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Literature DB >> 31594405

Structural biology of the TGFβ family.

Erich J Goebel¹, Kaitlin N Hart², Jason C McCoy¹, Thomas B Thompson¹.

Abstract

Keywords: NMR; Structural biology; X-ray crystallography; kinase; protein–protein interactions; structure function

Year: 2019 PMID： 31594405 PMCID： PMC6920667 DOI： 10.1177/1535370219880894

Source DB: PubMed Journal: Exp Biol Med (Maywood) ISSN： 1535-3699

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153 in total

1. Structural mechanism of Smad4 recognition by the nuclear oncoprotein Ski: insights on Ski-mediated repression of TGF-beta signaling.

Authors: Jia Wei Wu; Ariel R Krawitz; Jijie Chai; Wenyu Li; Fangjiu Zhang; Kunxin Luo; Yigong Shi
Journal: Cell Date: 2002-11-01 Impact factor: 41.582

2. A flexible activin explains the membrane-dependent cooperative assembly of TGF-beta family receptors.

Authors: Jason Greenwald; Mark E Vega; George P Allendorph; Wolfgang H Fischer; Wylie Vale; Senyon Choe
Journal: Mol Cell Date: 2004-08-13 Impact factor: 17.970

3. Phosphorylation of Ser465 and Ser467 in the C terminus of Smad2 mediates interaction with Smad4 and is required for transforming growth factor-beta signaling.

Authors: S Souchelnytskyi; K Tamaki; U Engström; C Wernstedt; P ten Dijke; C H Heldin
Journal: J Biol Chem Date: 1997-10-31 Impact factor: 5.157

4. Noggin, cartilage morphogenesis, and joint formation in the mammalian skeleton.

Authors: L J Brunet; J A McMahon; A P McMahon; R M Harland
Journal: Science Date: 1998-05-29 Impact factor: 47.728

5. A structural basis for mutational inactivation of the tumour suppressor Smad4.

Authors: Y Shi; A Hata; R S Lo; J Massagué; N P Pavletich
Journal: Nature Date: 1997-07-03 Impact factor: 49.962

6. GDF11 forms a bone morphogenetic protein 1-activated latent complex that can modulate nerve growth factor-induced differentiation of PC12 cells.

Authors: Gaoxiang Ge; Delana R Hopkins; Wen-Bin Ho; Daniel S Greenspan
Journal: Mol Cell Biol Date: 2005-07 Impact factor: 4.272

7. von Willebrand factor type C domain-containing proteins regulate bone morphogenetic protein signaling through different recognition mechanisms.

Authors: Jin-Li Zhang; Yi Huang; Li-Yan Qiu; Joachim Nickel; Walter Sebald
Journal: J Biol Chem Date: 2007-05-04 Impact factor: 5.157

Structural biology of the TGFβ family.

1. Structural mechanism of Smad4 recognition by the nuclear oncoprotein Ski: insights on Ski-mediated repression of TGF-beta signaling.

2. A flexible activin explains the membrane-dependent cooperative assembly of TGF-beta family receptors.

3. Phosphorylation of Ser465 and Ser467 in the C terminus of Smad2 mediates interaction with Smad4 and is required for transforming growth factor-beta signaling.

4. Noggin, cartilage morphogenesis, and joint formation in the mammalian skeleton.

5. A structural basis for mutational inactivation of the tumour suppressor Smad4.

6. GDF11 forms a bone morphogenetic protein 1-activated latent complex that can modulate nerve growth factor-induced differentiation of PC12 cells.

7. von Willebrand factor type C domain-containing proteins regulate bone morphogenetic protein signaling through different recognition mechanisms.

8. Molecular recognition of BMP-2 and BMP receptor IA.

9. GARP regulates the bioavailability and activation of TGFβ.

10. Constitutively active transforming growth factor β receptor 1 in the mouse ovary promotes tumorigenesis.

1. A variant of human growth differentiation factor-9 that improves oocyte developmental competence.

2. Structural biology: Gaining atomic level insight into the biological function of macromolecules.

3. The orphan ligand, activin C, signals through activin receptor-like kinase 7.

Review 4. Molecular Mechanisms of AMH Signaling.

5. Characterization of tolloid-mediated cleavage of the GDF8 procomplex.

Review 6. Structural perspective of BMP ligands and signaling.

7. Differentiation of Murine C2C12 Myoblasts Strongly Reduces the Effects of Myostatin on Intracellular Signaling.

Review 8. Receptor binding competition: A paradigm for regulating TGF-β family action.

9. Mutational Analysis of the Putative Anti-Müllerian Hormone (AMH) Binding Interface on its Type II Receptor, AMHR2.

10. Structure of AMH bound to AMHR2 provides insight into a unique signaling pair in the TGF-β family.