Cryo-EM Structure of a Molluscan Hemocyanin Suggests Its Allosteric Mechanism-Reference-Cited by-同舟云学术

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Cryo-EM Structure of a Molluscan Hemocyanin Suggests Its Allosteric Mechanism

Published:2013-04 Issue:4 Volume:21 Page:604-613
ISSN:0969-2126
Container-title:Structure
language:en
Short-container-title:Structure

Author:

Zhang Qinfen,Dai Xinghong,Cong Yao,Zhang Junjie,Chen Dong-Hua,Dougherty Matthew T.,Wang Jiangyong,Ludtke Steven J.,Schmid Michael F.,Chiu Wah

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference44 articles.

1. Gene structure and hemocyanin isoform HtH2 from the mollusc Haliotis tuberculata indicate early and late intron hot spots;Altenhein;Gene,2002

2. Molecular evolution of the arthropod hemocyanin superfamily;Burmester;Mol. Biol. Evol.,2001

3. An expanded conformation of single-ring GroEL-GroES complex encapsulates an 86 kDa substrate;Chen;Structure,2006

4. Structural mechanism of SDS-induced enzyme activity of scorpion hemocyanin revealed by electron cryomicroscopy;Cong;Structure,2009

5. Crystal structure of a functional unit from Octopus hemocyanin;Cuff;J. Mol. Biol.,1998

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3. CryoEM structure and Alphafold molecular modelling of a novel molluscan hemocyanin;PLOS ONE;2023-06-22

4. Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications;Chemical Reviews;2020-04-22

5. Hemocyanin of the caenogastropod Pomacea canaliculata exhibits evolutionary differences among gastropod clades;PLOS ONE;2020-01-30

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