A highly membrane-active peptide in Flock House virus: implications for the mechanism of nodavirus infection.
about
Membranotropic Cell Penetrating Peptides: The Outstanding JourneyDeterminants of strain-specific differences in efficiency of reovirus entryStructure of a membrane-binding domain from a non-enveloped animal virus: insights into the mechanism of membrane permeability and cellular entry.NMR structure of a viral peptide inserted in artificial membranes: a view on the early steps of the birnavirus entry processAssembly and maturation of a T = 4 quasi-equivalent virus is guided by electrostatic and mechanical forces.Multi-disciplinary studies of viruses: the role of structure in shaping the questions and answers.Morphological changes in the T=3 capsid of Flock House virus during cell entry.The capsid of infectious bursal disease virus contains several small peptides arising from the maturation process of pVP2Dissecting quasi-equivalence in nonenveloped viruses: membrane disruption is promoted by lytic peptides released from subunit pentamers, not hexamers.A chaperone-activated nonenveloped virus perforates the physiologically relevant endoplasmic reticulum membrane.Dissecting the functional domains of a nonenveloped virus membrane penetration peptide.Virus entry paradigms.Viral weapons of membrane destruction: variable modes of membrane penetration by non-enveloped viruses.Cell penetrating peptides can exert biological activity: a review.Influence of membrane composition on the binding and folding of a membrane lytic peptide from the non-enveloped flock house virus.Functional genetic and biophysical analyses of membrane disruption by human adenovirusEffect of mutations in VP5 hydrophobic loops on rotavirus cell entryRescue of maturation-defective flock house virus infectivity with noninfectious, mature, viruslike particles.Infectious bursal disease virus, a non-enveloped virus, possesses a capsid-associated peptide that deforms and perforates biological membranes.Membrane partitioning of the cleavage peptide in flock house virus.Structural peptides of a nonenveloped virus are involved in assembly and membrane translocationPutative autocleavage of outer capsid protein micro1, allowing release of myristoylated peptide micro1N during particle uncoating, is critical for cell entry by reovirus.Low endocytic pH and capsid protein autocleavage are critical components of Flock House virus cell entryFolding a viral peptide in different membrane environments: pathway and sampling analyses.
P2860
Q26778015-AA73997A-7421-4052-88DD-36593CCFE3D8Q30155993-AF9E41F0-4B4F-4067-A50F-8939F207B46DQ31049547-83073F6A-769D-4A3D-8628-95CD61B36C73Q33552978-7FF89377-5DE7-4711-9CF0-919141143AD1Q34102316-C5E8B4F3-E567-45AB-B5D9-C641F6093DDAQ34186729-A5AA6CD4-EAAF-4371-B04A-6DD0C670BE33Q34301768-F138B032-6AE5-4975-93A1-56BEEE68CFDDQ34331938-7791915D-5C29-4BC8-A4BC-2AFD499D5B8CQ36246211-93AAE7A3-7C75-4142-8A4C-7F3DF3814843Q36315820-1E247746-7953-43D1-96CB-28FCE00AEE32Q37232773-E97798A4-0D2F-413D-873B-52D669E2D27AQ37614299-787DD2CA-AB3B-4C84-80D2-08D993853539Q37909045-5E1DBBEF-A9DC-495C-89D0-639B78FB8AD2Q38472405-CE84EFAC-A20F-4D7D-A9EF-2A84B6F1208CQ38843789-7686E162-C87B-4CB1-B764-F26FF55442C8Q39611726-5835B4A4-FFFF-4514-9C2D-1F508EFE3591Q39717493-B16B036F-9262-42C3-AF29-7FE6362E87D4Q40035957-8013EFAF-A0B7-4698-B79A-3AE39BE0D80BQ40135132-4777AA8F-3678-4562-9090-54D982B478ACQ40158248-2BB91138-AD82-4B25-A7DB-B54E8B1A1338Q40373908-37357592-68EC-49E3-8669-8688E38B622DQ40530759-51585B53-B5F5-4D9B-821F-656F02A3F98EQ42092014-3BF14DE0-CE50-4C48-8269-6AE4482ABDD5Q52691099-AF7C6D27-D9CC-4F9D-B1AC-FD5A098B6E75
P2860
A highly membrane-active peptide in Flock House virus: implications for the mechanism of nodavirus infection.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh-hant
name
A highly membrane-active pepti ...... hanism of nodavirus infection.
@en
A highly membrane-active pepti ...... hanism of nodavirus infection.
@nl
type
label
A highly membrane-active pepti ...... hanism of nodavirus infection.
@en
A highly membrane-active pepti ...... hanism of nodavirus infection.
@nl
prefLabel
A highly membrane-active pepti ...... hanism of nodavirus infection.
@en
A highly membrane-active pepti ...... hanism of nodavirus infection.
@nl
P2093
P1476
A highly membrane-active pepti ...... chanism of nodavirus infection
@en
P2093
J E Johnson
M Reza Ghadiri
P304
P356
10.1016/S1074-5521(99)80065-9
P577
1999-07-01T00:00:00Z