Work

Ring Separation Highlights the Protein-Folding Mechanism Used by the Phage EL-Encoded Chaperonin

Year: 2016

Type: article

Source: Structure

DOI: 10.1016/j.str.2016.02.006

Authors: Sudheer K. Molugu, Zacariah L. Hildenbrand, David Gene Morgan, Michael B. Sherman, Lilin He, Costa Georgopoulos, Natalia V. Sernova, Lidia P. Kurochkina, Vadim V. Mesyanzhinov, Konstantin A. Miroshnikov, Ricardo A. Bernal

Institutions: The University of Texas at El Paso, Indiana University Bloomington, Indiana University, The University of Texas Medical Branch at Galveston, Oak Ridge National Laboratory, University of Utah, Russian Academy of Sciences, Institute for Information Transmission Problems, Institute of Bioorganic Chemistry

Language: English

Topic: Heat shock proteins research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: National Science Foundation, Welch Foundation, National Cancer Institute, National Institute of General Medical Sciences, Basic Energy Sciences, Biological and Environmental Research

Awards: G3741648010, MRI: Acquisition of a Field Emission Gun Transmission Electron Microscope for Biological Structure Determination, Structural Significance of Point Mutations within the Human hsp60 Chaperonin, G7860235326

OpenAlex ID: W2307636869

FWCI: 1.213

Cites: 41

Cited by: 19

Related to: 10