The role of HSP70 and its co-chaperones in protein misfolding, aggregation and disease.
about
Dancing through Life: Molecular Dynamics Simulations and Network-Centric Modeling of Allosteric Mechanisms in Hsp70 and Hsp110 Chaperone Proteins.The development of modified human Hsp70 (HSPA1A) and its production in the milk of transgenic mice.B-Cell-Based and Soluble Biomarkers in Body Liquids for Predicting Acute/Chronic Graft-versus-Host Disease after Allogeneic Hematopoietic Stem Cell Transplantation.Molecular Mechanisms Underlying Neuroprotective Effect of Intranasal Administration of Human Hsp70 in Mouse Model of Alzheimer's Disease.Proteolytic degradation of heat shock protein A2 occurs in response to oxidative stress in male germ cells of the mouse.Walking the tightrope: proteostasis and neurodegenerative disease.Targeting Hsp70: A possible therapy for cancer.Encapsulated Hsp70 decreases endotoxin-induced production of ROS and TNFα in human phagocytes.The heat shock response in neurons and astroglia and its role in neurodegenerative diseases.Differential Targeting of Hsp70 Heat Shock Proteins HSPA6 and HSPA1A with Components of a Protein Disaggregation/Refolding Machine in Differentiated Human Neuronal Cells following Thermal Stress.Components of a mammalian protein disaggregation/refolding machine are targeted to nuclear speckles following thermal stress in differentiated human neuronal cells.The FKBP51 Glucocorticoid Receptor Co-Chaperone: Regulation, Function, and Implications in Health and Disease.Knockdown of Heat Shock Proteins HSPA6 (Hsp70B') and HSPA1A (Hsp70-1) Sensitizes Differentiated Human Neuronal Cells to Cellular Stress.The FgSsb-FgZuo-FgSsz complex regulates multiple stress responses and mycotoxin production via folding the soluble SNARE Vam7 and β2-tubulin in Fusarium graminearum.Domain Mapping of Heat Shock Protein 70 Reveals That Glutamic Acid 446 and Arginine 447 Are Critical for Regulating Superoxide Dismutase 2 Function.Proteomic analysis of ginsenoside Re attenuates hydrogen peroxide-induced oxidative stress in human umbilical vein endothelial cells.Heat shock protein 70 protects mouse against post-infection irritable bowel syndrome via up-regulating intestinal γδ T cell's Th17 response.
P2860
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P2860
The role of HSP70 and its co-chaperones in protein misfolding, aggregation and disease.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
The role of HSP70 and its co-chaperones in protein misfolding, aggregation and disease.
@en
type
label
The role of HSP70 and its co-chaperones in protein misfolding, aggregation and disease.
@en
prefLabel
The role of HSP70 and its co-chaperones in protein misfolding, aggregation and disease.
@en
P1476
The role of HSP70 and its co-chaperones in protein misfolding, aggregation and disease
@en
P2093
Emma J Duncan
Jacqueline van der Spuy
P304
P356
10.1007/978-3-319-11731-7_12
P577
2015-01-01T00:00:00Z