Nesprin-1alpha self-associates and binds directly to emerin and lamin A in vitro (Q24303760)

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James M Holaska

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Marian S Kim

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Kenneth K Lee

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Miriam Segura-Totten

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Katherine L Wilson

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Elizabeth M McNally

Crystal structure of the repetitive segments of spectrin

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language of work or name

English

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publication date

14 August 2002

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published in

FEBS Letters

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volume

525

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issue

1-3

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page(s)

135-40

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cites work

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Solution structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil

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The spectrin repeat folds into a three-helix bundle in solution.

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Myotilin, a novel sarcomeric protein with two Ig-like domains, is encoded by a candidate gene for limb-girdle muscular dystrophy

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The interaction of titin and alpha-actinin is controlled by a phospholipid-regulated intramolecular pseudoligand mechanism

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The spectrin repeat: a structural platform for cytoskeletal protein assemblies

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Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments

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Nuclear envelope and nuclear matrix: interactions and dynamics

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Direct interaction between emerin and lamin A

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The major nuclear envelope targeting domain of LAP2 coincides with its lamin binding region but is distinct from its chromatin interaction domain

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MAN1, an inner nuclear membrane protein that shares the LEM domain with lamina-associated polypeptide 2 and emerin

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LAP2 binds to BAF.DNA complexes: requirement for the LEM domain and modulation by variable regions

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Barrier-to-autointegration factor (BAF) bridges DNA in a discrete, higher-order nucleoprotein complex

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Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy

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Missense mutations in the rod domain of the lamin A/C gene as causes of dilated cardiomyopathy and conduction-system disease

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Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B)

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Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy

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Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy

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A previously unidentified host protein protects retroviral DNA from autointegration

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NXT1 is necessary for the terminal step of Crm1-mediated nuclear export

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Structures of two repeats of spectrin suggest models of flexibility

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A new model for the interaction of dystrophin with F-actin

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In vitro expressed dystrophin fragments do not associate with each other

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10.1016/S0014-5793(02)03105-8

21 January 2018

Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

819993

819993

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Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

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