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An unusual feature revealed by the crystal structure at 2.2 A resolution of human transforming growth factor-beta 2

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An unusual feature revealed by the crystal structure at 2.2 A resolution of human transforming growth factor-beta 2 (English)

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M P Schlunegger

1

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M G Grütter

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2

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language of work or name

English

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publication date

30 July 1992

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published in

Nature

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volume

358

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issue

6385

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page(s)

430-4

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cites work

The transforming growth factor-beta system, a complex pattern of cross-reactive ligands and receptors

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7 January 2021

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The transforming growth factor-beta family

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Expression cloning of the TGF-β type II receptor, a functional transmembrane serine/threonine kinase

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Wound healing in aged animals--effects of locally applied transforming growth factor beta 2 in different model systems

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Transforming growth factor-beta and the initiation of chondrogenesis and osteogenesis in the rat femur

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Complementary DNA sequences of ovarian follicular fluid inhibin show precursor structure and homology with transforming growth factor-beta

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Novel regulators of bone formation: molecular clones and activities

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Bone morphogenetic proteins.

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Crystallization and preliminary X-ray analysis of recombinant human transforming growth factor beta 2

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Solution conformation of endothelin determined by means of 1H-NMR spectroscopy and distance geometry calculations.

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Structure of the potato inhibitor complex of carboxypeptidase A at 2.5-A resolution

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Conformation of amino acid side-chains in proteins

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Expression cloning and characterization of the TGF-beta type III receptor

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Resolution of phase ambiguity in macromolecular crystallography

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Human transforming growth factor type beta 2: production by a prostatic adenocarcinoma cell line, purification, and initial characterization

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A graphics model building and refinement system for macromolecules

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Crystallographic R factor refinement by molecular dynamics

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Identification of a Novel Member (GDF-1) of the Transforming Growth Factor-β Superfamily

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Drosophila 60A gene, another transforming growth factor beta family member, is closely related to human bone morphogenetic proteins

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Identifiers

DOI

10.1038/358430A0

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Dimensions Publication ID

1002505540

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Fatcat ID

release_fes4zg4elnaonj4c5ywjhcsd2e

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PubMed ID

1641027

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Springer Nature article ID

10.1038/358430a0

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(Q28291529)

An unusual feature revealed by the crystal structure at 2.2 A resolution of human transforming growth factor-beta 2

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