These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

289 related articles for article (PubMed ID: 36613738)

  • 21. SurA is a cryptically grooved chaperone that expands unfolded outer membrane proteins.
    Marx DC; Plummer AM; Faustino AM; Devlin T; Roskopf MA; Leblanc MJ; Lessen HJ; Amann BT; Fleming PJ; Krueger S; Fried SD; Fleming KG
    Proc Natl Acad Sci U S A; 2020 Nov; 117(45):28026-28035. PubMed ID: 33093201
    [TBL] [Abstract][Full Text] [Related]  

  • 22. The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition.
    Hennecke G; Nolte J; Volkmer-Engert R; Schneider-Mergener J; Behrens S
    J Biol Chem; 2005 Jun; 280(25):23540-8. PubMed ID: 15840585
    [TBL] [Abstract][Full Text] [Related]  

  • 23. Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients.
    Calabrese AN; Schiffrin B; Watson M; Karamanos TK; Walko M; Humes JR; Horne JE; White P; Wilson AJ; Kalli AC; Tuma R; Ashcroft AE; Brockwell DJ; Radford SE
    Nat Commun; 2020 May; 11(1):2155. PubMed ID: 32358557
    [TBL] [Abstract][Full Text] [Related]  

  • 24. FkpA enhances membrane protein folding using an extensive interaction surface.
    Devlin T; Marx DC; Roskopf MA; Bubb QR; Plummer AM; Fleming KG
    Protein Sci; 2023 Apr; 32(4):e4592. PubMed ID: 36775935
    [TBL] [Abstract][Full Text] [Related]  

  • 25. The virulence factor PEB4 (Cj0596) and the periplasmic protein Cj1289 are two structurally related SurA-like chaperones in the human pathogen Campylobacter jejuni.
    Kale A; Phansopa C; Suwannachart C; Craven CJ; Rafferty JB; Kelly DJ
    J Biol Chem; 2011 Jun; 286(24):21254-65. PubMed ID: 21524997
    [TBL] [Abstract][Full Text] [Related]  

  • 26. Chaperone Spy Protects Outer Membrane Proteins from Folding Stress via Dynamic Complex Formation.
    He W; Yu G; Li T; Bai L; Yang Y; Xue Z; Pang Y; Reichmann D; Hiller S; He L; Liu M; Quan S
    mBio; 2021 Oct; 12(5):e0213021. PubMed ID: 34607455
    [TBL] [Abstract][Full Text] [Related]  

  • 27. Interaction between bacterial outer membrane proteins and periplasmic quality control factors: a kinetic partitioning mechanism.
    Wu S; Ge X; Lv Z; Zhi Z; Chang Z; Zhao XS
    Biochem J; 2011 Sep; 438(3):505-11. PubMed ID: 21671888
    [TBL] [Abstract][Full Text] [Related]  

  • 28. The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity.
    Behrens S; Maier R; de Cock H; Schmid FX; Gross CA
    EMBO J; 2001 Jan; 20(1-2):285-94. PubMed ID: 11226178
    [TBL] [Abstract][Full Text] [Related]  

  • 29. Insights into the function and structural flexibility of the periplasmic molecular chaperone SurA.
    Zhong M; Ferrell B; Lu W; Chai Q; Wei Y
    J Bacteriol; 2013 Mar; 195(5):1061-7. PubMed ID: 23275244
    [TBL] [Abstract][Full Text] [Related]  

  • 30. Conformational Dynamics of the Periplasmic Chaperone SurA.
    Jia M; Wu B; Yang Z; Chen C; Zhao M; Hou X; Niu X; Jin C; Hu Y
    Biochemistry; 2020 Sep; 59(35):3235-3246. PubMed ID: 32786408
    [TBL] [Abstract][Full Text] [Related]  

  • 31. Effects of Periplasmic Chaperones and Membrane Thickness on BamA-Catalyzed Outer-Membrane Protein Folding.
    Schiffrin B; Calabrese AN; Higgins AJ; Humes JR; Ashcroft AE; Kalli AC; Brockwell DJ; Radford SE
    J Mol Biol; 2017 Nov; 429(23):3776-3792. PubMed ID: 28919234
    [TBL] [Abstract][Full Text] [Related]  

  • 32. Solution NMR studies of membrane-protein-chaperone complexes.
    Burmann BM; Hiller S
    Chimia (Aarau); 2012; 66(10):759-63. PubMed ID: 23146261
    [TBL] [Abstract][Full Text] [Related]  

  • 33. Interaction of the periplasmic chaperone SurA with the inner membrane protein secretion (SEC) machinery.
    Troman LA; Alvira S; Daum B; Gold VAM; Collinson I
    Biochem J; 2023 Feb; 480(4):283-296. PubMed ID: 36701201
    [TBL] [Abstract][Full Text] [Related]  

  • 34. Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli.
    Rizzitello AE; Harper JR; Silhavy TJ
    J Bacteriol; 2001 Dec; 183(23):6794-800. PubMed ID: 11698367
    [TBL] [Abstract][Full Text] [Related]  

  • 35. The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues.
    Xu X; Wang S; Hu YX; McKay DB
    J Mol Biol; 2007 Oct; 373(2):367-81. PubMed ID: 17825319
    [TBL] [Abstract][Full Text] [Related]  

  • 36.
    Jia M; Hu Y; Jin C
    Biomol NMR Assign; 2019 Apr; 13(1):183-186. PubMed ID: 30684235
    [TBL] [Abstract][Full Text] [Related]  

  • 37. SurA assists the folding of Escherichia coli outer membrane proteins.
    Lazar SW; Kolter R
    J Bacteriol; 1996 Mar; 178(6):1770-3. PubMed ID: 8626309
    [TBL] [Abstract][Full Text] [Related]  

  • 38. The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins.
    Bitto E; McKay DB
    J Biol Chem; 2003 Dec; 278(49):49316-22. PubMed ID: 14506253
    [TBL] [Abstract][Full Text] [Related]  

  • 39. Identification of inhibitors of the E. coli chaperone SurA using in silico and in vitro techniques.
    Bell EW; Zheng EJ; Ryno LM
    Bioorg Med Chem Lett; 2018 Dec; 28(22):3540-3548. PubMed ID: 30301675
    [TBL] [Abstract][Full Text] [Related]  

  • 40. The protein-disulfide isomerase DsbC cooperates with SurA and DsbA in the assembly of the essential β-barrel protein LptD.
    Denoncin K; Vertommen D; Paek E; Collet JF
    J Biol Chem; 2010 Sep; 285(38):29425-33. PubMed ID: 20615876
    [TBL] [Abstract][Full Text] [Related]  

    [Previous]   [Next]    [New Search]
    of 15.