The N-Terminal Region of Fibrillin-1 Mediates a Bipartite Interaction with LTBP1.

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The N-Terminal Region of Fibrillin-1 Mediates a Bipartite Interaction with LTBP1.

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2017 nî lūn-bûn

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The N-Terminal Region of Fibrillin-1 Mediates a Bipartite Interaction with LTBP1.

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The N-Terminal Region of Fibrillin-1 Mediates a Bipartite Interaction with LTBP1.

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The N-Terminal Region of Fibrillin-1 Mediates a Bipartite Interaction with LTBP1.

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P1476

The N-Terminal Region of Fibrillin-1 Mediates a Bipartite Interaction with LTBP1.

@en

P2093

Edward D Lowe

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Hans F Dias

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Ian B Robertson

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Isabelle H Osuch

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Penny A Handford

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P2860

Specific sequence motif of 8-Cys repeats of TGF-beta binding proteins, LTBPs, creates a hydrophobic interaction surface for binding of small latent TGF-beta

ADAMTS10 protein interacts with fibrillin-1 and promotes its deposition in extracellular matrix of cultured fibroblasts.

Differential regulation of elastic fiber formation by fibulin-4 and -5

Latent transforming growth factor beta-binding protein 1 interacts with fibrillin and is a microfibril-associated protein

MolProbity: all-atom structure validation for macromolecular crystallography

TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts

Structure and interdomain interactions of a hybrid domain: a disulphide-rich module of the fibrillin/LTBP superfamily of matrix proteins

Latent TGF-β-binding proteins

Latent TGF-β structure and activation

Structural Analysis of Collagen Type I Interactions with Human Fibronectin Reveals a Cooperative Binding Mode

P304

1208-1221.e5

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P31

scholarly article

P356

10.1016/J.STR.2017.06.003

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P433

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

P478

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P50

Sacha Jensen

Christina Redfield

P577

2017-06-21T00:00:00Z

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P698

28669633

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P932

5548924

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