Tetramerization of SAMHD1 is required for biological activity and inhibition of HIV infection - Wikidata - awgldk - TriplyDB

Tetramerization of SAMHD1 is required for biological activity and inhibition of HIV infection

Tetramerization of SAMHD1 is required for biological activity and inhibition of HIV infection

http://www.wikidata.org/entity/Q24634238

about

New insights into an X-traordinary viral protein Mechanism of allosteric activation of SAMHD1 by dGTP Structural insight into dGTP-dependent activation of tetrameric SAMHD1 deoxynucleoside triphosphate triphosphohydrolase Intrinsic host restriction factors of human cytomegalovirus replication and mechanisms of viral escape Structural basis of lentiviral subversion of a cellular protein degradation pathway Mechanisms of Allosteric Activation and Inhibition of the Deoxyribonucleoside Triphosphate Triphosphohydrolase from Enterococcus faecalis The mechanism of substrate-controlled allosteric regulation of SAMHD1 activated by GTP Functional organization of human SAMHD1 and mechanisms of HIV-1 restriction The ribonuclease activity of SAMHD1 is required for HIV-1 restriction GTP activator and dNTP substrates of HIV-1 restriction factor SAMHD1 generate a long-lived activated state Effects of human SAMHD1 polymorphisms on HIV-1 susceptibility.SAMHD1 specifically affects the antiviral potency of thymidine analog HIV reverse transcriptase inhibitors dNTP pool modulation dynamics by SAMHD1 protein in monocyte-derived macrophages.Structural basis of cellular dNTP regulation by SAMHD1.SAMHD1 prevents autoimmunity by maintaining genome stability.A continuous enzyme-coupled assay for triphosphohydrolase activity of HIV-1 restriction factor SAMHD1 SAMHD1-mediated HIV-1 restriction in cells does not involve ribonuclease activity SAMHD1 is a biomarker for cytarabine response and a therapeutic target in acute myeloid leukemia.Substrates and Inhibitors of SAMHD1.Structural basis of allosteric activation of sterile α motif and histidine-aspartate domain-containing protein 1 (SAMHD1) by nucleoside triphosphates.Host factor SAMHD1 restricts DNA viruses in non-dividing myeloid cells Evolutionary toggling of Vpx/Vpr specificity results in divergent recognition of the restriction factor SAMHD1.Identification of critical regions in human SAMHD1 required for nuclear localization and Vpx-mediated degradation Structure of Escherichia coli dGTP triphosphohydrolase: a hexameric enzyme with DNA effector molecules.SAMHD1 specifically restricts retroviruses through its RNase activity.Phospho-dependent Regulation of SAMHD1 Oligomerisation Couples Catalysis and Restriction.CyclinA2-Cyclin-dependent Kinase Regulates SAMHD1 Protein Phosphohydrolase Domain.SAMHD1 is a single-stranded nucleic acid binding protein with no active site-associated nuclease activity Impaired dNTPase activity of SAMHD1 by phosphomimetic mutation of Thr-592 The SAMHD1 dNTP Triphosphohydrolase Is Controlled by a Redox Switch.Structural Insights into the High-efficiency Catalytic Mechanism of the Sterile α-Motif/Histidine-Aspartate Domain-containing Protein.Heterozygous colon cancer-associated mutations of SAMHD1 have functional significance The Cleavage and Polyadenylation Specificity Factor 6 (CPSF6) Subunit of the Capsid-recruited Pre-messenger RNA Cleavage Factor I (CFIm) Complex Mediates HIV-1 Integration into Genes.Restrictive influence of SAMHD1 on Hepatitis B Virus life cycle.HIV-2 and SIVmac accessory virulence factor Vpx down-regulates SAMHD1 enzyme catalysis prior to proteasome-dependent degradation Interferon regulatory factor 3 is a key regulation factor for inducing the expression of SAMHD1 in antiviral innate immunity.Deoxynucleoside triphosphate (dNTP) synthesis and destruction regulate the replication of both cell and virus genomes.Effects of T592 phosphomimetic mutations on tetramer stability and dNTPase activity of SAMHD1 can not explain the retroviral restriction defect.Restriction of virus infection but not catalytic dNTPase activity is regulated by phosphorylation of SAMHD1.Antagonism of SAMHD1 is actively maintained in natural infections of simian immunodeficiency virus

P2860

Q21131105-B806B736-4009-4756-982C-6F08FFA1E2BD Q24338757-8034A340-FABD-4927-80A3-E72E15F269B4 Q24339547-687C5F71-E132-4710-A559-A5EB953AC628 Q26738747-B8A63E3D-7F18-4FBA-8A72-24F3FA2322A0 Q27680878-6DDF938C-0C25-4FA7-B6BE-3CD5FA794265 Q27680881-B5DA4F30-DC60-47E8-B5C0-7ADE6567A01D Q27698300-D0D77F58-DC73-4635-BB38-3ADD62EC3C36 Q28073284-A5ACB95A-6702-48FC-A7A7-589085D2BB3E Q29147390-638D67AE-F78C-43B1-9A90-C410416C6EBE Q33606917-F8D3C4D2-3D74-4ACF-B495-23DEEAE8EDA2 Q33911427-650962BF-29BF-4CE1-967C-5F7C61C15EA1 Q34058270-21854975-8790-482B-8614-B4A6891AEF50 Q34169187-06ACE567-48A3-4099-BA48-E75B1F038508 Q34383850-150EC527-374E-40AB-BFFE-D4FE7CA40CA0 Q34399058-FFE32120-41ED-4301-BC4A-902EED59CC9E Q34444278-D0FCA89E-229E-4B29-85C3-4D1116C9C1B7 Q34542134-D342220F-B446-4A41-9F10-3EB06FF65FB4 Q34547626-CC964351-F23D-47E8-BDAE-6C206F01BEEA Q34548496-E1235C24-869C-4606-B725-D32479A9807F Q34552616-7E50C1DF-DC57-4C18-9D8D-85DC94411C5F Q34795512-F6DA098D-5982-4284-A1DF-47F2150FB806 Q34845553-4D94AB5C-372E-4311-95F4-04BBBBC6D81C Q34846363-0D0C7D66-683B-4646-866D-570806445006 Q35451250-51C7AE4E-89B8-4501-B95B-CFD78EAB3A64 Q35670483-4359E1DD-7950-47FD-BFAF-A40CEEBF8FB1 Q35796953-3E34EFEB-5134-4D54-8520-5D6190F23F63 Q35860974-E08922A4-37F5-431D-BEA0-4DB5005FE7D1 Q35885990-85B1C88D-CCA2-4A83-9585-67BC2BEB0AEA Q36283619-EF653219-29FE-460C-9287-70728DFB336B Q36343183-97C35517-A493-4BF2-BAB2-5701D30DAFAA Q36444075-0FB95AC7-0E4F-44F0-BEC0-FF7F67D97601 Q36866147-DBC13B40-A9F2-4672-BA30-1F8E69686525 Q36941113-4D29D438-020F-43AE-9D37-EE2D9EBF3C85 Q36941510-520853C5-4E85-4046-8339-516A0B5DA5A0 Q36967370-D0AE8155-8A37-4B55-A023-3485389811CC Q37093160-CA4D5D7D-7E4D-461C-8FAA-8BC316C41D01 Q37143440-D86CB18B-DED9-49CC-A524-DAF6D4DCA00B Q37166784-65BFDDA4-42F7-4874-85F4-462C3A478B03 Q37252735-10C0088E-F1D3-40DE-8708-776FBD33E5E9 Q37421230-CFFE215E-F513-4D7D-8061-0A4A0B827B03

P2860

Tetramerization of SAMHD1 is required for biological activity and inhibition of HIV infection

http://www.wikidata.org/entity/Q24634238

description

2013 nî lūn-bûn

@nan

2013 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

Tetramerization of SAMHD1 is r ...... nd inhibition of HIV infection

@ast

Tetramerization of SAMHD1 is r ...... nd inhibition of HIV infection

@en

Tetramerization of SAMHD1 is r ...... nd inhibition of HIV infection

@nl

type

label

Tetramerization of SAMHD1 is r ...... nd inhibition of HIV infection

@ast

Tetramerization of SAMHD1 is r ...... nd inhibition of HIV infection

@en

Tetramerization of SAMHD1 is r ...... nd inhibition of HIV infection

@nl

prefLabel

Tetramerization of SAMHD1 is r ...... nd inhibition of HIV infection

@ast

Tetramerization of SAMHD1 is r ...... nd inhibition of HIV infection

@en

Tetramerization of SAMHD1 is r ...... nd inhibition of HIV infection

@nl

P1433

Q24634238-891CECFE-2AFF-449B-919A-17BDD636C9E1

P1476

Q24634238-5C35A770-F260-4729-BBA6-A3749E391D6B

P2093

Q24634238-03B051A6-EC9E-440E-921C-A2B800204A68

Q24634238-317B6E04-4B5A-42BC-87B9-762B4A23A729

Q24634238-52EA9CA8-22D3-4D6D-BA16-1B6286D6309B

Q24634238-620D73B2-2755-4463-BC68-A38E2929EFC0

Q24634238-62A85F5A-CE5E-4D3B-A9B7-507DCD980925

Q24634238-75F42CA0-9875-447C-82C0-03D91C45E473

Q24634238-C2E73F0D-490C-4E3D-AB2B-A7CA87F3F241

Q24634238-F5058F97-1433-4506-AE76-DDE664D6C936

Q24634238-F8D5E6FE-0CBB-4D6A-86F8-225573655F29

P2860

Q24634238-01D4359A-939F-4B31-B629-8F0661F3CE63

Q24634238-0605F9F3-35B3-4A4E-9190-D0F98D0CF03D

Q24634238-131D7FB8-D08D-498F-83D9-56CD1541490E

Q24634238-144FF8A4-CDFC-4020-BC1A-DA8FE23B993C

Q24634238-2941EA3E-6B51-48AE-92CF-4592B9BB5CB7

Q24634238-2E7ECD85-70C1-45F2-9CFA-3000E23A814F

Q24634238-3E64B5C0-F50D-49AC-9C14-E85F72A3FC17

Q24634238-43268B6C-88CC-4060-92B3-5860CE32BF97

Q24634238-45070B54-D0E8-43F8-9889-098C785F9DFD

Q24634238-4715EED9-B42F-4708-A778-3724E577DEE5

P304

Q24634238-003A3687-FF91-401A-939A-72A107F36A49

P31

Q24634238-97308092-DC4E-470E-A580-C31F1F0A1820

P3181

Q24634238-D7080AEE-9CB2-4692-BE96-C80C1E114470

P356

Q24634238-6487AA6B-4380-4D48-AA7D-60A2FF8BFDE4

P407

Q24634238-CB0A34D8-021A-4C79-811A-AE4CEF8BC5B5

P433

Q24634238-6BDA759E-08C5-4590-90BB-2C9DCFD00A96

P478

Q24634238-4816A788-A5BC-4CEB-8640-1473B6003D17

P50

Q24634238-9817C636-8C25-4FDA-9463-58F5FB8FD54F

Q24634238-F9080992-77E6-4004-93AC-DDDA74212693

P577

Q24634238-9936EDAF-B3A6-4625-AF60-71134C6864EF

P698

Q24634238-E221B217-762B-4918-BA65-E3B9A39A6D4F

P921

Q24634238-6FB71C84-A53B-4C53-8CC7-F6D243230623

P932

Q24634238-DF17C13E-FC83-4B8B-B308-78B2A0938C13

P3181

P356

JBC.M112.443796

P1433

Journal of Biological Chemistry

P1476

Tetramerization of SAMHD1 is r ...... nd inhibition of HIV infection

@en

P2093

Caili Hao

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

Chuanping Wang

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

Jacek Skowronski

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

Jennifer Mehrens

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

Jinwoo Ahn

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

Junpeng Yan

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

Marcin Golczak

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

Maria DeLucia

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

Sarabpreet Kaur

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

P2860

SAMHD1-deficient CD14+ cells from individuals with Aicardi-Goutières syndrome are highly susceptible to HIV-1 infection

HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis

Mutations involved in Aicardi-Goutières syndrome implicate SAMHD1 as regulator of the innate immune response

Evolutionary and functional analyses of the interaction between the myeloid restriction factor SAMHD1 and the lentiviral Vpx protein

SAMHD1 is the dendritic- and myeloid-cell-specific HIV-1 restriction factor counteracted by Vpx

SAMHD1 restricts HIV-1 reverse transcription in quiescent CD4(+) T-cells

SAMHD1 restricts the replication of human immunodeficiency virus type 1 by depleting the intracellular pool of deoxynucleoside triphosphates

Vpx relieves inhibition of HIV-1 infection of macrophages mediated by the SAMHD1 protein

Aicardi-Goutieres syndrome and related phenotypes: linking nucleic acid metabolism with autoimmunity

Lentiviral Vpr usurps Cul4-DDB1[VprBP] E3 ubiquitin ligase to modulate cell cycle

P304

10406-17

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

P31

scholarly article

P3181

1230276

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

P356

10.1074/JBC.M112.443796

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

P407

P433

15

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

P478

288

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

P50

Angela M Gronenborn

Krzysztof Palczewski

P577

2013-04-12T00:00:00Z

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

P698

23426366

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

P921

P932

3624423

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