HIV-1 infection through the CCR5 receptor is blocked by receptor dimerization. - Wikidata - awgldk - TriplyDB

HIV-1 infection through the CCR5 receptor is blocked by receptor dimerization.

HIV-1 infection through the CCR5 receptor is blocked by receptor dimerization.

http://www.wikidata.org/entity/Q35110857

about

CCR5 monoclonal antibodies for HIV-1 therapy Stoichiometry of envelope glycoprotein trimers in the entry of human immunodeficiency virus type 1 Multiple active states and oligomerization of CCR5 revealed by functional properties of monoclonal antibodies.Chemokine receptor oligomerization and allostery.Viral exploitation and subversion of the immune system through chemokine mimicry.Ligand binding to somatostatin receptors induces receptor-specific oligomer formation in live cells.Peptide interactions with G-protein coupled receptors.Genetic variation in the CCL18-CCL3-CCL4 chemokine gene cluster influences HIV Type 1 transmission and AIDS disease progression.Heteromerization of human cytomegalovirus encoded chemokine receptors.Cell-specific RNA aptamer against human CCR5 specifically targets HIV-1 susceptible cells and inhibits HIV-1 infectivity.Cannabinoid receptor 2-mediated attenuation of CXCR4-tropic HIV infection in primary CD4+ T cells A novel synthetic bivalent ligand to probe chemokine receptor CXCR4 dimerization and inhibit HIV-1 entry.Functional and genetic analysis of coreceptor usage by dualtropic HIV-1 subtype C isolates.Long-lasting multifunctional CD8(+) T cell responses in end-stage melanoma patients can be induced by dendritic cell vaccination.Acting on Hormone Receptors with Minimal Side Effect on Cell Proliferation: A Timely Challenge Illustrated with GLP-1R and GPER Bioluminescence resonance energy transfer studies reveal constitutive dimerization of the human lutropin receptor and a lack of correlation between receptor activation and the propensity for dimerization.Modulation of chemokine receptor activity through dimerization and crosstalk Pharmacological modulation of chemokine receptor function.Mechanisms regulating chemokine receptor activity.Unique role of the chemokine domain of fractalkine in cell capture. Kinetics of receptor dissociation correlate with cell adhesion.Identification of an unique CXCR4 epitope whose ligation inhibits infection by both CXCR4 and CCR5 tropic human immunodeficiency type-I viruses.Development of a rapid cell-fusion-based phenotypic HIV-1 tropism assay Blocking HIV-1 infection via CCR5 and CXCR4 receptors by acting in trans on the CCR2 chemokine receptor.Reduced cell surface expression of CCR5 in CCR5Delta 32 heterozygotes is mediated by gene dosage, rather than by receptor sequestration.Allo-immunization elicits CCR5 antibodies, SDF-1 chemokines, and CD8-suppressor factors that inhibit transmission of R5 and X4 HIV-1 in women.Altering expression levels of human immunodeficiency virus type 1 gp120-gp41 affects efficiency but not kinetics of cell-cell fusion.Upregulation of surface feline CXCR4 expression following ectopic expression of CCR5: implications for studies of the cell tropism of feline immunodeficiency virus.Thiazolides Elicit Anti-Viral Innate Immunity and Reduce HIV Replication.Regulation of CCR7-dependent cell migration through CCR7 homodimer formation.Constitutive oligomerization of human D2 dopamine receptors expressed in Spodoptera frugiperda 9 (Sf9) and in HEK293 cells. Analysis using co-immunoprecipitation and time-resolved fluorescence resonance energy transfer.Marked structural and functional heterogeneity in CXCR4: separation of HIV-1 and SDF-1alpha responses.Two amino acid substitutions within the first external loop of CCR5 induce human immunodeficiency virus-blocking antibodies in mice and chickens.Agonist-independent and -dependent oligomerization of dopamine D(2) receptors by fusion to fluorescent proteins.Closely related, yet unique: Distinct homo- and heterodimerization patterns of G protein coupled chemokine receptors and their fine-tuning by cholesterol.

P2860

Q22242739-F92B21EA-1A1E-4B2D-976D-9FF94C2C35C3 Q30447936-ECA684A4-9368-44F7-8CA3-505678AD525B Q30857101-A2A992D9-3DF8-4FAE-9C26-EED4A0FEFADC Q33810517-33862310-DD0C-4EBD-881C-ECDF7A1EA476 Q33933260-7987CA7D-FE8E-4F99-AE19-E5B05B72791D Q34017536-DFB97151-FB40-4D81-B940-8956731BCC7A Q34483031-AEA1A23E-0130-43AD-8908-58140A990F4B Q34658462-6721B90E-EB40-4F22-BD1A-4A4CF0562A9A Q35167034-5CA5BBD3-29D8-4395-9766-5EDE76B80841 Q35205365-EF1F1F0A-2639-41E2-B528-F28B7AB3CDE8 Q35842577-6BBAABE3-EE56-4637-B597-2111D4DCF54C Q36334029-2D7991BD-35A3-4B5E-90E5-DE14DB9E3779 Q36382002-8BF5C73E-F359-4CFB-B00A-D3F1C44E5624 Q36597497-17187DDA-AF51-413B-A2C8-B56B7259D7B4 Q36800401-B1327B53-6516-4433-A8BD-47C5D6CB8409 Q37134357-57D92760-1906-4834-839F-5239975EDE99 Q37355817-5BAA5105-27C4-47BE-B051-1CB4027A1221 Q37893687-12AE4382-F28E-41B3-870B-2E1757033F13 Q37942973-62F51C29-CCFF-465B-8FFA-E05DF1DE9003 Q38309472-BAC7A25D-A769-4EC6-9CA7-FCA609D9938A Q38859512-7F36EFBE-1CAF-4CB7-834C-B01AE92556BE Q39094162-730EACF0-CE0A-44BA-846A-379CA30678ED Q39315677-94641FCE-738A-4C3F-90E6-F3A2A97B6A7B Q39556857-F873854E-9651-40F4-A8A9-8167DF2824E3 Q39577265-7B0E5F32-2A68-4C6F-BF17-7233C7C3A00E Q39682931-AE54584C-1444-4BE1-88B6-F4179BE5FF55 Q39684660-C35B4949-33D5-45BD-8AAD-F655CAF72520 Q39717911-5216E792-A5E3-4554-8F88-8C929705AEB9 Q41448192-8CB95ACA-E1DF-43E6-AF9E-525C6BD627A6 Q42046489-6DD5EDC3-F1B4-4284-B07B-CF6BA0BA0407 Q42817463-9E42BD9E-3549-44A2-9433-89AD75708991 Q43112410-6A447DC3-35D7-4111-98F8-4A004863B13C Q43780931-BCEE0492-6220-4061-A443-8BD9A9BFFA92 Q52660783-66B0C638-B94A-4E51-8C35-E909D7E0CD05

P2860

HIV-1 infection through the CCR5 receptor is blocked by receptor dimerization.

http://www.wikidata.org/entity/Q35110857

description

2000 nî lūn-bûn

@nan

2000 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի մարտին հրատարակված գիտական հոդված

@hy

2000年の論文

@ja

2000年論文

@yue

2000年論文

@zh-hant

2000年論文

@zh-hk

2000年論文

@zh-mo

2000年論文

@zh-tw

2000年论文

@wuu

name

HIV-1 infection through the CCR5 receptor is blocked by receptor dimerization.

@ast

HIV-1 infection through the CCR5 receptor is blocked by receptor dimerization.

@en

type

label

HIV-1 infection through the CCR5 receptor is blocked by receptor dimerization.

@ast

HIV-1 infection through the CCR5 receptor is blocked by receptor dimerization.

@en

prefLabel

HIV-1 infection through the CCR5 receptor is blocked by receptor dimerization.

@ast

HIV-1 infection through the CCR5 receptor is blocked by receptor dimerization.

@en

P1433

Q35110857-F1341B0A-CD07-471B-BDCE-31E938AC0D3E

P1476

Q35110857-39B10E4E-C024-47B6-B821-2A642DD0B6A7

P2093

Q35110857-12C17413-E144-4324-B7F4-59E3995567FD

Q35110857-48DEC979-C7B9-4AF9-A47D-5858774A293A

Q35110857-6E1C11BB-8E11-4C51-9DF3-554BC956B256

Q35110857-7F0863AA-7BDC-41EB-A407-44F939B8F8C7

Q35110857-C95F4754-2700-40F9-A597-587F90B4CDD4

Q35110857-F1F7932F-F6CF-4F1F-8F90-6C4B2EA8314D

P2860

Q35110857-03D7D0C8-4E72-4A1B-9053-18766162AC6A

Q35110857-1B88E399-D4E3-4A31-9F19-6F4F2B4CEC6F

Q35110857-26F39255-5F19-4D0F-95B1-9E5D04F5B288

Q35110857-2F2C2E7C-EEAB-49A4-A4E6-F1C153C35005

Q35110857-32CF2B11-4A02-41D3-A08B-BEB052593A40

Q35110857-36E919DF-F02D-4949-BA68-179BEB64AB71

Q35110857-3CD9A202-8C28-475C-8558-4233529756EE

Q35110857-42CA4532-06B6-400E-ACA0-DB3920C07786

Q35110857-444173F2-4E0C-4891-BC5C-66C216504ECF

Q35110857-4932A41D-1FFC-4A8D-BEB0-DCA4B9FE1B61

P304

Q35110857-0C8C75E4-C7B1-4DE4-87FD-1503863A3C55

P31

Q35110857-8364B791-5CF7-4186-9D3B-08FB18FFD45A

P356

Q35110857-4564643F-76F7-4B3B-B457-C68D59AF2FE8

Q35110857-5260A4A8-C093-4669-9F04-4D2C44AA7B50

P407

Q35110857-D9F27011-2564-4856-A9A3-06057DAB5DA9

P433

Q35110857-2FB8C7F6-BD5B-4DD1-8CB7-15D1DBE4DF2A

P478

Q35110857-7F507256-BCE3-40E0-B593-2861FC8948ED

P50

Q35110857-78BF935F-1D43-4292-BFE5-E6E6AFF03006

P577

Q35110857-6F7C1CB1-0605-4483-87C4-0EA466B2BA5E

P698

Q35110857-0AC56AFB-02C8-480D-A464-97EE8BE93B01

P932

Q35110857-94FEF674-FC3A-48C2-9764-0BA7F4A2832D

P356

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

HIV-1 infection through the CCR5 receptor is blocked by receptor dimerization

@en

P2093

Lucas P

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

Martín de Ana A

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

Martínez-A C

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

Rodríguez-Frade JM

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

Vila-Coro AJ

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

del Real G

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

P2860

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

A new classification for HIV-1

Monocyte chemoattractant protein-1-induced CCR2B receptor desensitization mediated by the G protein-coupled receptor kinase 2

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

The chemokine SDF-1alpha triggers CXCR4 receptor dimerization and activates the JAK/STAT pathway

CC CKR5: a RANTES, MIP-1alpha, MIP-1beta receptor as a fusion cofactor for macrophage-tropic HIV-1

Resistance to HIV-1 infection in caucasian individuals bearing mutant alleles of the CCR-5 chemokine receptor gene

Homozygous defect in HIV-1 coreceptor accounts for resistance of some multiply-exposed individuals to HIV-1 infection

Chemokines and leukocyte traffic

P304

3388-3393

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

P31

scholarly article

P356

10.1073/PNAS.050457797

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

10.1073/PNAS.97.7.3388

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

P407

P433

7

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

P478

97

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

P50

P577

2000-03-01T00:00:00Z

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

P698

10725362

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

P932

16249

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