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.
178 related articles for article (PubMed ID: 31063619)
1. Frustrated Interfaces Facilitate Dynamic Interactions between Native Client Proteins and Holdase Chaperones. He L; Hiller S Chembiochem; 2019 Nov; 20(22):2803-2806. PubMed ID: 31063619 [TBL] [Abstract][Full Text] [Related]
2. A molecular mechanism of chaperone-client recognition. He L; Sharpe T; Mazur A; Hiller S Sci Adv; 2016 Nov; 2(11):e1601625. PubMed ID: 28138538 [TBL] [Abstract][Full Text] [Related]
3. Common Patterns in Chaperone Interactions with a Native Client Protein. He L; Hiller S Angew Chem Int Ed Engl; 2018 May; 57(20):5921-5924. PubMed ID: 29498447 [TBL] [Abstract][Full Text] [Related]
4. Chaperone-Bound Clients: The Importance of Being Dynamic. Hiller S Trends Biochem Sci; 2019 Jun; 44(6):517-527. PubMed ID: 30611607 [TBL] [Abstract][Full Text] [Related]
5. Heterogeneous binding of the SH3 client protein to the DnaK molecular chaperone. Lee JH; Zhang D; Hughes C; Okuno Y; Sekhar A; Cavagnero S Proc Natl Acad Sci U S A; 2015 Aug; 112(31):E4206-15. PubMed ID: 26195753 [TBL] [Abstract][Full Text] [Related]
11. Impact of holdase chaperones Skp and SurA on the folding of β-barrel outer-membrane proteins. Thoma J; Burmann BM; Hiller S; Müller DJ Nat Struct Mol Biol; 2015 Oct; 22(10):795-802. PubMed ID: 26344570 [TBL] [Abstract][Full Text] [Related]
12. Insights into the client protein release mechanism of the ATP-independent chaperone Spy. He W; Li X; Xue H; Yang Y; Mencius J; Bai L; Zhang J; Xu J; Wu B; Xue Y; Quan S Nat Commun; 2022 May; 13(1):2818. PubMed ID: 35595811 [TBL] [Abstract][Full Text] [Related]
13. Characterizations of the Interactions between Escherichia coli Periplasmic Chaperone HdeA and Its Native Substrates during Acid Stress. Yu XC; Yang C; Ding J; Niu X; Hu Y; Jin C Biochemistry; 2017 Oct; 56(43):5748-5757. PubMed ID: 29016106 [TBL] [Abstract][Full Text] [Related]
14. How do Chaperones Bind (Partly) Unfolded Client Proteins? Sučec I; Bersch B; Schanda P Front Mol Biosci; 2021; 8():762005. PubMed ID: 34760928 [TBL] [Abstract][Full Text] [Related]
15. Structural basis for the antifolding activity of a molecular chaperone. Huang C; Rossi P; Saio T; Kalodimos CG Nature; 2016 Sep; 537(7619):202-206. PubMed ID: 27501151 [TBL] [Abstract][Full Text] [Related]
16. Substrate protein folds while it is bound to the ATP-independent chaperone Spy. Stull F; Koldewey P; Humes JR; Radford SE; Bardwell JCA Nat Struct Mol Biol; 2016 Jan; 23(1):53-58. PubMed ID: 26619265 [TBL] [Abstract][Full Text] [Related]
17. The Periplasmic Chaperones Skp and SurA. Mas G; Thoma J; Hiller S Subcell Biochem; 2019; 92():169-186. PubMed ID: 31214987 [TBL] [Abstract][Full Text] [Related]
18. Chaperones and chaperone-substrate complexes: Dynamic playgrounds for NMR spectroscopists. Burmann BM; Hiller S Prog Nucl Magn Reson Spectrosc; 2015 Apr; 86-87():41-64. PubMed ID: 25919198 [TBL] [Abstract][Full Text] [Related]
19. The dynamic dimer structure of the chaperone Trigger Factor. Morgado L; Burmann BM; Sharpe T; Mazur A; Hiller S Nat Commun; 2017 Dec; 8(1):1992. PubMed ID: 29222465 [TBL] [Abstract][Full Text] [Related]