Robert Smock, Ph.D.

Affiliations: 
2011 Molecular & Cellular Biology University of Massachusetts, Amherst, Amherst, MA 
Area:
protein folding
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Lila M. Gierasch grad student 2011 U Mass Amherst
 (Components of a protein machine: Allosteric domain assembly and a disordered c-terminus enable the chaperone functions of HSP70.)
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Publications

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Smock RG, Blackburn ME, Gierasch LM. (2018) Correction: Conserved, disordered C terminus of DnaK enhances cellular survival upon stress and DnaK chaperone activity. The Journal of Biological Chemistry. 293: 14295
Smock RG, Yadid I, Dym O, et al. (2016) De Novo Evolutionary Emergence of a Symmetrical Protein Is Shaped by Folding Constraints. Cell
Horwich AL, Buchner J, Smock RG, et al. (2012) Chaperones and protein folding Comprehensive Biophysics. 3: 212-237
Smock RG, Blackburn ME, Gierasch LM. (2011) 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
Smock RG, Rivoire O, Russ WP, et al. (2010) An interdomain sector mediating allostery in Hsp70 molecular chaperones. Molecular Systems Biology. 6: 414
Clerico EM, Zhuravleva A, Smock RG, et al. (2010) Segmental isotopic labeling of the Hsp70 molecular chaperone DnaK using expressed protein ligation. Biopolymers. 94: 742-52
Smock RG, Gierasch LM. (2009) Sending signals dynamically. Science (New York, N.Y.). 324: 198-203
Marcelino AM, Smock RG, Gierasch LM. (2006) Evolutionary coupling of structural and functional sequence information in the intracellular lipid-binding protein family. Proteins. 63: 373-84
Smock RG, Gierasch LM. (2005) Finding the fittest fold: using the evolutionary record to design new proteins. Cell. 122: 832-4
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