| Year |
Citation |
Score |
| 2019 |
Schmidt D, Boehm M, McClendon CL, Torella R, Gohlke H. Cosolvent-enhanced Sampling and Unbiased Identification of Cryptic Pockets Suitable for Structure-based Drug Design. Journal of Chemical Theory and Computation. PMID 30998331 DOI: 10.1021/Acs.Jctc.8B01295 |
0.479 |
|
| 2017 |
Pfleger C, Minges A, Boehm M, McClendon CL, Torella R, Gohlke H. Ensemble- and rigidity theory-based perturbation approach to analyze dynamic allostery. Journal of Chemical Theory and Computation. PMID 29112408 DOI: 10.1021/Acs.Jctc.7B00529 |
0.412 |
|
| 2017 |
Kim J, Ahuja LG, Chao FA, Xia Y, McClendon CL, Kornev AP, Taylor SS, Veglia G. A dynamic hydrophobic core orchestrates allostery in protein kinases. Science Advances. 3: e1600663. PMID 28435869 DOI: 10.1126/Sciadv.1600663 |
0.474 |
|
| 2017 |
Ahuja LG, Kornev AP, McClendon CL, Veglia G, Taylor SS. Mutation of a kinase allosteric node uncouples dynamics linked to phosphotransfer. Proceedings of the National Academy of Sciences of the United States of America. PMID 28115705 DOI: 10.1073/Pnas.1620667114 |
0.502 |
|
| 2016 |
Meharena HS, Fan X, Ahuja LG, Keshwani MM, McClendon CL, Chen AM, Adams JA, Taylor SS. Decoding the Interactions Regulating the Active State Mechanics of Eukaryotic Protein Kinases. Plos Biology. 14: e2000127. PMID 27902690 DOI: 10.1371/Journal.Pbio.2000127 |
0.484 |
|
| 2015 |
Meng H, McClendon CL, Dai Z, Li K, Zhang X, He S, Shang E, Liu Y, Lai L. Discovery of Novel 15-Lipoxygenase Activators To Shift the Human Arachidonic Acid Metabolic Network toward Inflammation Resolution. Journal of Medicinal Chemistry. PMID 26290290 DOI: 10.1021/Acs.Jmedchem.5B01011 |
0.372 |
|
| 2015 |
Hasnain S, McClendon CL, Tremont Hsu M, Jacobson MP, Bandyopadhyay P. A Computational Model for E. coli Cytoplasm: Diffusion and Hydrodynamics Biophysical Journal. 108: 116a-117a. DOI: 10.1016/J.Bpj.2014.11.654 |
0.317 |
|
| 2014 |
Srivastava AK, McDonald LR, Cembran A, Kim J, Masterson LR, McClendon CL, Taylor SS, Veglia G. Synchronous opening and closing motions are essential for cAMP-dependent protein kinase A signaling. Structure (London, England : 1993). 22: 1735-43. PMID 25458836 DOI: 10.1016/J.Str.2014.09.010 |
0.489 |
|
| 2014 |
McClendon CL, Kornev AP, Gilson MK, Taylor SS. Dynamic architecture of a protein kinase. Proceedings of the National Academy of Sciences of the United States of America. 111: E4623-31. PMID 25319261 DOI: 10.1073/Pnas.1418402111 |
0.459 |
|
| 2014 |
Hasnain S, McClendon CL, Hsu MT, Jacobson MP, Bandyopadhyay P. A new coarse-grained model for E. coli cytoplasm: accurate calculation of the diffusion coefficient of proteins and observation of anomalous diffusion. Plos One. 9: e106466. PMID 25180859 DOI: 10.1371/Journal.Pone.0106466 |
0.307 |
|
| 2013 |
Aglietti RA, Floor SN, McClendon CL, Jacobson MP, Gross JD. Active site conformational dynamics are coupled to catalysis in the mRNA decapping enzyme Dcp2. Structure (London, England : 1993). 21: 1571-80. PMID 23911090 DOI: 10.1016/J.Str.2013.06.021 |
0.471 |
|
| 2013 |
Rapp C, Snow S, Laufer T, McClendon CL. The role of tyrosine sulfation in the dimerization of the CXCR4:SDF-1 complex. Protein Science : a Publication of the Protein Society. 22: 1025-36. PMID 23740770 DOI: 10.1002/Pro.2288 |
0.387 |
|
| 2013 |
Wan X, Ma Y, McClendon CL, Huang LJ, Huang N. Ab initio modeling and experimental assessment of Janus Kinase 2 (JAK2) kinase-pseudokinase complex structure. Plos Computational Biology. 9: e1003022. PMID 23592968 DOI: 10.1371/Journal.Pcbi.1003022 |
0.5 |
|
| 2013 |
Rapp C, Klerman H, Levine E, McClendon CL. Hydrogen bond strengths in phosphorylated and sulfated amino acid residues. Plos One. 8: e57804. PMID 23472106 DOI: 10.1371/Journal.Pone.0057804 |
0.401 |
|
| 2013 |
Datta D, McClendon CL, Jacobson MP, Wells JA. Substrate and inhibitor-induced dimerization and cooperativity in caspase-1 but not caspase-3. The Journal of Biological Chemistry. 288: 9971-81. PMID 23386603 DOI: 10.1074/Jbc.M112.426460 |
0.573 |
|
| 2012 |
McClendon CL, Hua L, Barreiro A, Jacobson MP. Comparing Conformational Ensembles Using the Kullback-Leibler Divergence Expansion. Journal of Chemical Theory and Computation. 8: 2115-2126. PMID 23316121 DOI: 10.1021/Ct300008D |
0.38 |
|
| 2012 |
Cembran A, Masterson LR, McClendon CL, Taylor SS, Gao J, Veglia G. Conformational equilibrium of N-myristoylated cAMP-dependent protein kinase A by molecular dynamics simulations. Biochemistry. 51: 10186-96. PMID 23205665 DOI: 10.1021/Bi301279F |
0.495 |
|
| 2011 |
Sadowsky JD, Burlingame MA, Wolan DW, McClendon CL, Jacobson MP, Wells JA. Turning a protein kinase on or off from a single allosteric site via disulfide trapping. Proceedings of the National Academy of Sciences of the United States of America. 108: 6056-61. PMID 21430264 DOI: 10.1073/Pnas.1102376108 |
0.606 |
|
| 2010 |
Morcos F, Chatterjee S, McClendon CL, Brenner PR, López-Rendón R, Zintsmaster J, Ercsey-Ravasz M, Sweet CR, Jacobson MP, Peng JW, Izaguirre JA. Modeling conformational ensembles of slow functional motions in Pin1-WW. Plos Computational Biology. 6: e1001015. PMID 21152000 DOI: 10.1371/Journal.Pcbi.1001015 |
0.412 |
|
| 2010 |
Rafi SB, McClendon CL, Jacobson MP. Using Statistically Significant Correlated Motions of Residues in a MD Based Approach to Investigate Allostery in Ubiquitin Conjugating Protein Biophysical Journal. 98: 388a. DOI: 10.1016/J.Bpj.2009.12.2091 |
0.434 |
|
| 2009 |
McClendon CL, Friedland G, Mobley DL, Amirkhani H, Jacobson MP. Quantifying Correlations Between Allosteric Sites in Thermodynamic Ensembles. Journal of Chemical Theory and Computation. 5: 2486-2502. PMID 20161451 DOI: 10.1021/Ct9001812 |
0.463 |
|
| 2007 |
Wells JA, McClendon CL. Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature. 450: 1001-9. PMID 18075579 DOI: 10.1038/Nature06526 |
0.512 |
|
| 2006 |
McClendon CL, Vaidehi N, Kam VW, Zhang D, Goddard WA. Fidelity of seryl-tRNA synthetase to binding of natural amino acids from HierDock first principles computations. Protein Engineering, Design & Selection : Peds. 19: 195-203. PMID 16517553 DOI: 10.1093/Protein/Gzl001 |
0.372 |
|
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