Domain-Swapped Dimers of Intracellular Lipid-Binding Proteins: Evidence for Ordered Folding Intermediates-Reference-Cited by-同舟云学术

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Domain-Swapped Dimers of Intracellular Lipid-Binding Proteins: Evidence for Ordered Folding Intermediates

Published:2016-09 Issue:9 Volume:24 Page:1590-1598
ISSN:0969-2126
Container-title:Structure
language:en
Short-container-title:Structure

Author:

Assar Zahra,Nossoni Zahra,Wang Wenjing,Santos Elizabeth M.,Kramer Kevin,McCornack Colin,Vasileiou Chrysoula,Borhan Babak,Geiger James H.

Funder

NIH

DOE

Michigan Economic Development Corporation

Michigan Technology Tri-Corridor

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference48 articles.

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2. Rlefined structure of dimeric diphtheria-toxin at 2.0-Angstrom resolution;Bennett;Protein Sci.,1994

3. 3D domain swapping - a mechanism for oligomer assembly;Bennett;Protein Sci.,1995

4. Rational design of a colorimetric pH sensor from a soluble retinoic acid chaperone;Berbasova;J. Am. Chem. Soc.,2013

5. Light-activated reversible imine isomerization: towards a photochromic protein switch;Berbasova;ChemBioChem,2016

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2. Protein Assembly by Design;Chemical Reviews;2021-08-18

3. Experimental and theoretical study on converting myoglobin into a stable domain-swapped dimer by utilizing a tight hydrogen bond network at the hinge region;RSC Advances;2021

4. Human Cellular Retinol Binding Protein II Forms a Domain‐Swapped Trimer Representing a Novel Fold and a New Template for Protein Engineering;ChemBioChem;2020-08-14

5. Engineering the hCRBPII Domain-Swapped Dimer into a New Class of Protein Switches;Journal of the American Chemical Society;2019-09-26

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