Transforming growth factor beta 1: three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor beta 2 - Wikidata - awgldk - TriplyDB

Transforming growth factor beta 1: three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor beta 2

Transforming growth factor beta 1: three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor beta 2

http://www.wikidata.org/entity/Q27733133

about

The CCN family of proteins: structure-function relationships Oligomeric interactions of TGF-β and BMP receptors Structures of an ActRIIB:activin A complex reveal a novel binding mode for TGF-beta ligand:receptor interactions A cytokine-neutralizing antibody as a structural mimetic of 2 receptor interactions Ternary Complex of Transforming Growth Factor- 1 Reveals Isoform-specific Ligand Recognition and Receptor Recruitment in the Superfamily Crystal structure of a coagulogen, the clotting protein from horseshoe crab: a structural homologue of nerve growth factor Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP-2 Real-time monitoring of the interactions of transforming growth factor-beta (TGF-beta ) isoforms with latency-associated protein and the ectodomains of the TGF-beta type II and III receptors reveals different kinetic models and stoichiometries of bi The effects of immunizing sheep with different BMP15 or GDF9 peptide sequences on ovarian follicular activity and ovulation rate Modern pathogenetic concepts of liver fibrosis suggest stellate cells and TGF-beta as major players and therapeutic targets An engineered transforming growth factor β (TGF-β) monomer that functions as a dominant negative to block TGF-β signaling Peptide ligands that use a novel binding site to target both TGF-β receptors.Medical applications of transforming growth factor-beta Bioactive TGF-beta can associate with lipoproteins and is enriched in those containing apolipoprotein E3.The transforming growth factor-betas: structure, signaling, and roles in nervous system development and functions.Molecular regulation of contractile smooth muscle cell phenotype: implications for vascular tissue engineering.Engineering fibrin-binding TGF-β1 for sustained signaling and contractile function of MSC based vascular constructs DynaFace: Discrimination between Obligatory and Non-obligatory Protein-Protein Interactions Based on the Complex's Dynamics.Molecular recognition in bone morphogenetic protein (BMP)/receptor interaction.The role of proteins of the transforming growth factor-beta superfamily in the intraovarian regulation of follicular development.The biology of activin: recent advances in structure, regulation and function Proteins on the catwalk: modelling the structural domains of the CCN family of proteins.Structural studies of the TGF-βs and their receptors - insights into evolution of the TGF-β superfamily.A soluble transforming growth factor-beta (TGF-beta ) type I receptor mimics TGF-beta responses.Inhibition of S-Adenosylmethionine-Dependent Methyltransferase Attenuates TGFβ1-Induced EMT and Metastasis in Pancreatic Cancer: Putative Roles of miR-663a and miR-4787-5p.Production, Isolation, and Structural Analysis of Ligands and Receptors of the TGF-β Superfamily.Structural Biology and Evolution of the TGF-β Family TGF-β1 conjugated to gold nanoparticles results in protein conformational changes and attenuates the biological function.Modulation of the functional binding sites for TGF-beta on the type II receptor leads to suppression of TGF-beta signaling.The tryptophan-rich motifs of the thrombospondin type 1 repeats bind VLAL motifs in the latent transforming growth factor-beta complex.The expression and antigenicity identification of recombinant rat TGF-beta1 in bacteria.An active site of transforming growth factor-beta(1) for growth inhibition and stimulation.Mutational analysis of a transforming growth factor-beta receptor binding site.Primary structure requirements for Xenopus nodal-related 3 and a comparison with regions required by Xenopus nodal-related 2.First structural glimpse of CCN3 and CCN5 multifunctional signaling regulators elucidated by small angle x-ray scattering.Pressuromodulation at the cell membrane as the basis for small molecule hormone and peptide regulation of cellular and nuclear function Biological activity differences between TGF-β1 and TGF-β3 correlate with differences in the rigidity and arrangement of their component monomers.Structures of a pan-specific antagonist antibody complexed to different isoforms of TGFβ reveal structural plasticity of antibody-antigen interactions.pH modulates the TGF-β ligands binding to the receptors: a computational analysis.Transforming growth factor-β gene silencing using adenovirus expressing TGF-β1 or TGF-β2 shRNA.

P2860

Q24658424-601B31BA-2263-460F-B880-E4BD9635C34E Q27023170-80151078-2299-464C-B9B6-64BFEDE1C568 Q27640830-14F2D536-3692-4D90-9CA8-84FF2ABFEB2F Q27653116-852F6316-1832-4038-B881-8DE39078304D Q27660131-8C9CFC1C-1074-45DD-9AF3-7C5681537D44 Q27734652-AF6B68C9-9DC3-4416-9289-5FED1CAD9E30 Q28145537-3200584D-469C-4D0D-BFA4-3A00BA05AD8B Q28198041-FE03EB6C-4A55-4AF0-AE5C-305F01A260C1 Q28273199-00162553-973F-4B6A-AF65-9EDF2F790BA8 Q28303698-7DE64800-32BA-43F8-805A-CF19157301A7 Q33615675-673D6899-025B-48E0-BC90-2AAEF892C135 Q33708971-DC664D2B-1523-4894-9063-830F23122FA7 Q33723271-59274FE1-97DF-4807-BD1C-4A055BF2A1AC Q34043609-8AB81887-0E52-4AD3-B2E4-305B2470EAAB Q34083587-24BDE03A-081C-460B-95F8-36E8666D232B Q34146262-13DC203C-B7B5-40C7-A1EF-C88335C8403C Q35223959-A944511B-E61A-4C18-A3BE-A9E2184747A0 Q35822949-468782DB-36B2-4B27-81BE-CD262B81F912 Q35902283-23067C19-2DE4-4960-9ED4-0F42ABC2EF02 Q36038023-6775EE1C-08E0-4984-9D2C-DEF0FF6154E3 Q37247171-666FBBA4-30F6-49C8-B0C2-48FC544C8F2E Q37474542-6F3A798E-27FD-49BF-8BDC-4D5937380C40 Q38014989-4365308F-D806-4D3F-9460-6083FCBE192A Q38297197-B93DAF5F-7FBC-48DB-B0ED-575145F74111 Q38733932-ECD2A5C5-07BA-4611-A491-1E024A5C03E0 Q38823276-4B19380A-01C1-48BB-BB03-F813C1D440F6 Q38957057-A257147A-DD9A-4027-A730-E11F639312DD Q39207556-D638F9CD-BB5E-4AF8-A8A1-B53F6BB518ED Q40200583-B1E02765-44E6-42C3-9991-3540DC494DD5 Q40519781-2B20A62F-1439-47D0-A8DF-35950BAEAE1F Q40697063-F3949231-066C-4985-902D-B97256941C8B Q40928797-71F7A6F8-4F11-4CFA-8512-B10CB27D4103 Q41046801-3051B211-5CCC-4182-A62B-987AD7AF0B7C Q41734440-EE085D42-0F16-4C3F-A072-B0750AD82F5E Q41900588-D433D1D7-ABF6-40C5-A972-F06D495CF385 Q42153567-1BFA740F-FA8A-4D9F-A9DA-C03BA12C1E8A Q42546368-9E92E709-FEE5-4305-94BF-4ECA71BD9C87 Q42551215-B61723F3-F42D-427B-904C-CCAB90FA31BC Q42669680-C2DA0B37-9C5D-4DA7-B57A-F5DC5E928841 Q43727484-21F73D8C-94D2-44ED-A0D0-B03EDD5E6903

P2860

Transforming growth factor beta 1: three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor beta 2

http://www.wikidata.org/entity/Q27733133

description

1996 nî lūn-bûn

@nan

1996 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

1996 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

1996年の論文

@ja

1996年論文

@yue

1996年論文

@zh-hant

1996年論文

@zh-hk

1996年論文

@zh-mo

1996年論文

@zh-tw

1996年论文

@wuu

name

Transforming growth factor bet ...... nsforming growth factor beta 2

@ast

Transforming growth factor bet ...... nsforming growth factor beta 2

@en

Transforming growth factor bet ...... nsforming growth factor beta 2

@nl

type

label

Transforming growth factor bet ...... nsforming growth factor beta 2

@ast

Transforming growth factor bet ...... nsforming growth factor beta 2

@en

Transforming growth factor bet ...... nsforming growth factor beta 2

@nl

prefLabel

Transforming growth factor bet ...... nsforming growth factor beta 2

@ast

Transforming growth factor bet ...... nsforming growth factor beta 2

@en

Transforming growth factor bet ...... nsforming growth factor beta 2

@nl

P1433

Q27733133-D51EC4C0-13EF-403B-BA93-504E59D7F710

P1476

Q27733133-81D55359-5396-471A-AA56-EB25F5CD7CD9

P2093

Q27733133-13512F9A-EB8B-4C6E-84A9-F63CC1FC399B

Q27733133-2510DC3C-5B8E-4966-B981-7BDD80D64AE8

Q27733133-3D91B30E-62E8-4214-B7D5-F8059776A3A4

Q27733133-47022778-8FCD-4F8A-BB3F-20E2CC3DC8F0

Q27733133-4F360555-FB9C-4B20-83E8-62007ABA238B

Q27733133-922C8C43-2D2B-408F-B114-99C9EE85FE4B

Q27733133-9EC70A9F-F14C-4C45-BA1F-52DB001A0A06

Q27733133-B0720098-CF25-44BF-9F3C-283FD1BC2182

Q27733133-B33423DC-A9F1-401B-8BD5-1A987328BCE3

Q27733133-E2AB79A8-15C9-48E9-B4AC-89B3587F4F09

P304

Q27733133-1705C475-1ACB-42D4-8939-A4D975B188B5

P31

Q27733133-FADC089D-D847-40AC-B28B-15051A12FA14

P356

Q27733133-B17D5685-4242-488E-A634-2D06A2EE29F2

P407

Q27733133-8270C2C5-A0D5-470B-8CAC-7F6B42C54451

P433

Q27733133-6F0881AE-472A-4B95-9E6D-10C8324AF837

P478

Q27733133-51C0EFAF-611C-4C51-AB46-8BD57D742222

P577

Q27733133-D34A45C8-BEAE-452C-B160-A267BC72F3C4

P698

Q27733133-C279386E-7B50-40FD-A9CA-2A03BB25B842

P356

P1433

P1476

Transforming growth factor bet ...... nsforming growth factor beta 2

@en

P2093

A B Roberts

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

A P Hinck

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

B L Zhang

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

D A Torchia

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

J A Weatherbee

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

J Wenker

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

M B Sporn

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

M L Tsang

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

R Lucas

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

S J Archer

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

P304

8517-34

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

P31

scholarly article

P356

10.1021/BI9604946

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

P407

P433

26

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

P478

35

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

P577

1996-07-02T00:00:00Z

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

P698

8679613

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