A Biophysical Study of Integral Membrane Protein Folding-Reference-Cited by-同舟云学术

A Biophysical Study of Integral Membrane Protein Folding

Published:1997-12-01 Issue:49 Volume:36 Page:15156-15176
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Hunt John F.¹,Earnest Thomas N.¹,Bousché Olaf¹,Kalghatgi Krishna¹,Reilly Karlyne¹,Horváth Csaba¹,Rothschild Kenneth J.¹,Engelman Donald M.¹

Affiliation:

1. Department of Molecular Biophysics and Biochemistry and Department of Chemical Engineering, Yale University, New Haven, Connecticut 06511, and Department of Physics and Molecular Biophysics Laboratory, Boston University, Boston, Massachusetts 02215

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi970146j

Reference102 articles.

1. Signal recognition protein is required for the integration of acetylcholine receptor delta subunit, a transmembrane glycoprotein, into the endoplasmic reticulum membrane.

2. Principles that Govern the Folding of Protein Chains

3. Multiple topogenic sequences in bovine opsin.

4. The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin.

5. Images of purple membrane at 2.8 Å resolution obtained by cryo-electron microscopy

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