Histone deacetylase 6 regulates human immunodeficiency virus type 1 infection - Wikidata - awgldk - TriplyDB

Histone deacetylase 6 regulates human immunodeficiency virus type 1 infection

Histone deacetylase 6 regulates human immunodeficiency virus type 1 infection

http://www.wikidata.org/entity/Q24535531

about

Metabolism, cytoskeleton and cellular signalling in the grip of protein Nepsilon - and O-acetylation Circovirus transport proceeds via direct interaction of the cytoplasmic dynein IC1 subunit with the viral capsid protein Actin-binding protein drebrin regulates HIV-1-triggered actin polymerization and viral infection Gelsolin activity controls efficient early HIV-1 infection Regulation of Retinoic Acid Inducible Gene-I (RIG-I) Activation by the Histone Deacetylase 6 Viral Interactions with PDZ Domain-Containing Proteins-An Oncogenic Trait?Manipulation of the host protein acetylation network by human immunodeficiency virus type 1 How HIV takes advantage of the cytoskeleton in entry and replication Mice lacking histone deacetylase 6 have hyperacetylated tubulin but are viable and develop normally.Lymphocyte chemotaxis is regulated by histone deacetylase 6, independently of its deacetylase activity.HIV-1 requires Arf6-mediated membrane dynamics to efficiently enter and infect T lymphocytes.The PDZ-adaptor protein syntenin-1 regulates HIV-1 entry Transcriptional Gene Silencing (TGS) via the RNAi Machinery in HIV-1 Infections Jmjd3-mediated epigenetic regulation of inflammatory cytokine gene expression in serum amyloid A-stimulated macrophages.Paxillin inhibits HDAC6 to regulate microtubule acetylation, Golgi structure, and polarized migration.Clostridium difficile toxin A decreases acetylation of tubulin, leading to microtubule depolymerization through activation of histone deacetylase 6, and this mediates acute inflammation.Tubulin acetylation: responsible enzymes, biological functions and human diseases.Regulation of Tat acetylation and transactivation activity by the microtubule-associated deacetylase HDAC6.Histone deacetylase inhibitors for purging HIV-1 from the latent reservoir.Activity of the human immunodeficiency virus type 1 cell cycle-dependent internal ribosomal entry site is modulated by IRES trans-acting factors The HDAC6/APOBEC3G complex regulates HIV-1 infectiveness by inducing Vif autophagic degradation.Overexpression of Histone Deacetylase 6 Enhances Resistance to Porcine Reproductive and Respiratory Syndrome Virus in Pigs.Histone deacetylase 6 inhibition enhances oncolytic viral replication in glioma.The histone deacetylase inhibitor ITF2357 decreases surface CXCR4 and CCR5 expression on CD4(+) T-cells and monocytes and is superior to valproic acid for latent HIV-1 expression in vitro.HDAC6 regulates cellular viral RNA sensing by deacetylation of RIG-I.Passport control for foreign integrated DNAs: An unexpected checkpoint by class II HDAC4 revealed by amino acid starvation.Histone Deacetylase 6 Regulates Bladder Architecture and Host Susceptibility to Uropathogenic Escherichia coli.Retroviral proteins that interact with the host cell cytoskeleton Uropathogenic Escherichia coli invades host cells via an HDAC6-modulated microtubule-dependent pathway.Submembraneous microtubule cytoskeleton: regulation of ATPases by interaction with acetylated tubulin.The lupane-type triterpene 30-oxo-calenduladiol is a CCR5 antagonist with anti-HIV-1 and anti-chemotactic activities.Inclusion Body Fusion of Human Parainfluenza Virus Type 3 Regulated by Acetylated α-Tubulin Enhances Viral Replication.The tale of protein lysine acetylation in the cytoplasm.Viral infection: Moving through complex and dynamic cell-membrane structures.HDAC inhibitors in HIV.Trend of histone deacetylase inhibitors in cancer therapy: isoform selectivity or multitargeted strategy.Histone deacetylase 6 in health and disease.An overview of investigational Histone deacetylase inhibitors (HDACis) for the treatment of non-Hodgkin's lymphoma.Histone deacetylase 6 inhibits influenza A virus release by downregulating the trafficking of viral components to the plasma membrane via its substrate, acetylated microtubules.HIV-1 induces the formation of stable microtubules to enhance early infection.

P2860

Q24307834-2A043445-42DE-4970-AA3C-FB0A14DA9D72 Q24311598-5FEB72CE-1B90-4E64-874E-B248AA00FDD7 Q24316027-C5EC77F6-CD69-4D9A-88B0-99EDD053521D Q24338224-3A1F0465-16C7-462B-94C8-F0A56D90403B Q26700093-15F401B2-8F80-47F4-BF68-5DE0355C46D9 Q26770053-ABB5ECB5-A84E-444B-B599-9EDB0FCD513A Q26795463-A8A5E59D-D90E-4933-9584-443037ECEBA2 Q27021639-18008957-260A-42C6-A411-EADC839C0085 Q27919716-1F5D01B3-BBEE-421E-9C82-FBF1AB65C938 Q30477707-28563F57-7C8E-4121-826B-C6C260E26BB8 Q30499676-91C8A6E0-1C0B-4972-BEDC-9963B339F356 Q30515961-2D3693E0-4948-407D-AD61-5456833F2A36 Q33565167-386B652E-1670-4B68-8FF0-7D1266D53AFA Q33922619-3C725D4D-BD8C-4D6F-9548-300A420C2904 Q34003129-59BAC158-B394-407C-BA17-940071B747CF Q34236680-E5238F4A-93F4-4F67-888E-DBDC076BFF66 Q34487624-937024AF-9FF4-4026-B5BD-AD824E8AC5C0 Q34685118-55AA6428-CFAD-4624-82F8-96179FC0701B Q35016964-4B0C59B9-3582-4016-9209-D5B86E6DB1D3 Q35153487-3DD42DEB-941F-4CE3-A817-932D99538ECF Q35776289-98F9D9BD-A797-4378-9A65-C50FB2F3BEF9 Q36239538-D10CA1ED-805D-44A2-A381-5762B751B861 Q36266545-DA2B80A6-3D20-44A2-8247-0C6D3087292F Q36501927-99856E36-D8EB-4386-B42B-C32CBF6C3886 Q36584342-9145ECB8-ECC1-4A96-8B43-F87200B06026 Q36618586-6D74C826-9415-4A80-B2A1-3AAF20DC62DE Q36735425-FAB5E7C4-0B2C-4BF5-BC91-759F07272D80 Q36913964-20586C43-C72B-4565-93F6-2E66C552D02F Q37029864-F8CC2E00-3235-4561-AC7C-388D4860BD4D Q37255250-DB759F55-7BDD-4D5E-84CC-47B0CE1CDBE0 Q37269171-1EC5B8C9-09A2-4D38-80F2-5D5A411501C3 Q37593225-6DC968FF-544B-4689-930D-0543DFEDADDB Q37820143-C8BCACA5-9386-4422-AA04-CD2CCFFEB12C Q37941707-487CFB18-B347-49EC-B551-C601C592AC21 Q37956178-7BBA1BD7-9756-43F4-B975-5D38FE62B813 Q38208280-2146AB77-520A-46A1-B0FA-7C126238D561 Q38357741-A7521BD9-A387-4A82-AA54-CC14E43C8434 Q38765451-5F3D3BCA-8BAA-4919-9FDE-988FD36D1256 Q38974742-AA3E10A5-DBE4-4325-B1E3-DBB43F758138 Q39062821-90325D19-D89B-4434-ADF9-3D5F02ACD79B

P2860

Histone deacetylase 6 regulates human immunodeficiency virus type 1 infection

http://www.wikidata.org/entity/Q24535531

description

2005 nî lūn-bûn

@nan

2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2005年の論文

@ja

2005年学术文章

@wuu

2005年学术文章

@zh-cn

2005年学术文章

@zh-hans

2005年学术文章

@zh-my

2005年学术文章

@zh-sg

2005年學術文章

@yue

name

Histone deacetylase 6 regulates human immunodeficiency virus type 1 infection

@ast

Histone deacetylase 6 regulates human immunodeficiency virus type 1 infection

@en

Histone deacetylase 6 regulates human immunodeficiency virus type 1 infection

@en-gb

Histone deacetylase 6 regulates human immunodeficiency virus type 1 infection

@nl

type

label

Histone deacetylase 6 regulates human immunodeficiency virus type 1 infection

@ast

Histone deacetylase 6 regulates human immunodeficiency virus type 1 infection

@en

Histone deacetylase 6 regulates human immunodeficiency virus type 1 infection

@en-gb

Histone deacetylase 6 regulates human immunodeficiency virus type 1 infection

@nl

prefLabel

Histone deacetylase 6 regulates human immunodeficiency virus type 1 infection

@ast

Histone deacetylase 6 regulates human immunodeficiency virus type 1 infection

@en

Histone deacetylase 6 regulates human immunodeficiency virus type 1 infection

@en-gb

Histone deacetylase 6 regulates human immunodeficiency virus type 1 infection

@nl

P1433

Q24535531-1940D377-3D96-4672-B91C-DD737EC76E67

P1476

Q24535531-262AE558-8787-48CB-BD02-4BE5D129C5BC

P2093

Q24535531-299FE44C-B7C5-4081-AD6C-6B85DEA95E98

Q24535531-533FD191-2D32-4764-A6CD-29CEA27B2702

Q24535531-57ECCAEE-26A3-46C6-88B5-60A6D983A227

Q24535531-5CFE613D-F3EC-44E0-AA81-A962925E6186

Q24535531-61304340-06A7-4A7F-B16E-91F9FECF3200

Q24535531-C0405AAA-F81F-4423-AFF6-48379508CED9

Q24535531-CC39622C-0C57-4FDC-96AF-56589FAA4BBF

Q24535531-F66FD124-96FA-487F-8C57-F7E290C64C2D

P2860

Q24535531-058F951A-E5AC-4FC6-9F8F-775EE21CEC94

Q24535531-07EE9A55-9130-4F8A-88CA-B9F3B56BE652

Q24535531-0B6347E8-25B2-4317-AD90-25D7489CE2ED

Q24535531-0EAD8679-02BF-4E88-9EA0-29E02FC0ABB9

Q24535531-178239F1-2AF9-4CCC-B106-EFD21521C221

Q24535531-1A02E34F-5A6F-4605-87D5-9989FE131C52

Q24535531-1B12DBE2-A569-466A-92F9-1AD26EFC5C5F

Q24535531-1BD13BA3-2DC9-4E77-A2F3-F769A33474A1

Q24535531-1F01CCFD-322B-48FC-AA76-EC55D00E0974

Q24535531-239CA9CE-7507-4762-9BDE-FCBBB916C5FE

P304

Q24535531-A73363EA-9139-42B4-B308-DAC100A7C112

P31

Q24535531-FABF5A21-058C-4F1F-9FF4-2E61BC4C7958

P356

Q24535531-9F494081-047F-48BB-B12E-5E311313626B

P407

Q24535531-CC020F27-D2EE-49A8-A988-4CFB2A7631C8

P433

Q24535531-CB69C28E-F2C9-4EC8-9DC4-EED216A00348

P478

Q24535531-8E468AAC-516C-4CD7-A5C3-11A8DAC66B12

P50

Q24535531-8F29A67D-A5DC-4AEE-B3F8-A95D304DD25E

Q24535531-A619771B-A9BC-4837-AE99-47E773A86DEF

Q24535531-BA4F87EA-02D3-480D-868E-B14E6FB1A19E

Q24535531-CAD77F25-73F2-40B1-9CA3-23DC37C76F47

P577

Q24535531-9C586BDB-6CA7-4784-808D-6F28D1171F75

P698

Q24535531-52BA0144-031D-466F-9095-64C46B901D49

P921

Q24535531-66893FA3-D122-4426-B95B-9F6220BFCFBC

P932

Q24535531-01D15FF7-BF6B-4374-BD16-5F73EF959919

P356

MBC.E05-04-0354

P1433

Molecular Biology of the Cell

P1476

Histone deacetylase 6 regulates human immunodeficiency virus type 1 infection

@en

P2093

Angeles Ursa

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

Gerónimo Fernández

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

J Román Cabrero

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

M Angeles Muñoz-Fernández

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

Marta Barrero

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

Mónica Gordon-Alonso

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

Salvador Naranjo-Suárez

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

Susana Alvarez

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

P2860

Three proteins define a class of human histone deacetylases related to yeast Hda1p

HIV-1 Entry Cofactor: Functional cDNA Cloning of a Seven-Transmembrane, G Protein-Coupled Receptor

HIV-1 cell to cell transfer across an Env-induced, actin-dependent synapse

Identification of a major co-receptor for primary isolates of HIV-1

HDAC6 is a microtubule-associated deacetylase

HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor

The lymphocyte chemoattractant SDF-1 is a ligand for LESTR/fusin and blocks HIV-1 entry

Establishment of a functional human immunodeficiency virus type 1 (HIV-1) reverse transcription complex involves the cytoskeleton

A dual-tropic primary HIV-1 isolate that uses fusin and the beta-chemokine receptors CKR-5, CKR-3, and CKR-2b as fusion cofactors

Mechanisms of apoptosis induction by the HIV-1 envelope

P304

5445-5454

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

P31

scholarly article

P356

10.1091/MBC.E05-04-0354

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

P407

P433

11

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

P478

16

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

P50

Francisco Sánchez-Madrid

María Yáñez-Mó

Juan M Serrador

Agustín Valenzuela-Fernández

P577

2005-09-07T00:00:00Z

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

P698

16148047

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

P921

P932

1266439

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