NMR-based homology model for the solution structure of the C-terminal globular domain of EMILIN1 (Q27652968)

Federico Fogolari

8

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Alfonso Colombatti

Alfonso Colombatti

10

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Paolo Viglino

9

Paolo Viglino

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Giuliana Verdone

1

Giuliana Verdone

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Daniel O Cicero

4

Daniel Cicero

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Tommaso Eliseo

5

Tommaso Eliseo

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author name string

Simon A Colebrooke

3

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Jonathan Boyd

6

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Roberto Doliana

7

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Iain D Campbell

11

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Gennaro Esposito

12

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language of work or name

1 reference

February 2009

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number of pages

18

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Journal of Biomolecular NMR

inferred from page(s)

published in

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volume

43

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issue

2

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page(s)

79-96

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Molecular cloning and characterization of EndoGlyx-1, an EMILIN-like multisubunit glycoprotein of vascular endothelium

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Emilin1 deficiency causes structural and functional defects of lymphatic vasculature.

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The solution structure of EMILIN1 globular C1q domain reveals a disordered insertion necessary for interaction with the alpha4beta1 integrin

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Isolation and characterization of EMILIN-2, a new component of the growing EMILINs family and a member of the EMI domain-containing superfamily

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Emilin1 links TGF-beta maturation to blood pressure homeostasis

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Sequence-specific backbone NMR assignments for the C-terminal globular domain of EMILIN-1.

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