T Cell/Transmembrane, Ig, and Mucin-3 Allelic Variants Differentially Recognize Phosphatidylserine and Mediate Phagocytosis of Apoptotic Cells - Wikidata - awgldk - TriplyDB

T Cell/Transmembrane, Ig, and Mucin-3 Allelic Variants Differentially Recognize Phosphatidylserine and Mediate Phagocytosis of Apoptotic Cells

T Cell/Transmembrane, Ig, and Mucin-3 Allelic Variants Differentially Recognize Phosphatidylserine and Mediate Phagocytosis of Apoptotic Cells

http://www.wikidata.org/entity/Q27659032

about

TIM-family proteins promote infection of multiple enveloped viruses through virion-associated phosphatidylserine Human CD300a binds to phosphatidylethanolamine and phosphatidylserine, and modulates the phagocytosis of dead cells Immune Regulation and Antitumor Effect of TIM-1 TIM-3 Regulates Distinct Functions in Macrophages Host nucleotide polymorphism in hepatitis B virus-associated hepatocellular carcinoma Phosphatidylserine is a global immunosuppressive signal in efferocytosis, infectious disease, and cancer Focus on Extracellular Vesicles: Introducing the Next Small Big Thing Beyond CTLA-4 and PD-1, the Generation Z of Negative Checkpoint Regulators Phosphatidylserine receptors: enhancers of enveloped virus entry and infection Adaptive resistance to therapeutic PD-1 blockade is associated with upregulation of alternative immune checkpoints.Tumor-infiltrating DCs suppress nucleic acid-mediated innate immune responses through interactions between the receptor TIM-3 and the alarmin HMGB1 Apoptotic cells activate NKT cells through T cell Ig-like mucin-like-1 resulting in airway hyperreactivity Tim-3 directly enhances CD8 T cell responses to acute Listeria monocytogenes infection Characterizing functional domains for TIM-mediated enveloped virus entry Beginnings of a good apoptotic meal: the find-me and eat-me signaling pathways Find-me and eat-me signals in apoptotic cell clearance: progress and conundrums.Natural killer cell function and dysfunction in hepatitis C virus infection.Tim-3 and its role in regulating anti-tumor immunity.Regulation of T cell responses by the receptor molecule Tim-3.Antagonism of TIM-1 blocks the development of disease in a humanized mouse model of allergic asthma.Control of signaling-mediated clearance of apoptotic cells by the tumor suppressor p53 Rubella virus: first calcium-requiring viral fusion protein.TIM-3 does not act as a receptor for galectin-9.TIM-4, a receptor for phosphatidylserine, controls adaptive immunity by regulating the removal of antigen-specific T cells.Distinct role of Tim-3 in systemic lupus erythematosus and clear cell renal cell carcinoma Tim-3 is an inducible human natural killer cell receptor that enhances interferon gamma production in response to galectin-9 Tim-3 marks human natural killer cell maturation and suppresses cell-mediated cytotoxicity.Galectin-9 binding to Tim-3 renders activated human CD4+ T cells less susceptible to HIV-1 infection Distinct Trafficking of Cell Surface and Endosomal TIM-1 to the Immune Synapse.Preparation and characterization of a novel nanobody against T-cell immunoglobulin and mucin-3 (TIM-3).The Tim3-galectin 9 pathway induces antibacterial activity in human macrophages infected with Mycobacterium tuberculosis TIM-3 regulates innate immune cells to induce fetomaternal tolerance.Characterization of Human and Murine T-Cell Immunoglobulin Mucin Domain 4 (TIM-4) IgV Domain Residues Critical for Ebola Virus Entry.Role of the phosphatidylserine receptor TIM-1 in enveloped-virus entry.Calcium-Dependent Rubella Virus Fusion Occurs in Early Endosomes G protein α12 (Gα12) is a negative regulator of kidney injury molecule-1-mediated efferocytosis.Costimulatory genes: hotspots of conflict between host defense and autoimmunity.Genetic polymorphisms of immune checkpoint proteins PD-1 and TIM-3 are associated with survival of patients with hepatitis B virus-related hepatocellular carcinoma.Molecular mechanism for differential recognition of membrane phosphatidylserine by the immune regulatory receptor Tim4.Role of phosphatidylserine receptors in enveloped virus infection.

P2860

Q21131381-6BAF6DF6-2B17-4127-AE52-4DD195F451AE Q24304296-5251B9E2-DE58-41E8-8549-17DB352427FD Q26740298-2F31CB7A-64F1-4858-BAD5-CC14F3D6C8C5 Q26744557-9E7060DB-4F47-4DF4-9A70-4E7EDE522D8F Q26750792-8EF34163-1999-4626-BBA7-702742E2EFAE Q26766332-4B0B360D-6ADD-4D5E-A97C-E95857C5B08E Q26767273-01C12691-2488-4069-A820-DF1A9084079E Q26782799-0EB5C873-A872-4587-BA5B-C8DC6D4A481D Q27015034-B41C8DB8-D9CA-4347-85D3-D2F9A8987D27 Q27853339-B27EF150-CE52-4B6C-A72E-966BE7B5BDC6 Q28116224-BEA69CA3-D0DF-403B-A8E7-6F6F14ED53E8 Q28389278-DC459EEA-9408-4497-923F-4450C6AB27A6 Q28506567-D925DAE5-6752-459F-9974-43A92E6A2A52 Q30409350-93E6D45E-331F-45BB-8588-C95413C00979 Q30424410-D0AC3E25-E9D0-4944-BACF-AB6226A065EA Q30433111-D7C78C18-852B-4E98-B15B-04BDE42714A2 Q33892695-133B2D78-A9B3-473F-8FFA-71ABA636E322 Q33909020-5B8498E0-5C3D-44AE-B4E5-BAA65C54254A Q34017074-6F5ADB56-4657-43EE-B7FE-79C63764F5DB Q34028652-E02D31D5-140F-4C6B-849B-49C0E455576E Q34487653-25A0A791-A3F1-45F8-9AB3-065B6096E249 Q34633762-1F01B444-929F-4F52-AA5E-BFB66B920004 Q34649690-953D3999-AA3C-48FF-9889-EEB81EB5B013 Q35156453-62966DC9-D291-448F-8B73-9792E8F74C70 Q35870654-FB31A9FC-6E95-4342-9FF1-B32E352A6325 Q35876978-CF22B60E-D77D-4433-852C-4EC6E2CDCB72 Q35909663-AAE11546-3588-4BE2-9C65-33515E792307 Q35986628-503222C0-604F-4943-BCBA-23EFBB6C2DF7 Q36167228-88356CF6-F84E-4BA6-9B9F-D46CC70625F8 Q36213059-DB834DF1-EAFF-4098-AF2D-776BEDA185D1 Q36451717-A4A9F6F5-A921-4DD3-AC12-137B610C07F7 Q36487481-A8419870-C9CE-45EE-AA56-75D024BCAA01 Q37002542-1F093D4F-FF88-4B40-94FA-587C8A2499C7 Q37036794-585BB963-A1D4-4502-91C7-03CF3F84320F Q37073364-3355E2EB-F447-40C0-AD06-302F6445D6FF Q37148892-5F8D9944-6317-40E5-BD44-69E2EA8583A2 Q37172174-BD40CB7E-081D-4AC1-83AD-FD88B84336A1 Q37295612-405695C0-406D-4FBA-9297-C200FC28F834 Q37711963-4D20D70A-7DA8-4CBD-814C-6C4F8E6021E5 Q37713918-BCFA6750-8295-4716-8624-05D8722BD278

P2860

T Cell/Transmembrane, Ig, and Mucin-3 Allelic Variants Differentially Recognize Phosphatidylserine and Mediate Phagocytosis of Apoptotic Cells

http://www.wikidata.org/entity/Q27659032

description

2010 nî lūn-bûn

@nan

2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

T Cell/Transmembrane, Ig, and ...... hagocytosis of Apoptotic Cells

@ast

T Cell/Transmembrane, Ig, and ...... hagocytosis of Apoptotic Cells

@en

T Cell/Transmembrane, Ig, and ...... hagocytosis of Apoptotic Cells

@nl

type

label

T Cell/Transmembrane, Ig, and ...... hagocytosis of Apoptotic Cells

@ast

T Cell/Transmembrane, Ig, and ...... hagocytosis of Apoptotic Cells

@en

T Cell/Transmembrane, Ig, and ...... hagocytosis of Apoptotic Cells

@nl

prefLabel

T Cell/Transmembrane, Ig, and ...... hagocytosis of Apoptotic Cells

@ast

T Cell/Transmembrane, Ig, and ...... hagocytosis of Apoptotic Cells

@en

T Cell/Transmembrane, Ig, and ...... hagocytosis of Apoptotic Cells

@nl

P1433

Q27659032-56495A10-EE50-4F99-AC93-74F459D4E8B8

P1476

Q27659032-70D6C0EF-0B1D-4E00-999C-89B61F1862D7

P2093

Q27659032-194326AD-E4BD-4ECA-B4F9-DEC8147F136F

Q27659032-640F0167-2549-406F-8377-1C85A176AC23

Q27659032-674F9DA7-0250-484B-B6E9-16A19EF083FC

Q27659032-795E7559-4B55-4828-8904-CAD33DD57079

Q27659032-813D0BFD-7ED2-491A-84C8-877C9926FC17

Q27659032-88B93CA6-5EFA-4047-B842-942D76C63352

Q27659032-AB7F3800-C05F-40A1-97D6-D2808040F477

Q27659032-AD51B47D-65FD-40F5-842D-358201C4E9A6

Q27659032-C1968A7B-9E29-430F-8A9A-1E1E793A6146

Q27659032-C90A4505-5D7A-4D93-AAC1-85F919B713F4

P2860

Q27659032-034994B7-796A-468F-AB5B-DC3DE8BDCDAD

Q27659032-05A58C58-1DB4-478F-A220-1631C83D7EB7

Q27659032-07097228-6BF4-4D34-96B7-9118158299C9

Q27659032-07B640C5-4A7C-40E1-936A-4C5B4787A24C

Q27659032-095E9173-6B04-42EF-AD59-7ABE4E5FBA76

Q27659032-099641A0-8556-40A6-9A65-FB1AF21FA9D7

Q27659032-0C95CB8D-93A5-4007-87C5-289B1A6675D5

Q27659032-0EDDF035-FBD1-4AE0-8C17-39A12629AEA1

Q27659032-14470DA7-02A3-444C-A991-76FE0BFA0785

Q27659032-15E4AED2-E60A-40DF-B65D-6BD89A4C2995

P304

Q27659032-1F23D694-5150-4731-9FE7-42E44E2C7B84

P31

Q27659032-5D974227-4D42-4B6C-AD6A-6503F25C1DFB

P3181

Q27659032-EE56A223-AE89-4670-A9EB-B7B65D3F6931

P356

Q27659032-AD06F0EA-2602-492F-9779-7E53D47039A5

P407

Q27659032-4B98A99E-9EEF-4A76-B939-7A1FCB22BD8C

P433

Q27659032-63C9C32D-B17D-4AF9-B89A-8727DBDE683D

P478

Q27659032-B2A4D197-9639-4539-8066-EEE0D5E1763A

P577

Q27659032-75A24634-CD77-41D1-A40A-A5B4202AAFE9

P5875

Q27659032-D2F60195-DB12-4C5E-B6F6-0E5145549683

P698

Q27659032-8BC72531-8443-4566-AB62-3C9193A4A562

P921

Q27659032-81CC5D8D-8C7E-437E-9596-15DF80D4EF09

Q27659032-88CD67E6-54B9-496C-B65B-1032057EF754

Q27659032-AB7CB0B4-DC9B-43AB-95BA-4A3D71316472

P932

Q27659032-48F75730-FA3E-493B-ABD1-FCE1231FEDF0

P3181

P356

JIMMUNOL.0903059

P1433

Journal of Immunology

P1476

T Cell/Transmembrane, Ig, and ...... hagocytosis of Apoptotic Cells

@en

P2093

Angela Ballesteros

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

César Santiago

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

Dale T Umetsu

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

Gerardo G Kaplan

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

Gordon J Freeman

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

Hyun-Hee Lee

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

José M Casasnovas

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

Muriel Pichavant

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

Piia Karisola

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

Rosemarie H DeKruyff

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

P2860

TIM-1 and TIM-4 glycoproteins bind phosphatidylserine and mediate uptake of apoptotic cells.

Mechanisms of phosphatidylserine exposure, a phagocyte recognition signal, on apoptotic T lymphocytes

Ca(2+) bridges the C2 membrane-binding domain of protein kinase Calpha directly to phosphatidylserine

Structures of T Cell immunoglobulin mucin receptors 1 and 2 reveal mechanisms for regulation of immune responses by the TIM receptor family

T cell immunoglobulin mucin-3 crystal structure reveals a galectin-9-independent ligand-binding surface

Structures of T Cell Immunoglobulin Mucin Protein 4 Show a Metal-Ion-Dependent Ligand Binding Site where Phosphatidylserine Binds

Phasercrystallographic software

Promotion of tissue inflammation by the immune receptor Tim-3 expressed on innate immune cells

Identification of Tapr (an airway hyperreactivity regulatory locus) and the linked Tim gene family

Immunology: hepatitis A virus link to atopic disease

P304

1918-30

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

P31

scholarly article

P3181

668773

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

P356

10.4049/JIMMUNOL.0903059

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

P407

P433

4

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

P478

184

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

P577

2010-02-15T00:00:00Z

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

P5875

41056300

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

P698

20083673

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

P921

apoptotic process

transmembrane protein

P932

3128800

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