Thiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus fusion protein.
about
Two highly conserved cysteine residues in HPV16 L2 form an intramolecular disulfide bond and are critical for infectivity in human keratinocytesGalectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entryInflammatory and oxidative stress in rotavirus infectionPoxvirus cell entry: how many proteins does it take?Protein disulfide isomerase and host-pathogen interactionStructural basis of viral invasion: lessons from paramyxovirus FDynamic interactions of the UL16 tegument protein with the capsid of herpes simplex virus.Attachment and entry of Chlamydia have distinct requirements for host protein disulfide isomerase.Features of a spatially constrained cystine loop in the p10 FAST protein ectodomain define a new class of viral fusion peptides.Modification of the respiratory syncytial virus f protein in virus-like particles impacts generation of B cell memory.Bacitracin is not a specific inhibitor of protein disulfide isomerase.Cell-type specific requirements for thiol/disulfide exchange during HIV-1 entry and infectionProtein Disulfide Isomerase Superfamily in Disease and the Regulation of ApoptosisAssembly and immunological properties of Newcastle disease virus-like particles containing the respiratory syncytial virus F and G proteins.Reducible DNA nanoparticles enhance in vitro gene transfer via an extracellular mechanismCell surface protein disulfide isomerase regulates natriuretic peptide generation of cyclic guanosine monophosphate.The transmembrane domain sequence affects the structure and function of the Newcastle disease virus fusion protein.Neutrophils Turn Plasma Proteins into Weapons against HIV-1.The nairovirus nairobi sheep disease virus/ganjam virus induces the translocation of protein disulphide isomerase-like oxidoreductases from the endoplasmic reticulum to the cell surface and the extracellular space.Package of NDV-pseudotyped HIV-Luc virus and its application in the neutralization assay for NDV infection.Murine immune responses to virus-like particle-associated pre- and postfusion forms of the respiratory syncytial virus F proteinMutations in the DI-DII Linker of Human Parainfluenza Virus Type 3 Fusion Protein Result in Diminished Fusion Activity.The protein disulfide isomerase 1 of Phytophthora parasitica (PpPDI1) is associated with the haustoria-like structures and contributes to plant infection.Thiol-reactive reagents inhibits intracellular trafficking of human papillomavirus type 16 pseudovirions by binding to cysteine residues of major capsid protein L1.Overexpression of thiol/disulfide isomerases enhances membrane fusion directed by the Newcastle disease virus fusion proteinRole of thiol/disulfide exchange in newcastle disease virus entryThe requirement of reactive oxygen intermediates for lymphocytic choriomeningitis virus binding and growth.Effect of cell membrane thiols and reduction-triggered disassembly on transfection activity of bioreducible polyplexesOpposing influence of intracellular and membrane thiols on the toxicity of reducible polycationsLaSota fusion (F) cleavage motif-mediated fusion activity is affected by other regions of the F protein from different genotype Newcastle disease virus in a chimeric virus: implication for virulence attenuationConformational changes in redox pairs of protein structures.PROTEIN DISULFIDE ISOMERASE LIKE 5-1 is a susceptibility factor to plant viruses.Membrane uncoating of intact enveloped viruses.Immunoregulation through membrane proteins modified by reducing conditions induced by immune reactions.The role of cellular oxidoreductases in viral entry and virus infection-associated oxidative stress: potential therapeutic applications.Labile disulfide bonds are common at the leucocyte cell surface.Inhibiting rotavirus infection by membrane-impermeant thiol/disulfide exchange blockers and antibodies against protein disulfide isomerase.Baculovirus GP64 disulfide bonds: the intermolecular disulfide bond of Autographa californica multicapsid nucleopolyhedrovirus GP64 is not essential for membrane fusion and virion budding.Identification of differentially regulated maize proteins conditioning Sugarcane mosaic virus systemic infection.Enhanced cellular uptake of maleimide-modified liposomes via thiol-mediated transport.
P2860
Q21143868-99934816-F482-4770-A66F-9032367FA351Q24306482-7FF7A748-FC70-4B9C-864B-6B6424E82732Q26749801-361D63E1-C205-47AF-845C-40874A971B03Q27002455-FE7F0649-6D22-4091-B378-915A67E30746Q27005875-726E5927-0BCC-4994-AFD9-5D06B90E736AQ27481675-457D441C-E6FC-4C1D-8CFC-FDFB3FFCFF11Q30443300-CDE0C989-0E31-45F0-B3D5-C5E8A69DB008Q33426342-F77479A7-62E5-4215-8BF0-8B59BDE860FFQ33883443-DD96293C-744F-4CA2-B3CE-6E52B9C1F1BBQ34059404-ECA609ED-543E-4106-BFB8-8DEF41869EC8Q34115847-8884C160-4322-4335-89AF-77189E92A352Q34315133-7DE58710-8A60-43D0-A72F-F2ECF662C869Q34318367-6B4898A6-8E7D-48BA-A503-EB2449693E43Q34457791-7B0143E8-90B3-42CF-9EB8-554017A9458DQ34543854-91A000EE-01AB-417F-9A0D-7F0C2590B8B0Q34565711-31439854-45CF-41C7-BF96-B29ACAA81F70Q34742453-519417B5-FE7A-4301-A8AE-274742AB5BB0Q34804975-A3678FD9-F37F-4486-9896-AA113BF964B1Q35143016-EC1EBE7F-4FE2-42AE-A719-AC31E59FFA6DQ35189635-2F6DC1DD-0E86-4232-970C-1DACD6AD9EA6Q35745343-F8648EC3-7CF9-4FA0-9D1B-331DB37D26A8Q35754943-09E721F7-493D-44B7-8226-52C3FC281536Q35964062-50B88E3D-D23F-48AB-BDA9-E6F35D598C76Q36285957-07503AE2-3569-4652-8A81-268D345F37C6Q36994662-5BEBE0C8-6BAD-4FAB-B0D5-C8A4CAEB70D1Q37033266-19681376-EB34-4816-8926-E9E20F3CD3E8Q37041299-60279C6F-3714-4AE7-B9C0-8376C30C305BQ37062939-D0015880-A167-412B-AE5E-7ADAA77C1ABBQ37180892-A0907CDB-12E3-4184-BC4F-42F80B27B096Q37296010-5AC16DA5-4C99-4187-83EC-879179AA4B8EQ37420197-0A754337-744E-4C2E-88BE-0359519A7A81Q37587704-0F334E72-9782-4E87-A8F8-87DC5A8C947BQ37776382-B22B9FDB-88DB-4DE7-9FCD-B117E245C513Q38066808-2C1E73E7-5E6F-40E8-9206-789F839891D7Q38547857-BB858C22-F07B-41A8-820B-1A9138C56E28Q39340040-D7BD12DB-5C4E-42A9-BDFC-D08F02BAF3C0Q39383750-5695A5F4-5421-4594-B200-DD7DDB6055A9Q39688936-8E16B09D-A7F2-44AE-B87C-6A071A21CCBCQ40155071-5F63B7A1-2D98-47C3-9FC5-353F72963492Q40520681-01550A74-B240-4B9A-A6AD-3ED5BA19987B
P2860
Thiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus fusion protein.
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
Thiol/disulfide exchange is re ...... disease virus fusion protein.
@ast
Thiol/disulfide exchange is re ...... disease virus fusion protein.
@en
type
label
Thiol/disulfide exchange is re ...... disease virus fusion protein.
@ast
Thiol/disulfide exchange is re ...... disease virus fusion protein.
@en
prefLabel
Thiol/disulfide exchange is re ...... disease virus fusion protein.
@ast
Thiol/disulfide exchange is re ...... disease virus fusion protein.
@en
P2093
P2860
P356
P1433
P1476
Thiol/disulfide exchange is re ...... disease virus fusion protein.
@en
P2093
Lori W McGinnes
Surbhi Jain
Trudy G Morrison
P2860
P304
P356
10.1128/JVI.01940-06
P407
P577
2006-12-06T00:00:00Z