MORC3, a Component of PML Nuclear Bodies, Has a Role in Restricting Herpes Simplex Virus 1 and Human Cytomegalovirus.

about

MORC Proteins: Novel Players in Plant and Animal Health.High-Definition Analysis of Host Protein Stability during Human Cytomegalovirus Infection Reveals Antiviral Factors and Viral Evasion Mechanisms

P2860

Q43122065-722D066C-930F-486D-8FCF-6B545B5ACF01 Q57010098-14B0350D-79B1-4D96-9512-BA95325F0E0F

P2860

MORC3, a Component of PML Nuclear Bodies, Has a Role in Restricting Herpes Simplex Virus 1 and Human Cytomegalovirus.

Item

http://www.wikidata.org/entity/Q40605496

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

MORC3, a Component of PML Nucl ...... s 1 and Human Cytomegalovirus.

@en

type

Item

label

MORC3, a Component of PML Nucl ...... s 1 and Human Cytomegalovirus.

@en

prefLabel

MORC3, a Component of PML Nucl ...... s 1 and Human Cytomegalovirus.

@en

P1476

MORC3, a Component of PML Nucl ...... s 1 and Human Cytomegalovirus.

@en

P2093

Anne Orr

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

Roger D Everett

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

P2860

Splice variants of the nuclear dot-associated Sp100 protein contain homologies to HMG-1 and a human nuclear phosphoprotein-box motif

Reconstitution of the KRAB-KAP-1 repressor complex: a model system for defining the molecular anatomy of RING-B box-coiled-coil domain-mediated protein-protein interactions

Role of SUMO-1-modified PML in nuclear body formation

Nucleocytoplasmic translocation of Stat1 is regulated by a leucine-rich export signal in the coiled-coil domain

A point mutation in the N-terminal coiled-coil domain releases c-Fes tyrosine kinase activity and survival signaling in myeloid leukemia cells

PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0

Evidence for a role of the cellular ND10 protein PML in mediating intrinsic immunity against human cytomegalovirus infections

Dynamic regulation of p53 subnuclear localization and senescence by MORC3

Human cytomegalovirus infection causes degradation of Sp100 proteins that suppress viral gene expression

Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption

P304

8621-8633

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

P31

scholarly article

P356

10.1128/JVI.00621-16

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

P407

English

P433

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

P478

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

P50

Elizabeth Sloan

P577

2016-07-20T00:00:00Z

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

P698

27440897

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

P921

Cytomegalovirus

P932

5021396

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

MORC3, a Component of PML Nuclear Bodies, Has a Role in Restricting Herpes Simplex Virus 1 and Human Cytomegalovirus.

about

P2860

P2860

MORC3, a Component of PML Nuclear Bodies, Has a Role in Restricting Herpes Simplex Virus 1 and Human Cytomegalovirus.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932