Interaction of HSPA5 (Grp78, BIP) with negatively charged phospholipid membranes via oligomerization involving the N-terminal end domain
出版年份 2020 全文链接
标题
Interaction of HSPA5 (Grp78, BIP) with negatively charged phospholipid membranes via oligomerization involving the N-terminal end domain
作者
关键词
-
出版物
CELL STRESS & CHAPERONES
Volume -, Issue -, Pages -
出版商
Springer Science and Business Media LLC
发表日期
2020-07-28
DOI
10.1007/s12192-020-01134-9
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注意:仅列出部分参考文献,下载原文获取全部文献信息。- The small heat shock proteins, HSPB1 and HSPB5, interact differently with lipid membranes
- (2019) Antonio De Maio et al. CELL STRESS & CHAPERONES
- Heat Shock Proteins Are Essential Components in Transformation and Tumor Progression: Cancer Cell Intrinsic Pathways and Beyond
- (2019) Lang et al. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
- Thermal aggregates of human mortalin and Hsp70-1A behave as supramolecular assemblies
- (2019) Vanessa T.R. Kiraly et al. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
- Disposing of misfolded ER proteins: A troubled substrate's way out of the ER
- (2019) Christina Oikonomou et al. MOLECULAR AND CELLULAR ENDOCRINOLOGY
- Molecular AFM imaging of Hsp70-1A association with dipalmitoyl phosphatidylserine reveals membrane blebbing in the presence of cholesterol
- (2018) Constanze Lamprecht et al. CELL STRESS & CHAPERONES
- Middle East respiratory syndrome coronavirus and bat coronavirus HKU9 both can utilize GRP78 for attachment onto host cells
- (2018) Hin Chu et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Mechanical properties of BiP protein determined by nano-rheology
- (2018) Nathalie Casanova-Morales et al. PROTEIN SCIENCE
- The endoplasmic reticulum (ER) chaperone BiP is a master regulator of ER functions: Getting by with a little help from ERdj friends
- (2018) Kristine Faye R. Pobre et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Binding of Pneumocystis carinii to the lung epithelial cell receptor HSPA5 (GRP78)
- (2018) Theodore J. Kottom et al. JOURNAL OF MEDICAL MICROBIOLOGY
- Bacterial Hsp70 (DnaK) and mammalian Hsp70 interact differently with lipid membranes
- (2016) Victor Lopez et al. CELL STRESS & CHAPERONES
- Protein misfolding in the endoplasmic reticulum as a conduit to human disease
- (2016) Miao Wang et al. NATURE
- From Conformation to Interaction: Techniques to Explore the Hsp70/ Hsp90 Network
- (2015) Fernanda Batista et al. CURRENT PROTEIN & PEPTIDE SCIENCE
- Characterization and Mechanism of Stress-induced Translocation of 78-Kilodalton Glucose-regulated Protein (GRP78) to the Cell Surface
- (2015) Yuan-Li Tsai et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Hsp70 Forms Antiparallel Dimers Stabilized by Post-translational Modifications to Position Clients for Transfer to Hsp90
- (2015) Nina Morgner et al. Cell Reports
- Monitoring Charge Flux to Quantify Unusual Ligand-Induced Ion Channel Activity for Use in Biological Nanopore-Based Sensors
- (2014) Florika C. Macazo et al. ANALYTICAL CHEMISTRY
- Interaction of heat shock protein 70 with membranes depends on the lipid environment
- (2014) Gabrielle Armijo et al. CELL STRESS & CHAPERONES
- Extracellular Hsp70: Export and Function
- (2014) Antonio De Maio CURRENT PROTEIN & PEPTIDE SCIENCE
- Hsp70 Translocates into the Plasma Membrane after Stress and Is Released into the Extracellular Environment in a Membrane-Associated Form that Activates Macrophages
- (2014) V. L. Vega et al. JOURNAL OF IMMUNOLOGY
- Hsp70 Oligomerization Is Mediated by an Interaction between the Interdomain Linker and the Substrate-Binding Domain
- (2013) Francesco A. Aprile et al. PLoS One
- Lipids of mitochondria
- (2013) Susanne E. Horvath et al. PROGRESS IN LIPID RESEARCH
- Extracellular Heat Shock Proteins
- (2013) Antonio De Maio et al. SHOCK
- Endoplasmic Reticulum Stress Sensing in the Unfolded Protein Response
- (2013) B. M. Gardner et al. Cold Spring Harbor Perspectives in Biology
- The critical roles of endoplasmic reticulum chaperones and unfolded protein response in tumorigenesis and anticancer therapies
- (2012) B Luo et al. ONCOGENE
- The Molecular Chaperone Hsp70 Family Members Function by a Bidirectional Heterotrophic Allosteric Mechanism
- (2011) Kelly P. da Silva et al. PROTEIN AND PEPTIDE LETTERS
- The Distribution and Function of Phosphatidylserine in Cellular Membranes
- (2010) Peter A. Leventis et al. Annual Review of Biophysics
- Mechanisms of the Hsp70 chaperone systemThis paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer review process.
- (2010) Jason C. Young Biochemistry and Cell Biology
- Extracellular heat shock proteins, cellular export vesicles, and the Stress Observation System: A form of communication during injury, infection, and cell damage
- (2010) Antonio De Maio CELL STRESS & CHAPERONES
- The critical role of GRP78 in physiologic and pathologic stress
- (2010) Kyle T Pfaffenbach et al. CURRENT OPINION IN CELL BIOLOGY
- Cell Surface Relocalization of the Endoplasmic Reticulum Chaperone and Unfolded Protein Response Regulator GRP78/BiP
- (2010) Yi Zhang et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Binding of heat shock protein 70 to extracellular phosphatidylserine promotes killing of normoxic and hypoxic tumor cells
- (2009) Daniela Schilling et al. FASEB JOURNAL
- Molecular Chaperone BiP Interacts with Borna Disease Virus Glycoprotein at the Cell Surface
- (2009) T. Honda et al. JOURNAL OF VIROLOGY
- Unconventional Mechanisms of Protein Transport to the Cell Surface of Eukaryotic Cells
- (2008) Walter Nickel et al. Annual Review of Cell and Developmental Biology
- Guidelines for the nomenclature of the human heat shock proteins
- (2008) Harm H. Kampinga et al. CELL STRESS & CHAPERONES
- Membrane Phosphatidylserine Regulates Surface Charge and Protein Localization
- (2008) T. Yeung et al. SCIENCE
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