Robert Smock, Ph.D. - Publications
Affiliations: | 2011 | Molecular & Cellular Biology | University of Massachusetts, Amherst, Amherst, MA |
Area:
protein foldingYear | Citation | Score | |||
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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 | 0.396 | |||
2016 | Smock RG, Yadid I, Dym O, Clarke J, Tawfik DS. De Novo Evolutionary Emergence of a Symmetrical Protein Is Shaped by Folding Constraints. Cell. PMID 26806127 DOI: 10.1016/J.Cell.2015.12.024 | 0.353 | |||
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 | 0.509 | |||
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 | 0.591 | |||
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 | 0.62 | |||
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 | 0.519 | |||
2009 | Smock RG, Gierasch LM. Sending signals dynamically. Science (New York, N.Y.). 324: 198-203. PMID 19359576 DOI: 10.1126/Science.1169377 | 0.449 | |||
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 | 0.377 | |||
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 | 0.513 | |||
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