| Year |
Citation |
Score |
| 2023 |
Rossi MA, Pozhidaeva AK, Clerico EM, Petridis C, Gierasch LM. New insights into the structure and function of the complex between the Escherichia coli Hsp70, DnaK, and its nucleotide-exchange factor, GrpE. The Journal of Biological Chemistry. 300: 105574. PMID 38110031 DOI: 10.1016/j.jbc.2023.105574 |
0.313 |
|
| 2023 |
Guay KP, Ke H, Canniff NP, George GT, Eyles SJ, Mariappan M, Contessa JN, Gershenson A, Gierasch LM, Hebert DN. ER chaperones use a protein folding and quality control glyco-code. Molecular Cell. PMID 38052210 DOI: 10.1016/j.molcel.2023.11.006 |
0.665 |
|
| 2023 |
Kaur U, Kihn KC, Ke H, Kuo W, Gierasch LM, Hebert DN, Wintrode PL, Deredge D, Gershenson A. The conformational landscape of a serpin N-terminal subdomain facilitates folding and in-cell quality control. Biorxiv : the Preprint Server For Biology. PMID 37163105 DOI: 10.1101/2023.04.24.537978 |
0.322 |
|
| 2022 |
Nordquist EB, Clerico EM, Chen J, Gierasch LM. Computationally-Aided Modeling of Hsp70-Client Interactions: Past, Present, and Future. The Journal of Physical Chemistry. B. PMID 36040440 DOI: 10.1021/acs.jpcb.2c03806 |
0.322 |
|
| 2022 |
Olds N, Clerico EM, Gierasch LM. Investigating the Determinants of Substrate Binding Orientation within the E. coli Hsp70 Chaperone Protein. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. PMID 35555549 DOI: 10.1096/fasebj.2022.36.S1.R3275 |
0.39 |
|
| 2021 |
Nordquist EB, English CA, Clerico EM, Sherman W, Gierasch LM, Chen J. Physics-based modeling provides predictive understanding of selectively promiscuous substrate binding by Hsp70 chaperones. Plos Computational Biology. 17: e1009567. PMID 34735438 DOI: 10.1371/journal.pcbi.1009567 |
0.329 |
|
| 2021 |
Clerico EM, Pozhidaeva AK, Jansen RM, Özden C, Tilitsky JM, Gierasch LM. Selective promiscuity in the binding of Hsp70 to an unfolded protein. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 34625496 DOI: 10.1073/pnas.2016962118 |
0.337 |
|
| 2020 |
Jansen RM, Clerico EM, Ozden C, Gierasch LM. Deducing the Origin of Hsp70 Binding Selectivity by Structural Study The Faseb Journal. 34: 1-1. DOI: 10.1096/Fasebj.2020.34.S1.04504 |
0.339 |
|
| 2019 |
Adams BM, Ke H, Gierasch LM, Gershenson A, Hebert DN. Proper secretion of the serpin antithrombin relies strictly on thiol-dependent quality control. The Journal of Biological Chemistry. PMID 31662433 DOI: 10.1074/Jbc.Ra119.010450 |
0.348 |
|
| 2019 |
Clerico EM, Meng W, Pozhidaeva A, Bhasne K, Petridis C, Gierasch LM. Hsp70 molecular chaperones: multifunctional allosteric holding and unfolding machines. The Biochemical Journal. 476: 1653-1677. PMID 31201219 DOI: 10.1042/Bcj20170380 |
0.448 |
|
| 2019 |
Pobre KFR, Powers DL, Ghosh K, Gierasch LM, Powers ET. Kinetic vs. Thermodynamic Control of Mutational Effects on Protein Homeostasis: A Perspective from Computational Modeling and Experiment. Protein Science : a Publication of the Protein Society. PMID 31074892 DOI: 10.1002/Pro.3639 |
0.39 |
|
| 2018 |
Mayer MP, Gierasch LM. Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones. The Journal of Biological Chemistry. PMID 30455352 DOI: 10.1074/Jbc.Rev118.002810 |
0.452 |
|
| 2018 |
Meng W, Clerico EM, McArthur N, Gierasch LM. Allosteric landscapes of eukaryotic cytoplasmic Hsp70s are shaped by evolutionary tuning of key interfaces. Proceedings of the National Academy of Sciences of the United States of America. 115: 11970-11975. PMID 30397123 DOI: 10.1073/Pnas.1811105115 |
0.44 |
|
| 2018 |
Thakur AK, Meng W, Gierasch LM. Local and non-local topological information in the denatured state ensemble of a β-barrel protein. Protein Science : a Publication of the Protein Society. PMID 30252171 DOI: 10.1002/Pro.3516 |
0.418 |
|
| 2018 |
Smock RG, Blackburn ME, Gierasch LM. Correction: Conserved, disordered C terminus of DnaK enhances cellular survival upon stress and DnaK chaperone activity. The Journal of Biological Chemistry. 293: 14295. PMID 30217867 DOI: 10.1074/jbc.AAC118.005458 |
0.666 |
|
| 2017 |
English CA, Sherman W, Meng W, Gierasch LM. The Hsp70 interdomain linker is a dynamic switch that enables allosteric communication between two structured domains. The Journal of Biological Chemistry. PMID 28754691 DOI: 10.1074/Jbc.M117.789313 |
0.453 |
|
| 2017 |
Lai AL, Clerico EM, Blackburn ME, Patel NA, Robinson CV, Borbat PP, Freed JH, Gierasch LM. Key features of an Hsp70 chaperone allosteric landscape revealed by ion mobility native mass spectrometry and double electron-electron resonance. The Journal of Biological Chemistry. PMID 28428246 DOI: 10.1074/Jbc.M116.770404 |
0.411 |
|
| 2017 |
Hingorani KS, Metcalf MC, Deming DT, Garman SC, Powers ET, Gierasch LM. Ligand-promoted protein folding by biased kinetic partitioning. Nature Chemical Biology. PMID 28218913 DOI: 10.1038/Nchembio.2303 |
0.431 |
|
| 2017 |
Kuo W, Kaur U, Deredge D, Kilcoyne CJ, Clerico EM, Wintrode PL, Gierasch LM, Gershenson A. Folding in Pieces Biophysical Journal. 112: 167a. DOI: 10.1016/J.Bpj.2016.11.921 |
0.404 |
|
| 2016 |
Hebert DN, Clerico EM, Gierasch LM. Division of Labor: ER-Resident BiP Co-Chaperones Match Substrates to Fates Based on Specific Binding Sequences. Molecular Cell. 63: 721-3. PMID 27588598 DOI: 10.1016/J.Molcel.2016.08.017 |
0.409 |
|
| 2016 |
Chandrasekhar K, Ke H, Wang N, Goodwin T, Gierasch LM, Gershenson A, Hebert DN. Cellular folding pathway of a metastable serpin. Proceedings of the National Academy of Sciences of the United States of America. PMID 27222580 DOI: 10.1073/Pnas.1603386113 |
0.432 |
|
| 2015 |
Hong J, Gierasch LM, Liu Z. Its preferential interactions with biopolymers account for diverse observed effects of trehalose. Biophysical Journal. 109: 144-53. PMID 26153711 DOI: 10.1016/J.Bpj.2015.05.037 |
0.376 |
|
| 2015 |
Zhuravleva A, Gierasch LM. Substrate-binding domain conformational dynamics mediate Hsp70 allostery. Proceedings of the National Academy of Sciences of the United States of America. 112: E2865-73. PMID 26038563 DOI: 10.1073/Pnas.1506692112 |
0.425 |
|
| 2015 |
Cho Y, Zhang X, Pobre KF, Liu Y, Powers DL, Kelly JW, Gierasch LM, Powers ET. Individual and collective contributions of chaperoning and degradation to protein homeostasis in E. coli. Cell Reports. 11: 321-33. PMID 25843722 DOI: 10.1016/J.Celrep.2015.03.018 |
0.365 |
|
| 2015 |
Clerico EM, Tilitsky JM, Meng W, Gierasch LM. How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions. Journal of Molecular Biology. 427: 1575-88. PMID 25683596 DOI: 10.1016/J.Jmb.2015.02.004 |
0.432 |
|
| 2015 |
Lai AL, Blackburn M, Clerico EM, Borbat P, Gierasch LM, Freed JH. Characterizing the Conformational Ensembles of the E. coli Hsp70, DnaK Reveals the Role of the Intermediate State Biophysical Journal. 108: 502a-503a. DOI: 10.1016/J.Bpj.2014.11.2752 |
0.382 |
|
| 2014 |
Gershenson A, Gierasch LM, Pastore A, Radford SE. Energy landscapes of functional proteins are inherently risky. Nature Chemical Biology. 10: 884-91. PMID 25325699 DOI: 10.1038/Nchembio.1670 |
0.364 |
|
| 2014 |
Theillet FX, Binolfi A, Frembgen-Kesner T, Hingorani K, Sarkar M, Kyne C, Li C, Crowley PB, Gierasch L, Pielak GJ, Elcock AH, Gershenson A, Selenko P. Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs). Chemical Reviews. 114: 6661-714. PMID 24901537 DOI: 10.1021/Cr400695P |
0.362 |
|
| 2014 |
General IJ, Liu Y, Blackburn ME, Mao W, Gierasch LM, Bahar I. ATPase subdomain IA is a mediator of interdomain allostery in Hsp70 molecular chaperones. Plos Computational Biology. 10: e1003624. PMID 24831085 DOI: 10.1371/Journal.Pcbi.1003624 |
0.458 |
|
| 2014 |
Hingorani KS, Gierasch LM. Comparing protein folding in vitro and in vivo: foldability meets the fitness challenge. Current Opinion in Structural Biology. 24: 81-90. PMID 24434632 DOI: 10.1016/J.Sbi.2013.11.007 |
0.429 |
|
| 2013 |
Ferrolino MC, Zhuravleva A, Budyak IL, Krishnan B, Gierasch LM. Delicate balance between functionally required flexibility and aggregation risk in a β-rich protein. Biochemistry. 52: 8843-54. PMID 24236614 DOI: 10.1021/Bi4013462 |
0.816 |
|
| 2013 |
Budyak IL, Zhuravleva A, Gierasch LM. The Role of Aromatic-Aromatic Interactions in Strand-Strand Stabilization of β-Sheets. Journal of Molecular Biology. 425: 3522-35. PMID 23810905 DOI: 10.1016/J.Jmb.2013.06.030 |
0.424 |
|
| 2013 |
Budyak IL, Krishnan B, Marcelino-Cruz AM, Ferrolino MC, Zhuravleva A, Gierasch LM. Early folding events protect aggregation-prone regions of a β-rich protein. Structure (London, England : 1993). 21: 476-85. PMID 23454187 DOI: 10.1016/J.Str.2013.01.013 |
0.812 |
|
| 2013 |
Gierasch LM. Moving the Protein Folding Problem from the Test Tube to the Cell Biophysical Journal. 104: 6a. DOI: 10.1016/J.Bpj.2012.11.058 |
0.447 |
|
| 2012 |
Zhuravleva A, Clerico EM, Gierasch LM. An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones. Cell. 151: 1296-307. PMID 23217711 DOI: 10.1016/J.Cell.2012.11.002 |
0.41 |
|
| 2012 |
Powers ET, Powers DL, Gierasch LM. FoldEco: a model for proteostasis in E. coli. Cell Reports. 1: 265-76. PMID 22509487 DOI: 10.1016/J.Celrep.2012.02.011 |
0.347 |
|
| 2012 |
Maki JL, Krishnan B, Gierasch LM. Using a low denaturant model to explore the conformational features of translocation-active SecA. Biochemistry. 51: 1369-79. PMID 22304380 DOI: 10.1021/Bi201793E |
0.76 |
|
| 2012 |
Horwich AL, Buchner J, Smock RG, Gierasch LM, Saibil HR. Chaperones and protein folding Comprehensive Biophysics. 3: 212-237. DOI: 10.1016/B978-0-12-374920-8.00313-1 |
0.744 |
|
| 2011 |
Wang Q, Zhuravleva A, Gierasch LM. Exploring weak, transient protein--protein interactions in crowded in vivo environments by in-cell nuclear magnetic resonance spectroscopy. Biochemistry. 50: 9225-36. PMID 21942871 DOI: 10.1021/Bi201287E |
0.404 |
|
| 2011 |
Smock RG, Blackburn ME, Gierasch LM. Conserved, disordered C terminus of DnaK enhances cellular survival upon stress and DnaK in vitro chaperone activity. The Journal of Biological Chemistry. 286: 31821-9. PMID 21768118 DOI: 10.1074/Jbc.M111.265835 |
0.765 |
|
| 2011 |
Zhuravleva A, Gierasch LM. Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones. Proceedings of the National Academy of Sciences of the United States of America. 108: 6987-92. PMID 21482798 DOI: 10.1073/Pnas.1014448108 |
0.439 |
|
| 2011 |
Gierasch LM. A career pathway in protein folding: from model peptides to postreductionist protein science. Protein Science : a Publication of the Protein Society. 20: 783-90. PMID 21404361 DOI: 10.1002/Pro.615 |
0.409 |
|
| 2011 |
Krishnan B, Gierasch LM. Dynamic local unfolding in the serpin α-1 antitrypsin provides a mechanism for loop insertion and polymerization. Nature Structural & Molecular Biology. 18: 222-6. PMID 21258324 DOI: 10.1038/Nsmb.1976 |
0.34 |
|
| 2011 |
Gierasch LM. How one bad protein spoils the barrel: structural details of β2-microglobulin amyloidogenicity. Molecular Cell. 41: 129-31. PMID 21255721 DOI: 10.1016/J.Molcel.2011.01.003 |
0.346 |
|
| 2011 |
Gershenson A, Gierasch LM. Protein folding in the cell: challenges and progress. Current Opinion in Structural Biology. 21: 32-41. PMID 21112769 DOI: 10.1016/J.Sbi.2010.11.001 |
0.382 |
|
| 2011 |
Zhuravleva A, Gierasch L. Backbone 1H, 13C, and 15N chemical shift assignments for the nucleotide-binding domain of E.coli DnaK in the nucleotide-free state Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr17209 |
0.334 |
|
| 2010 |
Smock RG, Rivoire O, Russ WP, Swain JF, Leibler S, Ranganathan R, Gierasch LM. An interdomain sector mediating allostery in Hsp70 molecular chaperones. Molecular Systems Biology. 6: 414. PMID 20865007 DOI: 10.1038/Msb.2010.65 |
0.776 |
|
| 2010 |
Liu Y, Gierasch LM, Bahar I. Role of Hsp70 ATPase domain intrinsic dynamics and sequence evolution in enabling its functional interactions with NEFs. Plos Computational Biology. 6. PMID 20862304 DOI: 10.1371/Journal.Pcbi.1000931 |
0.387 |
|
| 2010 |
Hong J, Gierasch LM. Macromolecular crowding remodels the energy landscape of a protein by favoring a more compact unfolded state. Journal of the American Chemical Society. 132: 10445-52. PMID 20662522 DOI: 10.1021/Ja103166Y |
0.407 |
|
| 2010 |
Clerico EM, Zhuravleva A, Smock RG, Gierasch LM. Segmental isotopic labeling of the Hsp70 molecular chaperone DnaK using expressed protein ligation. Biopolymers. 94: 742-52. PMID 20564022 DOI: 10.1002/Bip.21426 |
0.752 |
|
| 2010 |
Ghosh RP, Nikitina T, Horowitz-Scherer RA, Gierasch LM, Uversky VN, Hite K, Hansen JC, Woodcock CL. Unique physical properties and interactions of the domains of methylated DNA binding protein 2. Biochemistry. 49: 4395-410. PMID 20405910 DOI: 10.1021/Bi9019753 |
0.408 |
|
| 2010 |
Eyles SJ, Gierasch LM. Nature's molecular sponges: small heat shock proteins grow into their chaperone roles. Proceedings of the National Academy of Sciences of the United States of America. 107: 2727-8. PMID 20133678 DOI: 10.1073/Pnas.0915160107 |
0.712 |
|
| 2009 |
Gierasch LM, Gershenson A. Post-reductionist protein science, or putting Humpty Dumpty back together again. Nature Chemical Biology. 5: 774-7. PMID 19841622 DOI: 10.1038/Nchembio.241 |
0.393 |
|
| 2009 |
Smock RG, Gierasch LM. Sending signals dynamically. Science (New York, N.Y.). 324: 198-203. PMID 19359576 DOI: 10.1126/Science.1169377 |
0.72 |
|
| 2009 |
Clérico EM, Szyma?ska A, Gierasch LM. Exploring the interactions between signal sequences and E. coli SRP by two distinct and complementary crosslinking methods. Biopolymers. 92: 201-11. PMID 19280642 DOI: 10.1002/Bip.21181 |
0.418 |
|
| 2009 |
Ignatova Z, Gierasch LM. A method for direct measurement of protein stability in vivo. Methods in Molecular Biology (Clifton, N.J.). 490: 165-78. PMID 19157083 DOI: 10.1007/978-1-59745-367-7_7 |
0.451 |
|
| 2008 |
Ignatova Z, Gierasch LM. Chapter 3: A fluorescent window into protein folding and aggregation in cells. Methods in Cell Biology. 89: 59-70. PMID 19118672 DOI: 10.1016/S0091-679X(08)00603-1 |
0.467 |
|
| 2008 |
Krishnan B, Gierasch LM. Cross-strand split tetra-Cys motifs as structure sensors in a beta-sheet protein. Chemistry & Biology. 15: 1104-15. PMID 18940670 DOI: 10.1016/J.Chembiol.2008.09.006 |
0.471 |
|
| 2008 |
Ghosh RP, Horowitz-Scherer RA, Nikitina T, Gierasch LM, Woodcock CL. Rett syndrome-causing mutations in human MeCP2 result in diverse structural changes that impact folding and DNA interactions. The Journal of Biological Chemistry. 283: 20523-34. PMID 18499664 DOI: 10.1074/Jbc.M803021200 |
0.336 |
|
| 2008 |
Hinz J, Gierasch LM, Ignatova Z. Orthogonal cross-seeding: an approach to explore protein aggregates in living cells. Biochemistry. 47: 4196-200. PMID 18330996 DOI: 10.1021/Bi800002J |
0.332 |
|
| 2008 |
Gierasch LM, Deber CM, Brodsky B. Celebrating the scientific legacy of Elkan R. Blout. Biopolymers. 89: 323. PMID 18307218 DOI: 10.1002/Bip.20965 |
0.456 |
|
| 2008 |
Marcelino AM, Gierasch LM. Roles of beta-turns in protein folding: from peptide models to protein engineering. Biopolymers. 89: 380-91. PMID 18275088 DOI: 10.1002/Bip.20960 |
0.82 |
|
| 2008 |
Clérico EM, Maki JL, Gierasch LM. Use of synthetic signal sequences to explore the protein export machinery. Biopolymers. 90: 307-19. PMID 17918185 DOI: 10.1002/Bip.20856 |
0.76 |
|
| 2007 |
Ignatova Z, Thakur AK, Wetzel R, Gierasch LM. In-cell aggregation of a polyglutamine-containing chimera is a multistep process initiated by the flanking sequence. The Journal of Biological Chemistry. 282: 36736-43. PMID 17942400 DOI: 10.1074/Jbc.M703682200 |
0.341 |
|
| 2007 |
Ignatova Z, Gierasch LM. Effects of osmolytes on protein folding and aggregation in cells. Methods in Enzymology. 428: 355-72. PMID 17875429 DOI: 10.1016/S0076-6879(07)28021-8 |
0.439 |
|
| 2007 |
Swain JF, Dinler G, Sivendran R, Montgomery DL, Stotz M, Gierasch LM. Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker. Molecular Cell. 26: 27-39. PMID 17434124 DOI: 10.1016/J.Molcel.2007.02.020 |
0.779 |
|
| 2007 |
Krishnan B, Szymanska A, Gierasch LM. Site-specific fluorescent labeling of poly-histidine sequences using a metal-chelating cysteine. Chemical Biology & Drug Design. 69: 31-40. PMID 17313455 DOI: 10.1111/J.1747-0285.2007.00463.X |
0.365 |
|
| 2007 |
Ignatova Z, Krishnan B, Bombardier JP, Marcelino AM, Hong J, Gierasch LM. From the test tube to the cell: exploring the folding and aggregation of a beta-clam protein. Biopolymers. 88: 157-63. PMID 17206628 DOI: 10.1002/Bip.20665 |
0.803 |
|
| 2006 |
Lin BR, Gierasch LM, Jiang C, Tai PC. Electrophysiological studies in Xenopus oocytes for the opening of Escherichia coli SecA-dependent protein-conducting channels. The Journal of Membrane Biology. 214: 103-13. PMID 17530158 DOI: 10.1007/S00232-006-0079-1 |
0.368 |
|
| 2006 |
Mainprize IL, Beniac DR, Falkovskaia E, Cleverley RM, Gierasch LM, Ottensmeyer FP, Andrews DW. The structure of Escherichia coli signal recognition particle revealed by scanning transmission electron microscopy. Molecular Biology of the Cell. 17: 5063-74. PMID 16987964 DOI: 10.1091/Mbc.E06-05-0384 |
0.756 |
|
| 2006 |
Ignatova Z, Gierasch LM. Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant. Proceedings of the National Academy of Sciences of the United States of America. 103: 13357-61. PMID 16899544 DOI: 10.1073/Pnas.0603772103 |
0.427 |
|
| 2006 |
Ignatova Z, Gierasch LM. Extended polyglutamine tracts cause aggregation and structural perturbation of an adjacent beta barrel protein. The Journal of Biological Chemistry. 281: 12959-67. PMID 16524881 DOI: 10.1074/Jbc.M511523200 |
0.432 |
|
| 2006 |
Marcelino AM, Smock RG, Gierasch LM. Evolutionary coupling of structural and functional sequence information in the intracellular lipid-binding protein family. Proteins. 63: 373-84. PMID 16477649 DOI: 10.1002/Prot.20860 |
0.788 |
|
| 2006 |
Swain JF, Gierasch LM. The changing landscape of protein allostery. Current Opinion in Structural Biology. 16: 102-8. PMID 16423525 DOI: 10.1016/J.Sbi.2006.01.003 |
0.447 |
|
| 2006 |
Swain JF, Schulz EG, Gierasch LM. Direct comparison of a stable isolated Hsp70 substrate-binding domain in the empty and substrate-bound states. The Journal of Biological Chemistry. 281: 1605-11. PMID 16275641 DOI: 10.1074/Jbc.M509356200 |
0.469 |
|
| 2006 |
Rotondi KS, Gierasch LM. Natural polypeptide scaffolds: beta-sheets, beta-turns, and beta-hairpins. Biopolymers. 84: 13-22. PMID 16235261 DOI: 10.1002/Bip.20390 |
0.784 |
|
| 2005 |
Smock RG, Gierasch LM. Finding the fittest fold: using the evolutionary record to design new proteins. Cell. 122: 832-4. PMID 16179253 DOI: 10.1016/J.Cell.2005.09.005 |
0.732 |
|
| 2005 |
Swain JF, Gierasch LM. First glimpses of a chaperonin-bound folding intermediate. Proceedings of the National Academy of Sciences of the United States of America. 102: 13715-6. PMID 16172384 DOI: 10.1073/Pnas.0506510102 |
0.434 |
|
| 2005 |
Chou YT, Gierasch LM. The conformation of a signal peptide bound by Escherichia coli preprotein translocase SecA. The Journal of Biological Chemistry. 280: 32753-60. PMID 16046390 DOI: 10.1074/Jbc.M507532200 |
0.622 |
|
| 2005 |
Sinha N, Grant CV, Rotondi KS, Feduik-Rotondi L, Gierasch LM, Opella SJ. Peptides and the development of double- and triple-resonance solid-state NMR of aligned samples. The Journal of Peptide Research : Official Journal of the American Peptide Society. 65: 605-20. PMID 15885119 DOI: 10.1111/J.1399-3011.2005.00262.X |
0.768 |
|
| 2005 |
Ignatova Z, Gierasch LM. Aggregation of a slow-folding mutant of a beta-clam protein proceeds through a monomeric nucleus. Biochemistry. 44: 7266-74. PMID 15882065 DOI: 10.1021/Bi047404E |
0.406 |
|
| 2005 |
Rotondi KS, Gierasch LM. A well-defined amphipathic conformation for the calcium-free cyclic lipopeptide antibiotic, daptomycin, in aqueous solution. Biopolymers. 80: 374-85. PMID 15815985 DOI: 10.1002/Bip.20238 |
0.792 |
|
| 2005 |
Deber CM, Gierasch LM. Editorial: The Murray Goodman memorial issue Biopolymers - Peptide Science Section. 80: 59-62. DOI: 10.1002/Bip.20255 |
0.453 |
|
| 2004 |
Fak JJ, Itkin A, Ciobanu DD, Lin EC, Song XJ, Chou YT, Gierasch LM, Hunt JF. Nucleotide exchange from the high-affinity ATP-binding site in SecA is the rate-limiting step in the ATPase cycle of the soluble enzyme and occurs through a specialized conformational state. Biochemistry. 43: 7307-27. PMID 15182175 DOI: 10.1021/Bi0357208 |
0.589 |
|
| 2004 |
Ignatova Z, Gierasch LM. Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling. Proceedings of the National Academy of Sciences of the United States of America. 101: 523-8. PMID 14701904 DOI: 10.1073/Pnas.0304533101 |
0.404 |
|
| 2004 |
Gunasekaran K, Hagler AT, Gierasch LM. Sequence and structural analysis of cellular retinoic acid-binding proteins reveals a network of conserved hydrophobic interactions. Proteins. 54: 179-94. PMID 14696180 DOI: 10.1002/Prot.10520 |
0.445 |
|
| 2003 |
Rotondi KS, Gierasch LM. Local sequence information in cellular retinoic acid-binding protein I: specific residue roles in beta-turns. Biopolymers. 71: 638-51. PMID 14991674 DOI: 10.1002/Bip.10592 |
0.816 |
|
| 2003 |
Kabani M, Kelley SS, Morrow MW, Montgomery DL, Sivendran R, Rose MD, Gierasch LM, Brodsky JL. Dependence of endoplasmic reticulum-associated degradation on the peptide binding domain and concentration of BiP. Molecular Biology of the Cell. 14: 3437-48. PMID 12925775 DOI: 10.1091/Mbc.E02-12-0847 |
0.794 |
|
| 2003 |
Rotondi KS, Gierasch LM. Role of local sequence in the folding of cellular retinoic abinding protein I: structural propensities of reverse turns. Biochemistry. 42: 7976-85. PMID 12834350 DOI: 10.1021/Bi034304K |
0.83 |
|
| 2003 |
Rotondi KS, Rotondi LF, Gierasch LM. Native structural propensity in cellular retinoic acid-binding protein I 64-88: the role of locally encoded structure in the folding of a beta-barrel protein. Biophysical Chemistry. 100: 421-36. PMID 12646381 DOI: 10.1016/S0301-4622(02)00296-X |
0.83 |
|
| 2003 |
Benach J, Chou YT, Fak JJ, Itkin A, Nicolae DD, Smith PC, Wittrock G, Floyd DL, Golsaz CM, Gierasch LM, Hunt JF. Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA. The Journal of Biological Chemistry. 278: 3628-38. PMID 12403785 DOI: 10.1074/Jbc.M205992200 |
0.65 |
|
| 2003 |
Gierasch LM, Deber CM. Editorial: In Memory of Arno F. Spatola Biopolymers - Peptide Science Section. 71: 601. DOI: 10.1002/Bip.10589 |
0.45 |
|
| 2002 |
Chou YT, Swain JF, Gierasch LM. Functionally significant mobile regions of Escherichia coli SecA ATPase identified by NMR. The Journal of Biological Chemistry. 277: 50985-90. PMID 12397065 DOI: 10.1074/Jbc.M209237200 |
0.631 |
|
| 2002 |
Cleverley RM, Gierasch LM. Mapping the signal sequence-binding site on SRP reveals a significant role for the NG domain. The Journal of Biological Chemistry. 277: 46763-8. PMID 12244111 DOI: 10.1074/Jbc.M207427200 |
0.778 |
|
| 2002 |
Gierasch LM. Caught in the act: how ATP binding triggers cooperative conformational changes in a molecular machine. Molecular Cell. 9: 3-5. PMID 11804578 DOI: 10.1016/S1097-2765(02)00432-X |
0.327 |
|
| 2001 |
Swain JF, Sivendran R, Gierasch LM. Defining the structure of the substrate-free state of the DnaK molecular chaperone. Biochemical Society Symposium. 69-82. PMID 11573348 DOI: 10.1042/Bss0680069 |
0.797 |
|
| 2001 |
Triplett TL, Sgrignoli AR, Gao FB, Yang YB, Tai PC, Gierasch LM. Functional signal peptides bind a soluble N-terminal fragment of SecA and inhibit its ATPase activity. The Journal of Biological Chemistry. 276: 19648-55. PMID 11279006 DOI: 10.1074/Jbc.M100098200 |
0.43 |
|
| 2001 |
Cleverley RM, Zheng N, Gierasch LM. The cost of exposing a hydrophobic loop and implications for the functional role of 4.5 S RNA in the Escherichia coli signal recognition particle. The Journal of Biological Chemistry. 276: 19327-31. PMID 11278844 DOI: 10.1074/Jbc.M011130200 |
0.8 |
|
| 2001 |
Gunasekaran K, Eyles SJ, Hagler AT, Gierasch LM. Keeping it in the family: folding studies of related proteins. Current Opinion in Structural Biology. 11: 83-93. PMID 11179896 DOI: 10.1016/S0959-440X(00)00173-1 |
0.727 |
|
| 2001 |
Swain JF, Gierasch LM. Signal peptides bind and aggregate RNA. An alternative explanation for GTPase inhibition in the signal recognition particle. The Journal of Biological Chemistry. 276: 12222-7. PMID 11148214 DOI: 10.1074/Jbc.M011128200 |
0.357 |
|
| 2000 |
Eyles SJ, Gierasch LM. Multiple roles of prolyl residues in structure and folding. Journal of Molecular Biology. 301: 737-47. PMID 10966780 DOI: 10.1006/Jmbi.2000.4002 |
0.745 |
|
| 2000 |
Krishnan VV, Sukumar M, Gierasch LM, Cosman M. Dynamics of cellular retinoic acid binding protein I on multiple time scales with implications for ligand binding. Biochemistry. 39: 9119-29. PMID 10924105 DOI: 10.1021/Bi000296L |
0.391 |
|
| 2000 |
Pellecchia M, Montgomery DL, Stevens SY, Vander Kooi CW, Feng HP, Gierasch LM, Zuiderweg ER. Structural insights into substrate binding by the molecular chaperone DnaK. Nature Structural Biology. 7: 298-303. PMID 10742174 DOI: 10.1038/74062 |
0.435 |
|
| 2000 |
Feltham JL, Gierasch LM. GroEL-substrate interactions: molding the fold, or folding the mold? Cell. 100: 193-6. PMID 10660042 DOI: 10.1016/S0092-8674(00)81557-3 |
0.435 |
|
| 2000 |
Eyles SJ, Speir JP, Kruppa GH, Gierasch LM, Kaltashov IA. Protein conformational stability probed by fourier transform ion cyclotron resonance mass spectrometry Journal of the American Chemical Society. 122: 495-500. DOI: 10.1021/Ja991149H |
0.682 |
|
| 1999 |
Eyles SJ, Dresch T, Gierasch LM, Kaltashov IA. Unfolding dynamics of a beta-sheet protein studied by mass spectrometry. Journal of Mass Spectrometry : Jms. 34: 1289-95. PMID 10587623 DOI: 10.1002/(Sici)1096-9888(199912)34:12<1289::Aid-Jms882>3.0.Co;2-U |
0.689 |
|
| 1999 |
Wang Z, Feng Hp, Landry SJ, Maxwell J, Gierasch LM. Basis of substrate binding by the chaperonin GroEL. Biochemistry. 38: 12537-46. PMID 10504222 DOI: 10.1021/Bi991070P |
0.458 |
|
| 1999 |
Montgomery DL, Morimoto RI, Gierasch LM. Mutations in the substrate binding domain of the Escherichia coli 70 kDa molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling. Journal of Molecular Biology. 286: 915-32. PMID 10024459 DOI: 10.1006/Jmbi.1998.2514 |
0.421 |
|
| 1999 |
Eyles SJ, Dresch T, Gierasch LM, Kaltashov IA. Unfolding dynamics of a β-sheet protein studied by mass spectrometry† Paper presented at 17th Informal Meeting on Mass Spectrometry, Fiera di Primiero, Italy, May 1999. Journal of Mass Spectrometry. 34: 1289. DOI: 10.1002/(Sici)1096-9888(199912)34:12<1289::Aid-Jms882>3.3.Co;2-L |
0.652 |
|
| 1998 |
Clark PL, Weston BF, Gierasch LM. Probing the folding pathway of a beta-clam protein with single-tryptophan constructs. Folding & Design. 3: 401-12. PMID 9806942 DOI: 10.1016/S1359-0278(98)00053-4 |
0.628 |
|
| 1998 |
Kibbey RG, Rizo J, Gierasch LM, Anderson RG. The LDL receptor clustering motif interacts with the clathrin terminal domain in a reverse turn conformation. The Journal of Cell Biology. 142: 59-67. PMID 9660863 DOI: 10.1083/Jcb.142.1.59 |
0.347 |
|
| 1998 |
Feng HP, Gierasch LM. Molecular chaperones: clamps for the Clps? Current Biology : Cb. 8: R464-7. PMID 9651675 DOI: 10.1016/S0960-9822(98)70294-5 |
0.429 |
|
| 1997 |
Zheng N, Gierasch LM. Domain interactions in E. coli SRP: stabilization of M domain by RNA is required for effective signal sequence modulation of NG domain. Molecular Cell. 1: 79-87. PMID 9659905 DOI: 10.1016/S1097-2765(00)80009-X |
0.551 |
|
| 1997 |
Clark PL, Liu ZP, Rizo J, Gierasch LM. Cavity formation before stable hydrogen bonding in the folding of a beta-clam protein. Nature Structural Biology. 4: 883-6. PMID 9360599 DOI: 10.1038/Nsb1197-883 |
0.573 |
|
| 1997 |
Sukumar M, Gierasch LM. Local interactions in a Schellman motif dictate interhelical arrangement in a protein fragment. Folding & Design. 2: 211-22. PMID 9269562 DOI: 10.1016/S1359-0278(97)00030-8 |
0.469 |
|
| 1997 |
Clark PL, Sukumar M, Liu ZP, Rizo J, Rotondi K, Gierasch LM. Folding of a predominantly beta sheet protein with a central cavity Faseb Journal. 11: A871. |
0.791 |
|
| 1996 |
Bechinger B, Gierasch LM, Montal M, Zasloff M, Opella SJ. Orientations of helical peptides in membrane bilayers by solid state NMR spectroscopy. Solid State Nuclear Magnetic Resonance. 7: 185-91. PMID 9050156 DOI: 10.1016/0926-2040(95)01224-9 |
0.341 |
|
| 1996 |
Zheng N, Gierasch LM. Signal sequences: the same yet different. Cell. 86: 849-52. PMID 8808619 DOI: 10.1016/S0092-8674(00)80159-2 |
0.479 |
|
| 1996 |
Clark PL, Liu ZP, Zhang J, Gierasch LM. Intrinsic tryptophans of CRABPI as probes of structure and folding. Protein Science : a Publication of the Protein Society. 5: 1108-17. PMID 8762142 DOI: 10.1002/Pro.5560050613 |
0.57 |
|
| 1996 |
Hunt JF, Weaver AJ, Landry SJ, Gierasch L, Deisenhofer J. The crystal structure of the GroES co-chaperonin at 2.8 A resolution. Nature. 379: 37-45. PMID 8538739 DOI: 10.1038/379037A0 |
0.326 |
|
| 1996 |
Rizo J, Sutton RB, Breslau J, Koerber SC, Porter J, Hagler AT, Rivier JE, Gierasch LM. A novel conformation in a highly potent, constrained gonadotropin-releasing hormone antagonist Journal of the American Chemical Society. 118: 970-976. DOI: 10.1021/Ja953207E |
0.317 |
|
| 1995 |
Sukumar M, Rizo J, Wall M, Dreyfus LA, Kupersztoch YM, Gierasch LM. The structure of Escherichia coli heat-stable enterotoxin b by nuclear magnetic resonance and circular dichroism. Protein Science : a Publication of the Protein Society. 4: 1718-29. PMID 8528070 DOI: 10.1002/Pro.5560040907 |
0.396 |
|
| 1994 |
Liu ZP, Rizo J, Gierasch LM. Equilibrium folding studies of cellular retinoic acid binding protein, a predominantly beta-sheet protein. Biochemistry. 33: 134-42. PMID 8286330 DOI: 10.1021/Bi00167A017 |
0.444 |
|
| 1994 |
Sankaram MB, Marsh D, Gierasch LM, Thompson TE. Reorganization of lipid domain structure in membranes by a transmembrane peptide: an ESR spin label study on the effect of the Escherichia coli outer membrane protein A signal peptide on the fluid lipid domain connectivity in binary mixtures of dimyristoyl phosphatidylcholine and distearoyl phosphatidylcholine. Biophysical Journal. 66: 1959-68. PMID 8075330 DOI: 10.1016/S0006-3495(94)80989-0 |
0.359 |
|
| 1994 |
Gierasch LM. Molecular chaperones. Panning for chaperone-binding peptides. Current Biology : Cb. 4: 173-4. PMID 7953525 DOI: 10.1016/S0960-9822(94)00042-4 |
0.412 |
|
| 1994 |
Landry SJ, Gierasch LM. Polypeptide interactions with molecular chaperones and their relationship to in vivo protein folding. Annual Review of Biophysics and Biomolecular Structure. 23: 645-69. PMID 7919795 DOI: 10.1146/Annurev.Bb.23.060194.003241 |
0.402 |
|
| 1994 |
Jones JD, Gierasch LM. Effect of charged residue substitutions on the thermodynamics of signal peptide-lipid interactions for the Escherichia coli LamB signal sequence. Biophysical Journal. 67: 1546-61. PMID 7819487 DOI: 10.1016/S0006-3495(94)80628-9 |
0.399 |
|
| 1994 |
Jones JD, Gierasch LM. Effect of charged residue substitutions on the membrane-interactive properties of signal sequences of the Escherichia coli LamB protein. Biophysical Journal. 67: 1534-45. PMID 7819486 DOI: 10.1016/S0006-3495(94)80627-7 |
0.413 |
|
| 1994 |
Rizo J, Liu ZP, Gierasch LM. 1H and 15N resonance assignments and secondary structure of cellular retinoic acid-binding protein with and without bound ligand. Journal of Biomolecular Nmr. 4: 741-60. PMID 7812151 DOI: 10.1007/Bf00398406 |
0.447 |
|
| 1993 |
Rizo J, Blanco FJ, Kobe B, Bruch MD, Gierasch LM. Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments. Biochemistry. 32: 4881-94. PMID 8387821 DOI: 10.1021/Bi00069A025 |
0.375 |
|
| 1993 |
Wang Z, Jones JD, Rizo J, Gierasch LM. Membrane-bound conformation of a signal peptide: a transferred nuclear Overhauser effect analysis. Biochemistry. 32: 13991-9. PMID 8268177 DOI: 10.1021/Bi00213A032 |
0.396 |
|
| 1993 |
Stradley SJ, Rizo J, Gierasch LM. Conformation of a heptapeptide substrate bound to protein farnesyltransferase. Biochemistry. 32: 12586-90. PMID 8251476 DOI: 10.1021/Bi00210A006 |
0.454 |
|
| 1993 |
Miller JD, Wilhelm H, Gierasch L, Gilmore R, Walter P. GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation. Nature. 366: 351-4. PMID 8247130 DOI: 10.1038/366351A0 |
0.43 |
|
| 1993 |
Bienstock RJ, Rizo J, Koerber SC, Rivier JE, Hagler AT, Gierasch LM. Conformational analysis of a highly potent dicyclic gonadotropin-releasing hormone antagonist by nuclear magnetic resonance and molecular dynamics. Journal of Medicinal Chemistry. 36: 3265-73. PMID 8230116 DOI: 10.1021/Jm00074A006 |
0.377 |
|
| 1993 |
Landry SJ, Zeilstra-Ryalls J, Fayet O, Georgopoulos C, Gierasch LM. Characterization of a functionally important mobile domain of GroES. Nature. 364: 255-8. PMID 8100614 DOI: 10.1038/364255A0 |
0.404 |
|
| 1992 |
Rizo J, Gierasch LM. Constrained peptides: models of bioactive peptides and protein substructures. Annual Review of Biochemistry. 61: 387-418. PMID 1497316 DOI: 10.1146/Annurev.Bi.61.070192.002131 |
0.4 |
|
| 1992 |
Bruch MD, Rizo J, Gierasch LM. Impact of a micellar environment on the conformations of two cyclic pentapeptides. Biopolymers. 32: 1741-54. PMID 1472656 DOI: 10.1002/Bip.360321215 |
0.358 |
|
| 1992 |
Liu ZP, Gierasch LM. Combined use of molecular dynamics simulations and NMR to explore peptide bond isomerization and multiple intramolecular hydrogen-bonding possibilities in a cyclic pentapeptide, cyclo(Gly-Pro-D-Phe-Gly-Val). Biopolymers. 32: 1727-39. PMID 1472655 DOI: 10.1002/Bip.360321214 |
0.348 |
|
| 1992 |
Stroup AN, Rockwell AL, Gierasch LM. Solution conformations of two flexible cyclic pentapeptides: cyclo(Gly-Pro-D-Phe-Gly-Ala) and cyclo(Gly-Pro-D-Phe-Gly-Val). Biopolymers. 32: 1713-25. PMID 1472654 DOI: 10.1002/Bip.360321213 |
0.349 |
|
| 1992 |
Zhang J, Liu ZP, Jones TA, Gierasch LM, Sambrook JF. Mutating the charged residues in the binding pocket of cellular retinoic acid-binding protein simultaneously reduces its binding affinity to retinoic acid and increases its thermostability. Proteins. 13: 87-99. PMID 1377826 DOI: 10.1002/Prot.340130202 |
0.405 |
|
| 1992 |
Landry SJ, Jordan R, McMacken R, Gierasch LM. Different conformations for the same polypeptide bound to chaperones DnaK and GroEL. Nature. 355: 455-7. PMID 1346469 DOI: 10.1038/355455A0 |
0.432 |
|
| 1992 |
Rizo J, Koerber SC, Bienstock RJ, Rivier J, Gierasch LM, Hagler AT. Conformational analysis of a highly potent, constrained gonadotropin-releasing hormone antagonist. 2. Molecular dynamics simulations Journal of the American Chemical Society. 114: 2860-2871. DOI: 10.1021/Ja00034A016 |
0.322 |
|
| 1992 |
Rizo J, Koerber SC, Bienstock RJ, Rivier J, Hagler AT, Gierasch LM. Conformational analysis of a highly potent, constrained gonadotropin-releasing hormone antagonist. 1. Nuclear magnetic resonance Journal of the American Chemical Society. 114: 2852-2859. DOI: 10.1021/Ja00034A015 |
0.33 |
|
| 1991 |
McKnight CJ, Stradley SJ, Jones JD, Gierasch LM. Conformational and membrane-binding properties of a signal sequence are largely unaltered by its adjacent mature region. Proceedings of the National Academy of Sciences of the United States of America. 88: 5799-803. PMID 2062859 DOI: 10.1073/Pnas.88.13.5799 |
0.426 |
|
| 1991 |
Reiss Y, Stradley SJ, Gierasch LM, Brown MS, Goldstein JL. Sequence requirement for peptide recognition by rat brain p21ras protein farnesyltransferase. Proceedings of the National Academy of Sciences of the United States of America. 88: 732-6. PMID 1992464 DOI: 10.1073/Pnas.88.3.732 |
0.379 |
|
| 1991 |
Hoyt DW, Gierasch LM. Hydrophobic content and lipid interactions of wild-type and mutant OmpA signal peptides correlate with their in vivo function. Biochemistry. 30: 10155-63. PMID 1931946 DOI: 10.1021/Bi00106A012 |
0.368 |
|
| 1991 |
Bruch MD, Dhingra MM, Gierasch LM. Side chain-backbone hydrogen bonding contributes to helix stability in peptides derived from an alpha-helical region of carboxypeptidase A. Proteins. 10: 130-9. PMID 1896426 DOI: 10.1002/Prot.340100206 |
0.378 |
|
| 1991 |
Landry SJ, Gierasch LM. Recognition of nascent polypeptides for targeting and folding. Trends in Biochemical Sciences. 16: 159-63. PMID 1877092 DOI: 10.1016/0968-0004(91)90060-9 |
0.303 |
|
| 1991 |
Bansal A, Gierasch LM. The NPXY internalization signal of the LDL receptor adopts a reverse-turn conformation. Cell. 67: 1195-201. PMID 1760844 DOI: 10.1016/0092-8674(91)90295-A |
0.379 |
|
| 1991 |
Landry SJ, Gierasch LM. The chaperonin GroEL binds a polypeptide in an alpha-helical conformation. Biochemistry. 30: 7359-62. PMID 1677268 DOI: 10.1021/Bi00244A001 |
0.444 |
|
| 1990 |
Stradley SJ, Rizo J, Bruch MD, Stroup AN, Gierasch LM. Cyclic pentapeptides as models for reverse turns: Determination of the equilibrium distribution between type I and type II conformations of Pro-Asn and Pro-Ala β-turns Biopolymers. 29: 263-287. PMID 2328290 DOI: 10.1002/Bip.360290130 |
0.393 |
|
| 1990 |
Jones JD, McKnight CJ, Gierasch LM. Biophysical studies of signal peptides: Implications for signal sequence functions and the involvement of lipid in protein export Journal of Bioenergetics and Biomembranes. 22: 213-232. PMID 2202718 DOI: 10.1007/Bf00763166 |
0.388 |
|
| 1990 |
Stroup AN, Gierasch LM. Reduced tendency to form a β turn in peptides from the P22 tailspike protein correlates with a temperature-sensitive folding defect Biochemistry. 29: 9765-9771. PMID 2148688 DOI: 10.1021/Bi00494A002 |
0.415 |
|
| 1990 |
Struthers RS, Tanaka G, Koerber SC, Solmajer T, Baniak EL, Gierasch LM, Vale W, Rivier J, Hagler AT. Design of biologically active, conformationally constrained GnRH antagonists Proteins: Structure, Function and Genetics. 8: 295-304. PMID 2091022 DOI: 10.1002/Prot.340080403 |
0.375 |
|
| 1988 |
Schiksnis RA, Rockwell AL, Gierasch LM, Opella SJ. Detection of a structural interconversion in a peptide in solution with sensitivity-enhanced 15N chemical-exchange NMR spectroscopy Journal of Magnetic Resonance (1969). 79: 318-321. DOI: 10.1016/0022-2364(88)90223-5 |
0.304 |
|
| 1987 |
Baniak EL, Rivier JE, Struthers RS, Hagler AT, Gierasch LM. Nuclear magnetic resonance analysis and conformational characterization of a cyclic decapeptide antagonist of gonadotropin-releasing hormone Biochemistry. 26: 2642-2656. PMID 3300777 DOI: 10.1021/Bi00383A036 |
0.336 |
|
| 1987 |
Valentine KG, Rockwell AL, Gierasch LM, Opella SJ. 15N chemical-shift tensor of the imide nitrogen in the alanyl-prolyl peptide bond Journal of Magnetic Resonance (1969). 73: 519-523. DOI: 10.1016/0022-2364(87)90015-1 |
0.356 |
|
| 1986 |
Mueller L, Frey MH, Rockwell AL, Gierasch LM, Opella SJ. Dynamics of a hydrophobic peptide in membrane bilayers by solid-state nuclear magnetic resonance Biochemistry. 25: 557-561. PMID 3754152 DOI: 10.1021/Bi00351A007 |
0.312 |
|
| 1986 |
Briggs MS, Cornell DG, Dluhy RA, Gierasch LM. Conformations of signal peptides induced by lipids suggest initial steps in protein export Science. 233: 206-208. PMID 2941862 DOI: 10.1126/Science.2941862 |
0.423 |
|
| 1986 |
Spatola AF, Anwer MK, Rockwell AL, Gierasch LM. Compatibility of .beta.- and .gamma.-turn features with a peptide backbone modification: synthesis and conformational analysis of a model cyclic pseudopentapeptide Journal of the American Chemical Society. 108: 825-831. DOI: 10.1021/Ja00264A041 |
0.329 |
|
| 1986 |
Briggs MS, Gierasch LM. Molecular Mechanisms of Protein Secretion: The Role of the Signal Sequence Advances in Protein Chemistry. 38: 109-180. DOI: 10.1016/S0065-3233(08)60527-6 |
0.391 |
|
| 1985 |
Gierasch LM, Rockwell AL, Thompson KF, Briggs MS. Conformation-function relationships in hydrophobic peptides: interior turns and signal sequences. Biopolymers. 24: 117-35. PMID 3886031 DOI: 10.1002/Bip.360240111 |
0.412 |
|
| 1985 |
Briggs MS, Gierasch LM, Zlotnick A, Lear JD, DeGrado WF. In vivo function and membrane binding properties are correlated for Escherichia coli LamB signal peptides Science. 228: 1096-1099. PMID 3158076 DOI: 10.1126/Science.3158076 |
0.371 |
|
| 1985 |
Rose GD, Gierasch LM, Smith JA. Turns in peptides and proteins Advances in Protein Chemistry. 37: 1-109. PMID 2865874 DOI: 10.1016/S0065-3233(08)60063-7 |
0.311 |
|
| 1985 |
Bruch MD, Noggle JH, Gierasch LM. Conformational analysis of a cyclic pentapeptide by one-and two-dimensional nuclear overhauser effect spectroscopy Journal of the American Chemical Society. 107: 1400-1407. DOI: 10.1002/Chin.198529065 |
0.306 |
|
| 1984 |
Briggs MS, Gierasch LM. Exploring the conformational roles of signal sequences: Synthesis and conformational analysis of λ receptor protein wild-type and mutant signal peptides Biochemistry. 23: 3111-3114. PMID 6380582 DOI: 10.1021/Bi00309A001 |
0.411 |
|
| 1984 |
Thompson KF, Gierasch LM. Conformation of a peptide solubilizate in a reversed micelle water pool Journal of the American Chemical Society. 106: 3648-3652. DOI: 10.1002/Chin.198438078 |
0.311 |
|
| 1984 |
FLIPPEN-ANDERSON JL, GILARDI R, KARLE IL, FREY MH, OPELLA SJ, GIERASCH LM, GOODMAN M, MADISON V, DELANEY NG. ChemInform Abstract: CRYSTAL STRUCTURES, MOLECULAR CONFORMATIONS, INFRARED SPECTRA, AND CARBON-13 NMR SPECTRA OF METHYLPROLINE PEPTIDES IN THE SOLID STATE Chemischer Informationsdienst. 15. DOI: 10.1002/Chin.198405070 |
0.308 |
|
| 1983 |
Rose GD, Young WB, Gierasch LM. Interior turns in globular proteins Nature. 304: 654-657. PMID 6877386 DOI: 10.1038/304654A0 |
0.426 |
|
| 1983 |
Flippen-Anderson JL, Gilardi R, Karle IL, Frey MH, Opella SJ, Gierasch LM, Goodman M, Madison V, Delaney NG. Crystal structures, molecular conformations, infrared spectra, and carbon-13 NMR spectra of methylproline peptides in the solid state Journal of the American Chemical Society. 105: 6609-6614. DOI: 10.1021/Ja00360A011 |
0.305 |
|
| 1983 |
Gierasch LM, Lacy JE, Anderle G, Lalancette R, Mendelsohn R. Spectroscopic studies of a hydrophobic peptide in membranelike environments Biopolymers. 22: 381-385. DOI: 10.1002/Bip.360220149 |
0.353 |
|
| 1983 |
Spatola AF, Gierasch LM, Rockwell AL. Conformational comparison of cyclic peptide and pseudopeptide structures with intramolecular hydrogen bonding Biopolymers. 22: 147-151. DOI: 10.1002/Bip.360220123 |
0.303 |
|
| 1982 |
Gierasch LM, Lacy JE, Thompson KF, Rockwell AL, Watnick PI. Conformations of model peptides in membrane-mimetic environments. Biophysical Journal. 37: 275-84. PMID 7055624 DOI: 10.1016/S0006-3495(82)84676-6 |
0.337 |
|
| 1981 |
Gierasch LM, Deber CM, Madison V, Niu CH, Blout ER. Conformations of (X-L-Pro-Y)2 cyclic hexapeptides. Preferred beta-turn conformers and implications for beta turns in proteins. Biochemistry. 20: 4730-8. PMID 7295645 DOI: 10.1021/Bi00519A032 |
0.678 |
|
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