Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding.
about
Cooperation of an RNA packaging signal and a viral envelope protein in coronavirus RNA packagingThe role of severe acute respiratory syndrome (SARS)-coronavirus accessory proteins in virus pathogenesisThe Severe Acute Respiratory Syndrome (SARS)-coronavirus 3a protein may function as a modulator of the trafficking properties of the spike proteinMolecular mechanisms of severe acute respiratory syndrome (SARS)Regulation of Stress Responses and Translational Control by CoronavirusLocalization of mouse hepatitis virus nonstructural proteins and RNA synthesis indicates a role for late endosomes in viral replicationCoronavirus particle assembly: primary structure requirements of the membrane protein.Assembly of the coronavirus envelope: homotypic interactions between the M proteinsImmunocytochemical analysis of Uukuniemi virus budding compartments: role of the intermediate compartment and the Golgi stack in virus maturationMouse Hepatitis Coronavirus RNA Replication Depends on GBF1-Mediated ARF1 ActivationThe M, E, and N structural proteins of the severe acute respiratory syndrome coronavirus are required for efficient assembly, trafficking, and release of virus-like particles.The open reading frame 3a protein of severe acute respiratory syndrome-associated coronavirus promotes membrane rearrangement and cell death.Four proteins processed from the replicase gene polyprotein of mouse hepatitis virus colocalize in the cell periphery and adjacent to sites of virion assembly.Interaction of the coronavirus infectious bronchitis virus membrane protein with beta-actin and its implication in virion assembly and buddingSARS-CoV envelope protein palmitoylation or nucleocapid association is not required for promoting virus-like particle productionA single tyrosine in the severe acute respiratory syndrome coronavirus membrane protein cytoplasmic tail is important for efficient interaction with spike proteinA structural analysis of M protein in coronavirus assembly and morphology.Infectious bronchitis virus 3a protein localizes to a novel domain of the smooth endoplasmic reticulum.Intracellular complexes of viral spike and cellular receptor accumulate during cytopathic murine coronavirus infections.Expression of the two major envelope proteins of equine arteritis virus as a heterodimer is necessary for induction of neutralizing antibodies in mice immunized with recombinant Venezuelan equine encephalitis virus replicon particles.Retargeting of coronavirus by substitution of the spike glycoprotein ectodomain: crossing the host cell species barrierIdentification of a novel cleavage activity of the first papain-like proteinase domain encoded by open reading frame 1a of the coronavirus Avian infectious bronchitis virus and characterization of the cleavage products.Characterization of the coronavirus mouse hepatitis virus strain A59 small membrane protein E.Self-assembly of severe acute respiratory syndrome coronavirus membrane protein.Infectious bronchitis virus E protein is targeted to the Golgi complex and directs release of virus-like particles.Mouse hepatitis virus replicase proteins associate with two distinct populations of intracellular membranesCharacterization of the coronavirus M protein and nucleocapsid interaction in infected cells.Murine coronavirus requires lipid rafts for virus entry and cell-cell fusion but not for virus release.Palmitoylation of SARS-CoV S protein is necessary for partitioning into detergent-resistant membranes and cell-cell fusion but not interaction with M protein.A major determinant for membrane protein interaction localizes to the carboxy-terminal domain of the mouse coronavirus nucleocapsid protein.Contribution of trafficking signals in the cytoplasmic tail of the infectious bronchitis virus spike protein to virus infection.The coronavirus nucleocapsid is a multifunctional protein.Severe acute respiratory syndrome coronavirus group-specific open reading frames encode nonessential functions for replication in cell cultures and mice.Murine coronavirus replication induces cell cycle arrest in G0/G1 phase.Intracellular targeting signals contribute to localization of coronavirus spike proteins near the virus assembly site.A conserved domain in the coronavirus membrane protein tail is important for virus assembly.Coronavirus pathogenesis and the emerging pathogen severe acute respiratory syndrome coronavirus.A single polar residue and distinct membrane topologies impact the function of the infectious bronchitis coronavirus E protein.Picornavirus morphogenesis.The cytoplasmic tail of infectious bronchitis virus E protein directs Golgi targeting.
P2860
Q24529170-7A88FE8F-653B-41E0-92EA-DABD808A6C66Q24605877-8FEA48B2-5177-4040-B5D9-F5ADD549CC0AQ24792382-B22471B7-AF92-4C34-91B4-5CDFF06EB9C9Q24799739-C7D48CEA-FC5A-4F8F-B528-65658A9E5B4EQ26744222-54102C13-C009-4EE9-A7DC-028AC3C25191Q27469368-705742E0-38BE-435E-9D5C-EDDBFD4BF90BQ27469560-99167972-2923-4924-8767-F99C0A96075EQ27469592-5C4D61D7-6473-47BF-B87D-32B9814A6529Q27480779-E276F7A7-2C42-4768-A0B4-68484D29452CQ27486170-660DF337-0E2F-4468-AE01-FEFEC8E33A92Q30484261-E872ECCF-F3F6-46D7-92FB-3887DCF46EABQ30492548-0317470C-B641-4CC8-ABAC-E6834D7E2BA0Q30844680-0F457252-56FE-44C2-ABCD-38AE4A983172Q33418288-86BC206F-43B7-43FD-A33D-60361A0BDA89Q33582305-DA26577D-C272-41EC-B6AA-26EEE6530DA1Q33614610-101758FB-4B56-4DFB-93B7-DE97407F0CC9Q33763099-9EC886A3-03EF-45A4-9F1F-F6BA5181BA2AQ33780656-60D4B98C-8345-4629-86DF-814304915D40Q33783391-659AAA59-48FE-4E9C-9134-EDE800A9BD19Q33787304-9D6CB507-FFE8-40EA-9C5C-680268D7EC97Q33793489-7B76886C-3805-402A-A37A-46E03E840195Q33797237-96388BC6-421A-43F1-9701-33687EFDA1A0Q33798977-EF19F0CE-EBD1-4A31-A5C4-33123DBE29DCQ33800043-D69AAAEB-2FE4-46C7-9B29-704881E0564EQ33803912-8176AB31-1E75-4226-941A-7224371ADEC1Q33805898-550C0EF8-78B2-4AE8-86ED-0C5A70E8D83CQ33810949-0E8B6BF1-42F7-478A-9AE0-10C541E2D951Q33908845-8C5F90B8-8024-423D-9005-4B3AE1996EDEQ34037293-AD35766A-4372-4285-B07A-741C8CB6E5C8Q34092794-450540C9-B3E1-489C-B9F9-173BB7B549DFQ34092818-B0BE5DE3-3D3B-43BD-8A76-2B86F3B91EFCQ34102257-F5CD332C-3780-455C-B5D6-CCD234F1E2B0Q34142905-54282F3C-D0A9-45FD-A5D1-D1D9C0A2AF92Q34151707-3EE45197-42C7-4B81-A342-127A5675AEB8Q34152645-5BF2C728-3321-4A9D-B422-1B36BF1AE174Q34190645-62434CA2-5E59-4F29-854D-B2BB92BC2E8DQ34193942-D50245BF-70B9-4852-A751-29F92DB5A9A1Q34263059-B1243FB1-8313-4CA9-AA2F-E66EB136E92CQ34297832-EA5110CC-DCAB-4251-84F1-8C0156686DACQ34330304-5FFCC64F-9748-4017-8EAD-2D6E49E7F74C
P2860
Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding.
@ast
Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding.
@en
type
label
Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding.
@ast
Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding.
@en
prefLabel
Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding.
@ast
Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding.
@en
P2093
P2860
P1433
P1476
Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding.
@en
P2093
P2860
P304
P407
P577
1994-10-01T00:00:00Z