Lila Gierasch to Binding Sites
This is a "connection" page, showing publications Lila Gierasch has written about Binding Sites.
Connection Strength
1.227
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Clerico EM, Pozhidaeva AK, Jansen RM, ?zden C, Tilitsky JM, Gierasch LM. Selective promiscuity in the binding of E. coli Hsp70 to an unfolded protein. Proc Natl Acad Sci U S A. 2021 10 12; 118(41).
Score: 0.153
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Clerico EM, Meng W, Pozhidaeva A, Bhasne K, Petridis C, Gierasch LM. Hsp70 molecular chaperones: multifunctional allosteric holding and unfolding machines. Biochem J. 2019 06 14; 476(11):1653-1677.
Score: 0.130
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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. J Mol Biol. 1999 Feb 26; 286(3):915-32.
Score: 0.127
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Smock RG, Blackburn ME, Gierasch LM. Conserved, disordered C terminus of DnaK enhances cellular survival upon stress and DnaK in vitro chaperone activity. J Biol Chem. 2011 Sep 09; 286(36):31821-9.
Score: 0.075
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Zhuravleva A, Gierasch LM. Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones. Proc Natl Acad Sci U S A. 2011 Apr 26; 108(17):6987-92.
Score: 0.074
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Smock RG, Gierasch LM. Sending signals dynamically. Science. 2009 Apr 10; 324(5924):198-203.
Score: 0.064
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Cl?rico EM, Maki JL, Gierasch LM. Use of synthetic signal sequences to explore the protein export machinery. Biopolymers. 2008; 90(3):307-19.
Score: 0.059
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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. Mol Cell. 2007 Apr 13; 26(1):27-39.
Score: 0.056
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Krishnan B, Szymanska A, Gierasch LM. Site-specific fluorescent labeling of poly-histidine sequences using a metal-chelating cysteine. Chem Biol Drug Des. 2007 Jan; 69(1):31-40.
Score: 0.055
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Marcelino AM, Smock RG, Gierasch LM. Evolutionary coupling of structural and functional sequence information in the intracellular lipid-binding protein family. Proteins. 2006 May 01; 63(2):373-84.
Score: 0.052
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Swain JF, Schulz EG, Gierasch LM. Direct comparison of a stable isolated Hsp70 substrate-binding domain in the empty and substrate-bound states. J Biol Chem. 2006 Jan 20; 281(3):1605-11.
Score: 0.051
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Chou YT, Gierasch LM. The conformation of a signal peptide bound by Escherichia coli preprotein translocase SecA. J Biol Chem. 2005 Sep 23; 280(38):32753-60.
Score: 0.050
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Cleverley RM, Gierasch LM. Mapping the signal sequence-binding site on SRP reveals a significant role for the NG domain. J Biol Chem. 2002 Nov 29; 277(48):46763-8.
Score: 0.041
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Swain JF, Gierasch LM. A new twist for an Hsp70 chaperone. Nat Struct Biol. 2002 Jun; 9(6):406-8.
Score: 0.040
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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 Comput Biol. 2021 11; 17(11):e1009567.
Score: 0.038
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Swain JF, Sivendran R, Gierasch LM. Defining the structure of the substrate-free state of the DnaK molecular chaperone. Biochem Soc Symp. 2001; (68):69-82.
Score: 0.036
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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. Mol Cell. 1997 Dec; 1(1):79-87.
Score: 0.029
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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 Comput Biol. 2014 May; 10(5):e1003624.
Score: 0.023
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Landry SJ, Gierasch LM. The chaperonin GroEL binds a polypeptide in an alpha-helical conformation. Biochemistry. 1991 Jul 30; 30(30):7359-62.
Score: 0.019
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Liu Y, Gierasch LM, Bahar I. Role of Hsp70 ATPase domain intrinsic dynamics and sequence evolution in enabling its functional interactions with NEFs. PLoS Comput Biol. 2010 Sep 16; 6(9).
Score: 0.018
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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. 2010 May 25; 49(20):4395-410.
Score: 0.017
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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. 2004 Jun 15; 43(23):7307-27.
Score: 0.012
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Kibbey RG, Rizo J, Gierasch LM, Anderson RG. The LDL receptor clustering motif interacts with the clathrin terminal domain in a reverse turn conformation. J Cell Biol. 1998 Jul 13; 142(1):59-67.
Score: 0.008