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Connection

Lila Gierasch to Allosteric Regulation

This is a "connection" page, showing publications Lila Gierasch has written about Allosteric Regulation.
Connection Strength

1.893
  1. Zhuravleva A, Gierasch LM. Substrate-binding domain conformational dynamics mediate Hsp70 allostery. Proc Natl Acad Sci U S A. 2015 Jun 02; 112(22):E2865-73.
    View in: PubMed
    Score: 0.465
  2. 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.
    View in: PubMed
    Score: 0.265
  3. Swain JF, Gierasch LM. The changing landscape of protein allostery. Curr Opin Struct Biol. 2006 Feb; 16(1):102-8.
    View in: PubMed
    Score: 0.243
  4. Rossi MA, Pozhidaeva AK, Clerico EM, Petridis C, Gierasch LM. New insights into the structure and function of the complex?between the Escherichia coli Hsp70, DnaK, and its nucleotide-exchange factor, GrpE. J Biol Chem. 2024 01; 300(1):105574.
    View in: PubMed
    Score: 0.211
  5. Meng W, Clerico EM, McArthur N, Gierasch LM. Allosteric landscapes of eukaryotic cytoplasmic Hsp70s are shaped by evolutionary tuning of key interfaces. Proc Natl Acad Sci U S A. 2018 11 20; 115(47):11970-11975.
    View in: PubMed
    Score: 0.148
  6. English CA, Sherman W, Meng W, Gierasch LM. The Hsp70 interdomain linker is a dynamic switch that enables allosteric communication between two structured domains. J Biol Chem. 2017 09 08; 292(36):14765-14774.
    View in: PubMed
    Score: 0.135
  7. Lai AL, Clerico EM, Blackburn ME, Patel NA, Robinson CV, Borbat PP, Freed JH, Gierasch LM. Key features of an Hsp70 chaperone allosteric landscape revealed by ion-mobility native mass spectrometry and double electron-electron resonance. J Biol Chem. 2017 05 26; 292(21):8773-8785.
    View in: PubMed
    Score: 0.133
  8. Zhuravleva A, Clerico EM, Gierasch LM. An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones. Cell. 2012 Dec 07; 151(6):1296-307.
    View in: PubMed
    Score: 0.098
  9. 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.
    View in: PubMed
    Score: 0.087
  10. 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.
    View in: PubMed
    Score: 0.060
  11. 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.
    View in: PubMed
    Score: 0.038
  12. Pellecchia M, Montgomery DL, Stevens SY, Vander Kooi CW, Feng HP, Gierasch LM, Zuiderweg ER. Structural insights into substrate binding by the molecular chaperone DnaK. Nat Struct Biol. 2000 Apr; 7(4):298-303.
    View in: PubMed
    Score: 0.010
Connection Strength

The connection strength for concepts is the sum of the scores for each matching publication.

Publication scores are based on many factors, including how long ago they were written and whether the person is a first or senior author.