcellular imaging Proceedings of Spie - the International Society For Optical Engineering. 1161: 24-30. DOI: 10.1117/12.962684 |
0.503 |
|
1989 |
Agard DA, Hiraoka Y, Shaw P, Sedat JW. Chapter 13 Fluorescence Microscopy in Three Dimensions Methods in Cell Biology. 30: 353-374,374a,375-377. DOI: 10.1016/S0091-679X(08)60986-3 |
0.477 |
|
1989 |
Agard D, Belmont A, Hiroka Y, Paddy M, Sedat J. Structure and function relationships—The diploid nucleus of Cell Differentiation and Development. 27: 107. DOI: 10.1016/0922-3371(89)90339-0 |
0.689 |
|
1988 |
Agard DA, Hiraoka Y, Sedat JW. Three-dimensional light microscopy of diploid Drosophila chromosomes. Cell Motility and the Cytoskeleton. 10: 18-27. PMID 3141069 DOI: 10.1002/Cm.970100106 |
0.589 |
|
1988 |
Rykowski MC, Parmelee SJ, Agard DA, Sedat JW. Precise determination of the molecular limits of a polytene chromosome band: regulatory sequences for the Notch gene are in the interband. Cell. 54: 461-72. PMID 3135939 DOI: 10.1016/0092-8674(88)90067-0 |
0.554 |
|
1988 |
Spontak RJ, Williams MC, Agard DA. Three-dimensional study of cylindrical morphology in a styrene-butadiene-styrene block copolymer Polymer. 29: 387-395. DOI: 10.1016/0032-3861(88)90354-0 |
0.306 |
|
1987 |
Hiraoka Y, Sedat JW, Agard DA. The use of a charge-coupled device for quantitative optical microscopy of biological structures. Science (New York, N.Y.). 238: 36-41. PMID 3116667 DOI: 10.1126/Science.3116667 |
0.598 |
|
1987 |
Belmont AS, Sedat JW, Agard DA. A three-dimensional approach to mitotic chromosome structure: evidence for a complex hierarchical organization. The Journal of Cell Biology. 105: 77-92. PMID 3112167 DOI: 10.1083/Jcb.105.1.77 |
0.707 |
|
1985 |
Thomas GJ, Agard DA. Quantitative analysis of nucleic acids, proteins, and viruses by Raman band deconvolution. Biophysical Journal. 46: 763-8. PMID 6083811 DOI: 10.1016/S0006-3495(84)84074-6 |
0.311 |
|
1984 |
Gruenbaum Y, Hochstrasser M, Mathog D, Saumweber H, Agard DA, Sedat JW. Spatial organization of the Drosophila nucleus: a three-dimensional cytogenetic study. Journal of Cell Science. Supplement. 1: 223-34. PMID 6442295 DOI: 10.1242/Jcs.1984.Supplement_1.14 |
0.689 |
|
1983 |
Agard DA, Sedat JW. Three-dimensional architecture of a polytene nucleus. Nature. 302: 676-81. PMID 6403872 DOI: 10.1038/302676A0 |
0.571 |
|
1982 |
Agard DA, Stroud RM. Linking regions between helices in bacteriorhodopsin revealed. Biophysical Journal. 37: 589-602. PMID 7074187 |
0.458 |
|
1982 |
Agard DA, Stroud RM. α-Bungaratoxin structure revealed by a rapid method for averaging electron density of non-crystallographically translationally related molecules Acta Crystallographica Section A. 38: 186-194. DOI: 10.1107/S0567739482000436 |
0.504 |
|
1981 |
Agard DA, Steinberg RA, Stroud RM. Quantitative analysis of electrophoretograms: a mathematical approach to super-resolution. Analytical Biochemistry. 111: 257-68. PMID 7247021 DOI: 10.1016/0003-2697(81)90562-5 |
0.438 |
|
1980 |
Agard DA, Sedat JW. Three-dimensional analysis of biological specimens utilizing image processing techniques Proceedings of Spie - the International Society For Optical Engineering. 264: 110-117. DOI: 10.1117/12.959792 |
0.491 |
|
1979 |
Stroud RM, Agard DA. Structure determination of asymmetric membrane profiles using an iterative Fourier method. Biophysical Journal. 25: 495-512. PMID 318062 DOI: 10.1016/S0006-3495(79)85319-9 |
0.446 |
|
1977 |
Ross MJ, Klymkowsky MW, Agard DA, Stroud RM. Structural studies of a membrane-bound acetylcholine receptor from Torpedo californica. Journal of Molecular Biology. 116: 635-59. PMID 563472 DOI: 10.1016/0022-2836(77)90264-9 |
0.646 |
|
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