Myristylation and palmitylation of HSV-1 UL11 are not essential for its function. - Wikidata - awgldk - TriplyDB

Myristylation and palmitylation of HSV-1 UL11 are not essential for its function.

Myristylation and palmitylation of HSV-1 UL11 are not essential for its function.

http://www.wikidata.org/entity/Q41999353

about

Tegument Assembly and Secondary Envelopment of Alphaherpesviruses Replication of herpes simplex virus: egress of progeny virus at specialized cell membrane sites.Interaction and interdependent packaging of tegument protein UL11 and glycoprotein e of herpes simplex virus.Direct and specific binding of the UL16 tegument protein of herpes simplex virus to the cytoplasmic tail of glycoprotein E.Characterization and intracellular trafficking of Epstein-Barr virus BBLF1, a protein involved in virion maturation Elucidation of the block to herpes simplex virus egress in the absence of tegument protein UL16 reveals a novel interaction with VP22.Genome sequence of bubaline alphaherpesvirus 1 (BuHV1) isolated in Australia in 1972.Binding of Herpes Simplex Virus 1 UL20 to GODZ (DHHC3) Affects Its Palmitoylation and Is Essential for Infectivity and Proper Targeting and Localization of UL20 and Glycoprotein K.Regulated interaction of tegument proteins UL16 and UL11 from herpes simplex virus.Genome-wide engineering of an infectious clone of herpes simplex virus type 1 using synthetic genomics assembly methods.The absence of DHHC3 affects primary and latent HSV-1 infection.

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P2860

Myristylation and palmitylation of HSV-1 UL11 are not essential for its function.

http://www.wikidata.org/entity/Q41999353

description

2009 nî lūn-bûn

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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2009年论文

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2009年论文

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name

Myristylation and palmitylation of HSV-1 UL11 are not essential for its function.

@en

Myristylation and palmitylation of HSV-1 UL11 are not essential for its function.

@en-gb

type

label

Myristylation and palmitylation of HSV-1 UL11 are not essential for its function.

@en

Myristylation and palmitylation of HSV-1 UL11 are not essential for its function.

@en-gb

prefLabel

Myristylation and palmitylation of HSV-1 UL11 are not essential for its function.

@en

Myristylation and palmitylation of HSV-1 UL11 are not essential for its function.

@en-gb

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P356

J.VIROL.2009.10.046

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Myristylation and palmitylation of HSV-1 UL11 are not essential for its function.

@en

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Jason L Starkey

http://www.w3.org/2001/XMLSchema#string

John W Wills

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Nicholas L Baird

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P2860

Amino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids

Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1

Simple and highly efficient BAC recombineering using galK selection

Herpesvirus assembly: a tale of two membranes

Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins

Human cytomegalovirus UL99-encoded pp28 is required for the cytoplasmic envelopment of tegument-associated capsids.

Dynamic interactions of the UL16 tegument protein with the capsid of herpes simplex virus.

The equine herpesvirus 1 UL11 gene product localizes to the trans-golgi network and is involved in cell-to-cell spread.

Human cytomegalovirus cell-to-cell spread in the absence of an essential assembly protein.

Intracellular trafficking of the UL11 tegument protein of herpes simplex virus type 1.

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80-88

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scholarly article

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10.1016/J.VIROL.2009.10.046

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1

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