The carboxyl-terminal domain of inducible Hsp70 protects from ischemic injury in vivo and in vitro.
about
HSP72 protects cells from ER stress-induced apoptosis via enhancement of IRE1alpha-XBP1 signaling through a physical interactionHeat shock proteins in the brain: role of Hsp70, Hsp 27, and HO-1 (Hsp32) and their therapeutic potential.Xenon pretreatment may prevent early memory decline after isoflurane anesthesia and surgery in miceHeat shock proteins: cellular and molecular mechanisms in the central nervous system.Heat shock protein 72 overexpression prevents early postoperative memory decline after orthopedic surgery under general anesthesia in miceEnhanced Hsp70 expression protects against acute lung injury by modulating apoptotic pathways.Exercise preconditioning protects against spinal cord injury in rats by upregulating neuronal and astroglial heat shock protein 72.Overexpression of inducible heat shock protein 70 and its mutants in astrocytes is associated with maintenance of mitochondrial physiology during glucose deprivation stress.Astrocyte targeted overexpression of Hsp72 or SOD2 reduces neuronal vulnerability to forebrain ischemia.Overexpression of heat shock protein 72 attenuates NF-κB activation using a combination of regulatory mechanisms in microglia.Acute and prolonged hindlimb exercise elicits different gene expression in motoneurons than sensory neurons after spinal cord injuryBeyond anoxia: the physiology of metabolic downregulation and recovery in the anoxia-tolerant turtle.Chaperonopathies and chaperonotherapy.Postischemic brain injury is attenuated in mice lacking the beta2-adrenergic receptor.Regulation of apoptotic and inflammatory cell signaling in cerebral ischemia: the complex roles of heat shock protein 70Molecular physiology of preconditioning-induced brain tolerance to ischemia.Astrocyte-enriched miR-29a targets PUMA and reduces neuronal vulnerability to forebrain ischemiaNeuroprotective effects of geranylgeranylacetone in experimental traumatic brain injury.MicroRNAs regulate the chaperone network in cerebral ischemia.Pharmacologic heat shock protein 70 induction confers cytoprotection against inflammation in gliovascular cells.Hsp72 chaperone function is dispensable for protection against stress-induced apoptosisCloning of HSP90, expression and localization of HSP70/90 in different tissues including lactating/non-lactating yak (Bos grunniens) breast tissue.Overexpression of mitochondrial Hsp70/Hsp75 in rat brain protects mitochondria, reduces oxidative stress, and protects from focal ischemia.Very brief focal ischemia simulating transient ischemic attacks (TIAs) can injure brain and induce Hsp70 protein.TAT-Hsp70-mediated neuroprotection and increased survival of neuronal precursor cells after focal cerebral ischemia in mice.Spatiotemporal expression of Hsp20 and its phosphorylation in hippocampal CA1 pyramidal neurons after transient forebrain ischemia.Neuroprotective effects of individual or combined exposure to hypoxia and hypercapnia in the experiment.Hsp70 suppresses apoptosis in sympathetic neurones by preventing the activation of c-Jun.
P2860
Q21145793-3E445B53-CB4B-4FBB-BC98-FDB7826CD010Q27691409-C2B1859E-3610-45C0-B15D-1BC92B8AEA0DQ28743161-B379CFEC-EF87-4AA3-9B48-665EFED341A8Q30392284-5041584E-9139-45C7-BFEB-BA1FA1A74FFDQ30468926-55020BDE-E354-4248-B951-1FF2B31FABD7Q34087633-41191E9D-96D6-498C-89AE-29ABE5AC13E2Q34487007-F047A59F-9982-4B28-891B-C4C606E1A4B8Q34703681-AF811085-1E1F-451A-8799-53B78B9569DFQ35026095-0A8CB314-4032-40DB-BF6E-9551B6A407EDQ35091205-4FF77CC0-C3F4-4DC3-8B1C-B9A10DC37628Q35740049-5C456641-2848-45A5-A4E9-6B17150D3A41Q36627668-5ED31E26-DCC6-4F7E-A4B6-7A7E425954BAQ36809332-C3962656-091E-460A-BD1A-4DD0DD199F06Q36867076-4FD76330-BD7B-4525-BBEB-3255F807626FQ36923921-EB7E40A0-3487-4308-95F8-85C6A7BACA65Q37056974-1FFF7B93-41FC-4DA1-8CB7-FF22709CFD01Q37261050-2D4AA185-8008-4536-AE2E-54136728D883Q37365637-F917235F-BC58-4F74-97FE-5F3EFE6DC92BQ37396241-4C380573-FBED-4487-94A3-572FDB379984Q38895909-AB23F4B4-0492-4D5E-825F-044565B86220Q39935467-4F3A8184-B942-4402-AB04-3B469B02BB1BQ41034685-654219FB-F298-4AB7-82F7-B1E7C7435F2CQ42146138-2FF8FFBA-B53D-4F9C-97D2-7BECCBBFD43DQ43143762-9C6E8C89-BC44-4E51-A83E-920D17CCFD08Q46041604-0BE73045-6BE9-449F-8C24-1A198646A145Q46214468-44474E4C-6A79-4F5B-A2F9-54B83593E7E1Q48925794-75F51ADB-959B-42B7-B89A-43312AD8D268Q50659448-0182EDE9-87AA-42B6-9F1A-9223F3E7017E
P2860
The carboxyl-terminal domain of inducible Hsp70 protects from ischemic injury in vivo and in vitro.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
The carboxyl-terminal domain o ...... c injury in vivo and in vitro.
@en
The carboxyl-terminal domain o ...... c injury in vivo and in vitro.
@nl
type
label
The carboxyl-terminal domain o ...... c injury in vivo and in vitro.
@en
The carboxyl-terminal domain o ...... c injury in vivo and in vitro.
@nl
prefLabel
The carboxyl-terminal domain o ...... c injury in vivo and in vitro.
@en
The carboxyl-terminal domain o ...... c injury in vivo and in vitro.
@nl
P2093
P2860
P356
P1476
The carboxyl-terminal domain o ...... c injury in vivo and in vitro.
@en
P2093
Ari Man-Yi Chow
James G Hecker
Robin Anderson
Rona G Giffard
Yi-Bing Ouyang
Yunjuan Sun
P2860
P304
P356
10.1038/SJ.JCBFM.9600246
P577
2005-11-16T00:00:00Z