Identification of the N-terminal peptide binding site of glucose-regulated protein 94.
about
GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulumTargeted mutation of the mouse Grp94 gene disrupts development and perturbs endoplasmic reticulum stress signalingComparison of PGH2 binding site in prostaglandin synthases.Heat-shock protein-based vaccines for cancer and infectious disease.Enhancement of humoral immune responses to HBsAg by heat shock protein gp96 and its N-terminal fragment in mice.GP96 interacts with HHV-6 during viral entry and directs it for cellular degradation.The messenger and the message: gp96 (GRP94)-peptide interactions in cellular immunityNear infrared dyes as lifetime solvatochromic probes for micropolarity measurements of biological systems.Interaction of Toll-Like Receptors with the Molecular Chaperone Gp96 Is Essential for Its Activation of Cytotoxic T Lymphocyte Response.Heat shock protein vaccines: from bench to bedside.Heat shock proteins and regulatory T cellsHeat-shock protein-peptide complex-96 for the treatment of cancer.A Human Variant of Glucose-Regulated Protein 94 That Inefficiently Supports IGF Production.Allogeneic tumor-cell-based vaccines secreting endoplasmic reticulum chaperone gp96.Vaccine therapy for renal cancer.An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells.Efficient cross-priming of antiviral CD8+ T cells by antigen donor cells is GRP94 independentGlycoprotein 96-mediated presentation of human immunodeficiency virus type 1 (HIV-1)-specific human leukocyte antigen class I-restricted peptide and humoral immune responses to HIV-1 p24.GRP94 in ER quality control and stress responsesSecreted heat shock protein gp96-Ig: next-generation vaccines for cancer and infectious diseases.The peptide-binding activity of GRP94 is regulated by calcium.Testing the role of gp96 as peptide chaperone in antigen processing.Escherichia coli interaction with human brain microvascular endothelial cells induces signal transducer and activator of transcription 3 association with the C-terminal domain of Ec-gp96, the outer membrane protein A receptor for invasion.The ATPase cycle of the endoplasmic chaperone Grp94.
P2860
Q26860153-2F7B3B1B-A119-4872-A962-5CDF08E0B426Q27326154-4893A678-3CA1-4725-90DE-8B717518C8E8Q33528245-866BACF1-849B-4FFD-89F6-344B8982DB11Q34768299-38EAE85D-B787-4208-9656-7868C285B234Q35010256-1E1AAA4E-96D2-4236-921B-5DE1F5E2121CQ35485426-4B94C854-BD8C-4769-BA9A-2F3E2E9F3BDFQ36000449-0A9BDF4A-8F6A-47F4-9019-F43A467E7654Q36008649-D3F38FEB-0A50-412D-869D-2F9F8899C19FQ36018660-42CE134C-5BC7-4FF8-9366-681BAC4DF477Q36684490-A1A4E616-19B6-4087-B6CC-DA9F0C9D2513Q36729007-8A105CF3-A5C9-4BF2-B335-DE61629E336EQ36909395-F6EA65D4-5809-49A7-9E7C-CE530479F136Q36911625-B19178C0-E765-4D66-9FC3-9E99E0428FD4Q36981666-9420053A-8A2E-46EC-AD17-15DC199F5C14Q37259586-99AF24FA-3DEC-4B15-BFBA-05F6D1DBB385Q37261639-AD681FF4-326F-452E-A0A1-8A5EC95C4B8DQ37359887-379FC092-2DFF-425B-9D7A-1490056C2282Q37410002-98A13369-5565-432C-8E73-162D942D2BA5Q37707530-0686501B-9FEE-48D9-AF9F-4FE29E463AD4Q38164258-220D98C6-B84B-467C-BB00-93491F753E4AQ40148862-B2D62D8B-EF5F-46A4-84A0-D04BD14FA960Q40454951-BB186C98-E834-4223-A141-225A47246783Q43245507-C54AA255-5F46-46AA-91EC-DDB000E1ACF9Q46959087-161AE61B-18D0-4595-9579-FD448CF412AF
P2860
Identification of the N-terminal peptide binding site of glucose-regulated protein 94.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh
2004年學術文章
@zh-hant
name
Identification of the N-terminal peptide binding site of glucose-regulated protein 94.
@en
Identification of the N-terminal peptide binding site of glucose-regulated protein 94.
@en-gb
Identification of the N-terminal peptide binding site of glucose-regulated protein 94.
@nl
type
label
Identification of the N-terminal peptide binding site of glucose-regulated protein 94.
@en
Identification of the N-terminal peptide binding site of glucose-regulated protein 94.
@en-gb
Identification of the N-terminal peptide binding site of glucose-regulated protein 94.
@nl
prefLabel
Identification of the N-terminal peptide binding site of glucose-regulated protein 94.
@en
Identification of the N-terminal peptide binding site of glucose-regulated protein 94.
@en-gb
Identification of the N-terminal peptide binding site of glucose-regulated protein 94.
@nl
P2093
P2860
P50
P356
P1476
Identification of the N-terminal peptide binding site of glucose-regulated protein 94.
@en
P2093
Chhanda Biswas
Fred Stevens
Haim J Wolfson
Yair Argon
P2860
P304
16543-16552
P356
10.1074/JBC.M313060200
P407
P577
2004-01-30T00:00:00Z