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Journal ArticleDOI

The structure and function of α-actinin

TLDR
A number of distinct isoforms of 0c-actinin have been characterized including the skeletal and smooth muscle isoforms and the non-muscle isoforms isolated from brain, macrophages, platelets, and cultured fibroblasts.
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This article is published in Journal of Muscle Research and Cell Motility.The article was published on 1989-08-01. It has received 411 citations till now. The article focuses on the topics: Actinin, alpha 1 & Actinin.

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Citations
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ACTN3 Genotype Is Associated with Human Elite Athletic Performance

TL;DR: Associations between ACTN3 genotype and athletic performance suggest that the presence of alpha-actinin-3 has a beneficial effect on the function of skeletal muscle in generating forceful contractions at high velocity, and provides an evolutionary advantage because of increased sprint performance.
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Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin.

TL;DR: Evidence is presented that in fibroblasts alpha-actinin, but not vinculin, colocalizes extensively with the N-cadherin/catenin complex, and it is proposed that cadherin / catenin complexes are linked to the actin cytoskeleton via a direct association between alpha- actinin and alpha-caten in.
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Striated muscle cytoarchitecture: an intricate web of form and function.

TL;DR: The exciting conclusion is that the striated muscle cytoskeleton, an exquisitely tuned, dynamic molecular machine, is capable of responding to subtle changes in cellular physiology.
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Competitive binding of α-actinin and calmodulin to the NMDA receptor

TL;DR: In this article, α-Actinin-2, a member of the spectrin/dystrophin family of actin-binding proteins, is identified as a brain postsynaptic density protein that colocalizes in dendritic spines with NMDA receptors and the putative NMDA receptor-clustering molecule PSD-95.
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The molecular architecture of focal adhesions

TL;DR: The present knowledge of the architecture, molecular composition, and dynamics of focal contacts of adhesive animal cells, and of possible regulatory mechanisms involving a variety of signal transduction pathways are outlined.
References
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New perspectives in cell adhesion : RGD and integrins

TL;DR: Together, the adhesion proteins and their receptors constitute a versatile recognition system providing cells with anchorage, traction for migration, and signals for polarity, position, differentiation, and possibly growth.
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The Complete Sequence of Dystrophin Predicts a Rod-Shaped Cytoskeletal Protein

TL;DR: The complete sequence of the human Duchenne muscular dystrophy cDNA has been determined and dystrophin shares many features with the cytoskeletal protein spectrin and alpha-actinin and is likely to adopt a rod shape about 150 nm in length.
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α-Actinin: Immunofluorescent localization of a muscle structural protein in nonmuscle cells

TL;DR: The results suggest that alpha-actinin may be involved in the organization ofActin filament bundles, in the attachment of actin filaments to the plasma membrane, and in the assembly of actIn filaments in areas of cell to cell contact.
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Erythrocyte spectrin is comprised of many homologous triple helical segments

TL;DR: The results suggest that most of the human erythrocyte spectrin molecule is comprised of homologous segments with a 106 amino acid length per segment, and that spectrin is not related to any other proteins whose sequence was known.
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A rapid purification of alpha-actinin, filamin, and a 130,000-dalton protein from smooth muscle.

TL;DR: Brief, low ionic strength extraction of chicken gizzard at 37 degrees C yields a solution containing a limited number of proteins including alpha-actinin, filamin, actin, desmin, and a 130,000-dalton polypeptide.
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