Year |
Citation |
Score |
2023 |
Nogales E, Kellogg E. Structure challenges in the multivalency of Tau-microtubule interactions. Cytoskeleton (Hoboken, N.J.). PMID 37702417 DOI: 10.1002/cm.21788 |
0.525 |
|
2023 |
Park JU, Petassi MT, Hsieh SC, Mehrotra E, Schuler G, Budhathoki J, Truong VH, Thyme SB, Ke A, Kellogg EH, Peters JE. Multiple adaptations underly co-option of a CRISPR surveillance complex for RNA-guided DNA transposition. Molecular Cell. 83: 1827-1838.e6. PMID 37267904 DOI: 10.1016/j.molcel.2023.05.005 |
0.641 |
|
2022 |
Park JU, Tsai AW, Chen TH, Peters JE, Kellogg EH. Mechanistic details of CRISPR-associated transposon recruitment and integration revealed by cryo-EM. Proceedings of the National Academy of Sciences of the United States of America. 119: e2202590119. PMID 35914146 DOI: 10.1073/pnas.2202590119 |
0.316 |
|
2020 |
Cianfrocco M, Kellogg EH. What Could Go Wrong? A Practical Guide to Single-Particle Cryo-EM: From Biochemistry to Atomic Models. Journal of Chemical Information and Modeling. PMID 32078321 DOI: 10.1021/Acs.Jcim.9B01178 |
0.681 |
|
2019 |
Ghanim GE, Kellogg EH, Nogales E, Rio DC. Structure of a P element transposase-DNA complex reveals unusual DNA structures and GTP-DNA contacts. Nature Structural & Molecular Biology. PMID 31659330 DOI: 10.2210/Pdb6Pe2/Pdb |
0.508 |
|
2019 |
Kellogg EH, Ghanim G, Nogales E, Rio DC. Towards a Mechanistic Understanding of P element Transposition Using Single-Particle Cryo-EM Microscopy and Microanalysis. 25: 1288-1289. DOI: 10.1017/S1431927619007177 |
0.459 |
|
2019 |
Kellogg EH, Ghanim G, Nogales E, Rio DC. Cryo-EM Structure of the P-Element Transposase Strand-Transfer Complex Biophysical Journal. 116: 504a. DOI: 10.1016/J.Bpj.2018.11.2720 |
0.508 |
|
2018 |
Kellogg EH, Hejab NMA, Poepsel S, Downing KH, DiMaio F, Nogales E. Near-atomic model of microtubule-tau interactions. Science (New York, N.Y.). PMID 29748322 DOI: 10.1126/Science.Aat1780 |
0.687 |
|
2017 |
Howes SC, Geyer EA, LaFrance B, Zhang R, Kellogg EH, Westermann S, Rice LM, Nogales E. Structural and functional differences between porcine brain and budding yeast microtubules. Cell Cycle (Georgetown, Tex.). 1-22. PMID 29278985 DOI: 10.1080/15384101.2017.1415680 |
0.629 |
|
2017 |
Howes SC, Geyer EA, LaFrance B, Zhang R, Kellogg EH, Westermann S, Rice LM, Nogales E. Structural differences between yeast and mammalian microtubules revealed by cryo-EM. The Journal of Cell Biology. PMID 28652389 DOI: 10.1083/Jcb.201612195 |
0.634 |
|
2017 |
Nogales E, Kellogg EH. Challenges and opportunities in the high-resolution cryo-EM visualization of microtubules and their binding partners. Current Opinion in Structural Biology. 46: 65-70. PMID 28628789 DOI: 10.1016/J.Sbi.2017.06.003 |
0.591 |
|
2017 |
Kellogg EH, Hejab NM, Howes S, Northcote P, Miller JH, Fernando Díaz J, Downing KH, Nogales E. Insights into the distinct mechanisms of action of taxane and non-taxane microtubule stabilizers from cryo-EM structures. Journal of Molecular Biology. PMID 28104363 DOI: 10.1016/J.Jmb.2017.01.001 |
0.711 |
|
2016 |
Kellogg EH, Howes S, Ti SC, Ramírez-Aportela E, Kapoor TM, Chacón P, Nogales E. Near-atomic cryo-EM structure of PRC1 bound to the microtubule. Proceedings of the National Academy of Sciences of the United States of America. PMID 27493215 DOI: 10.1073/Pnas.1609903113 |
0.589 |
|
2014 |
Alushin GM, Lander GC, Kellogg EH, Zhang R, Baker D, Nogales E. High-resolution microtubule structures reveal the structural transitions in αβ-tubulin upon GTP hydrolysis. Cell. 157: 1117-29. PMID 24855948 DOI: 10.1016/J.Cell.2014.03.053 |
0.754 |
|
2014 |
Zhang R, Alushin G, Kellogg E, Nogales E. 3.8 Angstrom Resolution Structure of Microtubule by Cryo-Em Biophysical Journal. 106: 442a. DOI: 10.1016/J.Bpj.2013.11.2492 |
0.756 |
|
2014 |
Kellogg EH, Alushin GM, Lander GC, Baker D, Nogales E. Studying the Structural Origins of Microtubule Dynamic Instability through Combining Computational Modeling and cryoEM Biophysical Journal. 106: 351a. DOI: 10.1016/J.Bpj.2013.11.1996 |
0.755 |
|
2013 |
Leaver-Fay A, O'Meara MJ, Tyka M, Jacak R, Song Y, Kellogg EH, Thompson J, Davis IW, Pache RA, Lyskov S, Gray JJ, Kortemme T, Richardson JS, Havranek JJ, Snoeyink J, et al. Scientific benchmarks for guiding macromolecular energy function improvement. Methods in Enzymology. 523: 109-43. PMID 23422428 DOI: 10.1016/B978-0-12-394292-0.00006-0 |
0.645 |
|
2012 |
Kellogg EH, Lange OF, Baker D. Evaluation and optimization of discrete state models of protein folding. The Journal of Physical Chemistry. B. 116: 11405-13. PMID 22958200 DOI: 10.1021/Jp3044303 |
0.447 |
|
2012 |
Liu Y, Kellogg E, Liang H. Canonical and micro-canonical analysis of folding of trpzip2: an all-atom replica exchange Monte Carlo simulation study. The Journal of Chemical Physics. 137: 045103. PMID 22852659 DOI: 10.1063/1.4738760 |
0.392 |
|
2011 |
Kellogg EH, Leaver-Fay A, Baker D. Role of conformational sampling in computing mutation-induced changes in protein structure and stability. Proteins. 79: 830-8. PMID 21287615 DOI: 10.1002/Prot.22921 |
0.713 |
|
2010 |
Fowler DM, Araya CL, Fleishman SJ, Kellogg EH, Stephany JJ, Baker D, Fields S. High-resolution mapping of protein sequence-function relationships. Nature Methods. 7: 741-6. PMID 20711194 DOI: 10.1038/Nmeth.1492 |
0.44 |
|
2010 |
Jung HS, Okegawa Y, Shih PM, Kellogg E, Abdel-Ghany SE, Pilon M, Sjölander K, Shikanai T, Niyogi KK. Arabidopsis thaliana PGR7 encodes a conserved chloroplast protein that is necessary for efficient photosynthetic electron transport. Plos One. 5: e11688. PMID 20657737 DOI: 10.1371/Journal.Pone.0011688 |
0.304 |
|
2010 |
Leung CC, Kellogg E, Kuhnert A, Hänel F, Baker D, Glover JN. Insights from the crystal structure of the sixth BRCT domain of topoisomerase IIbeta binding protein 1. Protein Science : a Publication of the Protein Society. 19: 162-7. PMID 19937654 DOI: 10.1002/Pro.290 |
0.441 |
|
2009 |
Raman S, Vernon R, Thompson J, Tyka M, Sadreyev R, Pei J, Kim D, Kellogg E, DiMaio F, Lange O, Kinch L, Sheffler W, Kim BH, Das R, Grishin NV, et al. Structure prediction for CASP8 with all-atom refinement using Rosetta. Proteins. 77: 89-99. PMID 19701941 DOI: 10.1002/Prot.22540 |
0.718 |
|
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