The role of BiP in endoplasmic reticulum-associated degradation of major histocompatibility complex class I heavy chain induced by cytomegalovirus proteins.
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Protein disulphide isomerase is required for signal peptide peptidase-mediated protein degradationHepatitis C Virus Infection Induces Autophagy as a Prosurvival Mechanism to Alleviate Hepatic ER-Stress ResponseEffects of messenger RNA structure and other translational control mechanisms on major histocompatibility complex-I mediated antigen presentationThe delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiologyGRP78(BiP) facilitates the cytosolic delivery of anthrax lethal factor (LF) in vivo and functions as an unfoldase in vitro.Overexpression of the endoplasmic reticulum chaperone BiP3 regulates XA21-mediated innate immunity in rice.The p97 ATPase dislocates MHC class I heavy chain in US2-expressing cells via a Ufd1-Npl4-independent mechanism.BiP negatively affects ricin transport.Identification of subtilase cytotoxin (SubAB) receptors whose signaling, in association with SubAB-induced BiP cleavage, is responsible for apoptosis in HeLa cells.New cell-signaling pathways for controlling cytomegalovirus replication.The human cytomegalovirus protein pUL38 suppresses endoplasmic reticulum stress-mediated cell death independently of its ability to induce mTORC1 activation.Requirements for mouse mammary tumor virus Rem signal peptide processing and functionCyclophilin C Participates in the US2-Mediated Degradation of Major Histocompatibility Complex Class I Molecules.Beyond the endoplasmic reticulum: atypical GRP78 in cell viability, signalling and therapeutic targetingHuman cytomegalovirus specifically controls the levels of the endoplasmic reticulum chaperone BiP/GRP78, which is required for virion assembly.Characterization of the human cytomegalovirus gH/gL/UL128-131 complex that mediates entry into epithelial and endothelial cells.The unfolded protein response in hereditary haemochromatosis.A bipartite trigger for dislocation directs the proteasomal degradation of an endoplasmic reticulum membrane glycoproteinEndoplasmic reticulum chaperones participate in human cytomegalovirus US2-mediated degradation of class I major histocompatibility complex molecules.The unfolded protein response and autophagy: herpesviruses rule!The endoplasmic reticulum chaperone BiP/GRP78 is important in the structure and function of the human cytomegalovirus assembly compartment.Glucose-regulated protein 78 is an intracellular antiviral factor against hepatitis B virus.Diverse immune evasion strategies by human cytomegalovirus.A new paradigm: innate immune sensing of viruses via the unfolded protein response.The expanding roles of endoplasmic reticulum stress in virus replication and pathogenesis.LQT1-associated mutations increase KCNQ1 proteasomal degradation independently of Derlin-1.Human cytomegalovirus induces the endoplasmic reticulum chaperone BiP through increased transcription and activation of translation by using the BiP internal ribosome entry site.The Endoplasmic Reticulum-associated Degradation of Transthyretin Variants Is Negatively Regulated by BiP in Mammalian Cells.CSFV Infection Up-Regulates the Unfolded Protein Response to Promote Its Replication.Enzymes Involved in AMPylation and deAMPylation.Adaptation to constant light requires Fic-mediated AMPylation of BiP to protect against reversible photoreceptor degeneration
P2860
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P2860
The role of BiP in endoplasmic reticulum-associated degradation of major histocompatibility complex class I heavy chain induced by cytomegalovirus proteins.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
The role of BiP in endoplasmic ...... d by cytomegalovirus proteins.
@en
type
label
The role of BiP in endoplasmic ...... d by cytomegalovirus proteins.
@en
prefLabel
The role of BiP in endoplasmic ...... d by cytomegalovirus proteins.
@en
P2093
P2860
P356
P1476
The role of BiP in endoplasmic ...... ed by cytomegalovirus proteins
@en
P2093
David C Johnson
Kathy Shire
Lori Frappier
Mathieu S Chevalier
Michael C Denton
Todd W Wisner
P2860
P304
20910-20919
P356
10.1074/JBC.M602989200
P407
P577
2006-05-25T00:00:00Z