Signaling inputs converge on nuclear effectors in TGF-beta signaling.
about
Molecular regulation of pancreatic stellate cell functionCloning of a novel signaling molecule, AMSH-2, that potentiates transforming growth factor beta signalingRegulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligaseInactivation of menin, a Smad3-interacting protein, blocks transforming growth factor type beta signalingTransforming growth factor-beta receptor-associated protein 1 is a Smad4 chaperoneTranscription activation of FLRG and follistatin by activin A, through Smad proteins, participates in a negative feedback loop to modulate activin A functionFunctional proteomics mapping of a human signaling pathwayFeatures of a Smad3 MH1-DNA complex. Roles of water and zinc in DNA bindingDownregulation of Ski and SnoN co-repressors by anisomycinStoichiometry of active smad-transcription factor complexes on DNAJab1 antagonizes TGF-beta signaling by inducing Smad4 degradationTransforming growth factor-beta receptors interact with AP2 by direct binding to beta2 subunitTransforming growth factor beta-mediated transcriptional repression of c-myc is dependent on direct binding of Smad3 to a novel repressive Smad binding elementTo build a synapse: signaling pathways in neuromuscular junction assemblyMowat-Wilson syndromeRegulation of Smad signaling through a differential recruitment of coactivators and corepressors by ZEB proteinsOpposing functions of ZEB proteins in the regulation of the TGFbeta/BMP signaling pathwayThe SmadsCharacterization of a novel transcriptionally active domain in the transforming growth factor beta-regulated Smad3 proteinHER-2 overexpression differentially alters transforming growth factor-beta responses in luminal versus mesenchymal human breast cancer cellsTGF-β/BMP signaling and other molecular events: regulation of osteoblastogenesis and bone formationA cytokine-neutralizing antibody as a structural mimetic of 2 receptor interactionsStructure of Smad1 MH1/DNA complex reveals distinctive rearrangements of BMP and TGF- effectorsSmad7 is induced by CD40 and protects WEHI 231 B-lymphocytes from transforming growth factor-beta -induced growth inhibition and apoptosisFLRG, an activin-binding protein, is a new target of TGFbeta transcription activation through Smad proteinsIdentification of novel isoforms of activin receptor-like kinase 7 (ALK7) generated by alternative splicing and expression of ALK7 and its ligand, Nodal, in human placentaSmad6 represses Dlx3 transcriptional activity through inhibition of DNA bindingThe Discovery and Early Days of TGF-β: A Historical PerspectiveDifferent Smad2 partners bind a common hydrophobic pocket in Smad2 via a defined proline-rich motif.A direct intersection between p53 and transforming growth factor beta pathways targets chromatin modification and transcription repression of the alpha-fetoprotein geneThe orphan receptor serine/threonine kinase ALK7 signals arrest of proliferation and morphological differentiation in a neuronal cell lineThe non-ankyrin C terminus of Ikappa Balpha physically interacts with p53 in vivo and dissociates in response to apoptotic stress, hypoxia, DNA damage, and transforming growth factor-beta 1-mediated growth suppressionBMP type I receptor ALK2 is essential for proper patterning at late gastrulation during mouse embryogenesisTransforming growth factor-beta induces nuclear import of Smad3 in an importin-beta1 and Ran-dependent mannerBMP signaling modulation attenuates cerebral arteriovenous malformation formation in a vertebrate modelFunctional cloning of the proto-oncogene brain factor-1 (BF-1) as a Smad-binding antagonist of transforming growth factor-beta signaling.A novel transforming growth factor-beta receptor-interacting protein that is also a light chain of the motor protein dynein.Laminin α1 regulates age-related mesangial cell proliferation and mesangial matrix accumulation through the TGF-β pathwayMultiple myeloma disrupts the TRANCE/ osteoprotegerin cytokine axis to trigger bone destruction and promote tumor progression.Transforming growth factor beta1 (TGF-beta1) promotes endothelial cell survival during in vitro angiogenesis via an autocrine mechanism implicating TGF-alpha signaling
P2860
Q21093285-2B7D5A75-3F58-4AE2-856E-AC603242B912Q21284175-B4982238-DE34-4043-B599-3AAC0838CD4CQ24290743-75268417-137B-4A9F-A5BD-E47839094038Q24290996-35DFA7E8-091E-4870-B696-10B830085B4DQ24291004-92B2A6CE-2592-4110-95E3-49617E518ECBQ24294220-0D8BE408-7DC5-46F6-9B8C-73808B9B02C5Q24298398-294D3583-7CF2-4A1B-9065-0D357C42BF62Q24299610-F7A96FFB-2279-44C4-9A12-38765F9E88A1Q24305745-708647DE-28B3-4CF1-A4CE-8A0A9D557F3BQ24310563-B6FFF1A6-5A2E-4566-83DA-96DA2F19B22EQ24522552-D9E5F500-E66E-4460-85AC-362F1D2ED38AQ24537162-4D3DA760-5653-4C39-B79F-CCCAC6CAC362Q24629916-B639A67B-A13A-4788-A449-92DE8E253D87Q24631081-F6E2C95F-8332-4C5B-9686-65A9A828056BQ24677663-D951C4A8-B542-4814-BF6F-B80B62AC97C8Q24677861-4D22E8E6-04F5-461B-93F9-FFF4A4AE585AQ24677954-CE031500-130C-4537-89BD-C51CA013C8E9Q24805956-9477FF4B-6FA3-434D-97BE-53DEA13A2E10Q24815288-61BD9C83-4E52-4828-893D-180DCCAF67F0Q25257668-2ED472AF-3BCB-4C83-8349-24498D0CF77EQ26798172-D40101E0-7628-4C39-B838-369C9A6695CFQ27653116-7E85136F-95AB-4844-A96C-97B8153217E8Q27659721-9795BF0A-2CD9-49C0-8B03-89B91219C83AQ28139074-5577A69B-3E41-44E9-80D0-95C25EC81ABFQ28188703-2170D157-726D-412C-ABA5-E29B3AE20F37Q28212233-D1945C82-F51A-480F-BDC6-8223079FD430Q28239372-D5278BDD-6CE6-4A5A-A24F-A9410233DE5FQ28276556-AA97FA5C-D813-49BC-B8C0-38DB53EA0822Q28344738-59342612-0058-4A1D-BED2-AFF4E8D3479EQ28507391-85B5B81F-E850-424F-85B2-A79612DFE96DQ28567347-AF62D990-B402-45FC-920F-0507B6DF07F1Q28585698-F3542652-42E7-4AE3-9337-09F6BD37AD00Q28586330-A980E79B-DEAF-43E7-8554-A58F9482B471Q28608967-39A03A14-3D1A-4863-962F-E812BFFACCC6Q30609102-19B90466-56BE-4A46-8BA3-A663AE258606Q30700260-254B1F42-66F2-4DD9-BBFF-AD3BBDAB3D1FQ30873808-99400F8F-E963-42DB-9C72-D9C1EA1FCE84Q33708674-1FBFE691-8066-4253-AE13-7DEEFDCA1CD8Q33944735-699E912D-D812-4519-82FE-E73C1F078CC1Q34012586-D9D3FDDC-6C66-4985-8365-31E8B8D21AB0
P2860
Signaling inputs converge on nuclear effectors in TGF-beta signaling.
description
2000 nî lūn-bûn
@nan
2000 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年学术文章
@wuu
2000年学术文章
@zh-cn
2000年学术文章
@zh-hans
2000年学术文章
@zh-my
2000年学术文章
@zh-sg
2000年學術文章
@yue
name
Signaling inputs converge on nuclear effectors in TGF-beta signaling.
@ast
Signaling inputs converge on nuclear effectors in TGF-beta signaling.
@en
type
label
Signaling inputs converge on nuclear effectors in TGF-beta signaling.
@ast
Signaling inputs converge on nuclear effectors in TGF-beta signaling.
@en
prefLabel
Signaling inputs converge on nuclear effectors in TGF-beta signaling.
@ast
Signaling inputs converge on nuclear effectors in TGF-beta signaling.
@en
P2093
P1476
Signaling inputs converge on nuclear effectors in TGF-beta signaling.
@en
P2093
Miyazono K
ten Dijke P
P356
10.1016/S0968-0004(99)01519-4
P577
2000-02-01T00:00:00Z