Format
Sort by
Items per page

Send to

Choose Destination

Search results

Items: 6

1.

Interplay of disordered and ordered regions of a human small heat shock protein yields an ensemble of 'quasi-ordered' states.

Clouser AF, Baughman HE, Basanta B, Guttman M, Nath A, Klevit RE.

Elife. 2019 Oct 1;8. pii: e50259. doi: 10.7554/eLife.50259. [Epub ahead of print]

2.

Hydrogen-deuterium exchange mass spectrometry of membrane proteins in lipid nanodiscs.

Redhair M, Clouser AF, Atkins WM.

Chem Phys Lipids. 2019 May;220:14-22. doi: 10.1016/j.chemphyslip.2019.02.007. Epub 2019 Feb 22. Review.

PMID:
30802434
3.

HspB1 and Hsc70 chaperones engage distinct tau species and have different inhibitory effects on amyloid formation.

Baughman HER, Clouser AF, Klevit RE, Nath A.

J Biol Chem. 2018 Feb 23;293(8):2687-2700. doi: 10.1074/jbc.M117.803411. Epub 2018 Jan 3.

4.

pH-dependent structural modulation is conserved in the human small heat shock protein HSBP1.

Clouser AF, Klevit RE.

Cell Stress Chaperones. 2017 Jul;22(4):569-575. doi: 10.1007/s12192-017-0783-z. Epub 2017 Mar 22.

5.

Control over overall shape and size in de novo designed proteins.

Lin YR, Koga N, Tatsumi-Koga R, Liu G, Clouser AF, Montelione GT, Baker D.

Proc Natl Acad Sci U S A. 2015 Oct 6;112(40):E5478-85. doi: 10.1073/pnas.1509508112. Epub 2015 Sep 22.

6.

Structure of the α-crystallin domain from the redox-sensitive chaperone, HSPB1.

Rajagopal P, Liu Y, Shi L, Clouser AF, Klevit RE.

J Biomol NMR. 2015 Oct;63(2):223-8. doi: 10.1007/s10858-015-9973-0. Epub 2015 Aug 5. No abstract available.

Supplemental Content

Loading ...
Support Center