Decreased sensitivity of tristetraprolin-deficient cells to p38 inhibitors suggests the involvement of tristetraprolin in the p38 signaling pathway - Wikidata - awgldk - TriplyDB

Decreased sensitivity of tristetraprolin-deficient cells to p38 inhibitors suggests the involvement of tristetraprolin in the p38 signaling pathway

Decreased sensitivity of tristetraprolin-deficient cells to p38 inhibitors suggests the involvement of tristetraprolin in the p38 signaling pathway

http://www.wikidata.org/entity/Q28350388

about

The tandem CCCH zinc finger protein tristetraprolin and its relevance to cytokine mRNA turnover and arthritis Cytoplasmic localization of tristetraprolin involves 14-3-3-dependent and -independent mechanisms Destabilization of vascular endothelial growth factor mRNA by the zinc-finger protein TIS11b MK2-induced tristetraprolin:14-3-3 complexes prevent stress granule association and ARE-mRNA decay Functional cloning of BRF1, a regulator of ARE-dependent mRNA turnover.The ARE-dependent mRNA-destabilizing activity of BRF1 is regulated by protein kinase B The Herpesvirus saimiri small nuclear RNAs recruit AU-rich element-binding proteins but do not alter host AU-rich element-containing mRNA levels in virally transformed T cells The roles of TTP and BRF proteins in regulated mRNA decay Chaperone Hsp27, a novel subunit of AUF1 protein complexes, functions in AU-rich element-mediated mRNA decay Tristetraprolin and its family members can promote the cell-free deadenylation of AU-rich element-containing mRNAs by poly(A) ribonuclease The control of inflammation via the phosphorylation and dephosphorylation of tristetraprolin: a tale of two phosphatases Phosphorylation of human tristetraprolin in response to its interaction with the Cbl interacting protein CIN85 ZFP36L1 is regulated by growth factors and cytokines in keratinocytes and influences their VEGF production BRF1 protein turnover and mRNA decay activity are regulated by protein kinase B at the same phosphorylation sites ZFP36L1 negatively regulates erythroid differentiation of CD34+ hematopoietic stem cells by interfering with the Stat5b pathway The p38 MAPK pathway inhibits tristetraprolin-directed decay of interleukin-10 and pro-inflammatory mediator mRNAs in murine macrophages Expression and purification of recombinant tristetraprolin that can bind to tumor necrosis factor-alpha mRNA and serve as a substrate for mitogen-activated protein kinases RNA-destabilizing factor tristetraprolin negatively regulates NF-kappaB signaling Functional analysis of KSRP interaction with the AU-rich element of interleukin-8 and identification of inflammatory mRNA targets.Phosphorylation of p40AUF1 regulates binding to A + U-rich mRNA-destabilizing elements and protein-induced changes in ribonucleoprotein structure.Regulation of A + U-rich element-directed mRNA turnover involving reversible phosphorylation of AUF1.Identification of the anti-inflammatory protein tristetraprolin as a hyperphosphorylated protein by mass spectrometry and site-directed mutagenesis Phosphorylation site analysis of the anti-inflammatory and mRNA-destabilizing protein tristetraprolin.The potential of p38 MAPK inhibitors to modulate periodontal infections.Crosstalk in inflammation: the interplay of glucocorticoid receptor-based mechanisms and kinases and phosphatases Treatment of inflammatory arthritis via targeting of tristetraprolin, a master regulator of pro-inflammatory gene expression.The MAP kinase-activated protein kinase 2 (MK2) contributes to the Shiga toxin-induced inflammatory response Identification of a major phosphopeptide in human tristetraprolin by phosphopeptide mapping and mass spectrometry.Myocardial knockdown of mRNA-stabilizing protein HuR attenuates post-MI inflammatory response and left ventricular dysfunction in IL-10-null mice.Neuronal ELAV proteins enhance mRNA stability by a PKCalpha-dependent pathway RNA-binding protein Csx1 mediates global control of gene expression in response to oxidative stress.Polyubiquitinated tristetraprolin protects from TNF-induced, caspase-mediated apoptosis Expression, purification, and biochemical characterization of the antiinflammatory tristetraprolin: a zinc-dependent mRNA binding protein affected by posttranslational modifications.Immunological characterization of tristetraprolin as a low abundance, inducible, stable cytosolic protein Negative feedback regulation of MKK6 mRNA stability by p38alpha mitogen-activated protein kinase Phosphorylation of tristetraprolin by MK2 impairs AU-rich element mRNA decay by preventing deadenylase recruitment.Mitogen-activated protein kinase-activated protein kinase 2 regulates tumor necrosis factor mRNA stability and translation mainly by altering tristetraprolin expression, stability, and binding to adenine/uridine-rich element The biosynthesis characteristics of TTP and TNF can be regulated through a posttranscriptional molecular loop Nitric oxide activation of Erk1/2 regulates the stability and translation of mRNA transcripts containing CU-rich elements p38 Mitogen-activated protein kinase-dependent and -independent signaling of mRNA stability of AU-rich element-containing transcripts

P2860

Q21195674-B5AFB4DD-3673-4399-B424-8D027DC92850 Q24292426-94926567-B958-4AD6-A83A-9DFE3008A16A Q24306395-2DFB313F-8992-4EB9-BA4D-D83CDD876072 Q24316111-7F1EDF27-74FB-484D-B1D9-E1DC75B248BE Q24534314-3438A1E0-9EDA-4D76-987B-BD5110B8F319 Q24558903-419D72EF-0C3B-4674-9815-438F23E2743C Q24567618-2B88C6AF-1476-4FEA-9C7C-5DB0E0E8722E Q24633013-A2614ACE-A3BA-4289-AE4D-6B09A4831633 Q24658102-2F2AA879-0341-437E-8727-F4E0DCD7A860 Q24673281-433139AC-10A1-4CC1-B71B-9A3FAADA1621 Q28076811-B73D44EB-515C-4DB8-9C27-68B38B4E064F Q28115076-B8F0C274-76A7-4880-8037-4E7E80BD2652 Q28115802-73878E80-B05E-4370-AD25-76FB37A372E7 Q28117267-5CDEF8BC-BAE7-4B9F-8F7B-DEE16E6D30EA Q28119162-82E3EB5A-8F75-404F-B6AD-B86FC664A8FD Q28243779-A2A18745-517D-44C7-9644-BCC8E1B90696 Q28609864-BCC1665B-0311-44ED-AA46-16A167075E13 Q30434431-DF92F997-F340-4242-8C10-51D980814A4D Q30480964-D18C93C2-BC37-4E74-A0B9-02CE6DAFCD83 Q30951116-944C5025-F1B2-4B8D-ACD9-2CC52EC2731E Q30951136-CB4706CA-A981-431F-B2E0-05D39F487C71 Q33226407-EAF12C34-5903-4795-8428-AA7920E45DFD Q33309340-F8848972-822B-47F7-804B-2344C9776564 Q33606744-9340B735-9DA4-4CDA-B5E7-0B2D035FF3E7 Q33636430-354B667E-410E-4924-B43C-9F905F31C750 Q33731727-13742C33-C6D2-401A-B78F-45466F75B2E2 Q33808280-B9E74984-9A91-4A7D-92C9-81B0597CF819 Q33881972-8EEB8E94-5F4A-4383-B727-1A2BBC3466C6 Q33919479-BCA1DA31-33CC-46EA-9181-B20219A6634C Q33922898-F1B45E3A-C4D3-4539-984E-3AB9C3E9BA44 Q34052793-D28F9EC5-E048-41C6-A331-93F8DD02B3DA Q34139073-B7B282EE-E46D-4F8E-95DF-6DB43666E845 Q34314339-F85DD9C0-ADA5-4F55-9C03-E3A2D093595D Q34314352-37D48F93-B12F-4E67-A447-60D90EADBE1B Q34462888-FDDA152B-B996-403D-98A7-A7EC62A1AD08 Q34485096-99CFFCCE-CCC3-4F2E-89AC-C458D27CE451 Q34519852-E6759A69-780F-42FD-9EF6-6A99FA08EBAD Q34536989-465F1555-1EFE-469F-B634-999019CBA57B Q34666775-69348B77-A415-46C4-AADB-1ADCE7F993D9 Q34811464-5E7311A3-0C3C-4337-958E-79EC8CF284C7

P2860

Decreased sensitivity of tristetraprolin-deficient cells to p38 inhibitors suggests the involvement of tristetraprolin in the p38 signaling pathway

http://www.wikidata.org/entity/Q28350388

description

2001 nî lūn-bûn

@nan

2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2001年の論文

@ja

2001年学术文章

@wuu

2001年学术文章

@zh-cn

2001年学术文章

@zh-hans

2001年学术文章

@zh-my

2001年学术文章

@zh-sg

2001年學術文章

@yue

name

Decreased sensitivity of trist ...... n in the p38 signaling pathway

@ast

Decreased sensitivity of trist ...... n in the p38 signaling pathway

@en

Decreased sensitivity of trist ...... n in the p38 signaling pathway

@nl

type

label

Decreased sensitivity of trist ...... n in the p38 signaling pathway

@ast

Decreased sensitivity of trist ...... n in the p38 signaling pathway

@en

Decreased sensitivity of trist ...... n in the p38 signaling pathway

@nl

prefLabel

Decreased sensitivity of trist ...... n in the p38 signaling pathway

@ast

Decreased sensitivity of trist ...... n in the p38 signaling pathway

@en

Decreased sensitivity of trist ...... n in the p38 signaling pathway

@nl

P1433

Q28350388-2AB2E9D8-F838-4AC7-8967-96861A42B469

P1476

Q28350388-0CD9187A-7717-4BD2-A2E8-125736E730A4

P2093

Q28350388-123E3691-6534-4B81-8642-17F9DBD316CE

Q28350388-14F41C69-8629-4D51-B8DF-73BE81F58B4E

Q28350388-679BC294-76DD-414F-BB39-499B92927565

Q28350388-776B4053-6436-422E-A553-7B5E26222596

Q28350388-EFCE38B7-E120-4573-B249-02AEC5CE97D3

P2860

Q28350388-018DB697-CE81-479B-89E0-F654EA7A635E

Q28350388-0ED969E8-3DC7-4666-A780-B0B1CFD445E5

Q28350388-1FAE9C4E-00A8-458D-B81A-CE8C5462D25D

Q28350388-2647EC01-DAF0-4DF9-9E78-3F3BE5B16715

Q28350388-348EACB7-15C9-44EB-932C-ED04DF237D86

Q28350388-3E69F833-1D98-4A9C-8D9F-FE88D4A1719A

Q28350388-424FB0F6-1D52-4FF5-B229-DB29C4E6B54A

Q28350388-430CD620-BB0E-4AE5-8046-5A56AB8856D0

Q28350388-4A1906D0-C12F-49DE-A9C8-3FBAEBFD5C20

Q28350388-4D6DED82-489D-48B8-939F-8257428B4AB1

P304

Q28350388-E1A9673D-9E02-4B1F-87B3-7A75F0D70DDB

P31

Q28350388-B7E6AFD9-6468-40A2-9319-6C31D5D01E69

P3181

Q28350388-A1776044-CF46-49C6-840E-362D55A3CAB0

P356

Q28350388-0B22EF88-B464-4932-9E2C-E96BF7B92E19

P407

Q28350388-451F6F31-15B4-416E-92FD-304C118161F3

P433

Q28350388-571DCB0D-D2FB-485B-B5D6-0A0B2B41C8A4

P478

Q28350388-E5B770F6-D888-4756-89F0-66134A18577E

P50

Q28350388-BC9CFA1F-59C5-42A6-AECC-4BC7B93B8E5E

P577

Q28350388-C2BB4B1D-F0A5-4D4B-B964-1395211C108A

P698

Q28350388-8BE9B0BE-1037-437B-9762-66C15F3B72E7

P921

Q28350388-67914B92-32FF-4F66-B758-0C5A4A524ADB

P932

Q28350388-309E3A46-362C-47DF-9CB9-4B3372446386

P3181

P356

P1433

Journal of Biological Chemistry

P1476

Decreased sensitivity of trist ...... n in the p38 signaling pathway

@en

P2093

D Campbell

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

E A Kennington

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

E Carballo

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

P J Blackshear

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

W S Lai

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

P2860

Evidence that tristetraprolin binds to AU-rich elements and promotes the deadenylation and destabilization of tumor necrosis factor alpha mRNA.

Interactions of CCCH zinc finger proteins with mRNA. Binding of tristetraprolin-related zinc finger proteins to Au-rich elements and destabilization of mRNA

A protein kinase involved in the regulation of inflammatory cytokine biosynthesis

Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin

The p38/RK mitogen-activated protein kinase pathway regulates interleukin-6 synthesis response to tumor necrosis factor

Novel homologues of CSBP/p38 MAP kinase: activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles

Phosphorylation of tristetraprolin, a potential zinc finger transcription factor, by mitogen stimulation in intact cells and by mitogen-activated protein kinase in vitro

A pathogenetic role for TNF alpha in the syndrome of cachexia, arthritis, and autoimmunity resulting from tristetraprolin (TTP) deficiency

MAPKAP kinase 2 is essential for LPS-induced TNF-alpha biosynthesis

TIA-1 is a translational silencer that selectively regulates the expression of TNF-alpha

P304

42580-42587

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

P31

scholarly article

P3181

3185918

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

P356

10.1074/JBC.M104953200

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

P407

P433

45

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

P478

276

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

P50

P577

2001-09-06T00:00:00Z

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

P698

11546803

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

P921

P932

1351389

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