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A hidden aggregation-prone structure in the heart of hypoxia inducible factor prolyl hydroxylase.

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第一作者： Hamid,Hadi-Alijanvand

第一单位： Department of Biological Sciences, Institute for Advanced Studies in Basic Sciences (IASBS), Zanjan, Iran.;Institute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran, Iran.

作者： Hamid,Hadi-Alijanvand ^[1] ; Elizabeth A,Proctor ^[2] ; Feng,Ding ^[3] ; Nikolay V,Dokholyan ^[4] ; Ali A,Moosavi-Movahedi ^[5]

作者单位： Department of Biological Sciences, Institute for Advanced Studies in Basic Sciences (IASBS), Zanjan, Iran.;Institute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran, Iran. ^[1] Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139. ^[2] Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, School of Medicine, Chapel Hill, North Carolina, 27599.;Department of Physics and Astronomy, Clemson University, Clemson, South Carolina, 29634. ^[3] Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, School of Medicine, Chapel Hill, North Carolina, 27599.;Curriculum in Bioinformatics and Computational Biology, University of North Carolina at Chapel Hill, School of Medicine, Chapel Hill, North Carolina, 27599.;Program in Molecular and Cellular Biophysics, University of North Carolina at Chapel Hill, School of Medicine, Chapel Hill, North Carolina, 27599. ^[4] Institute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran, Iran.;Center of Excellence in Biothermodynamics, Institute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran, Iran. ^[5]

关键词 HIF-1 aggregation prone intermediate state angiogenesis calorimetry discrete molecular dynamics potential of mean force protein misfolding

医学主题词淀粉样蛋白(Amyloid);人类(Humans);分子动力学模拟(Molecular Dynamics Simulation);蛋白质构象(Protein Conformation);蛋白质解折叠(Protein Unfolding)

DOI 10.1002/prot.25011

PMID 26868435

发布时间 2017-01-07

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准确一般字义偏差语意偏离译文作用小提交