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Journal ArticleDOI

Biofunctionalization of a generic collagenous triple helix with the α2β1 integrin binding site allows molecular force measurements.

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TLDR
The recombinant non-hydroxylated mini-collagen, termed FC3, is produced and shows a preference for α2β1 over α1β1 integrin, especially when the chains were neither cross-linked nor prolyl-hydroxyylated, shedding light on the molecular forces of the α2 β1 Integrin-Collagen interaction, which affects tissue homeostasis by contracting the connective tissue and by contributing to interstitial tissue pressure regulation.
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This article is published in The International Journal of Biochemistry & Cell Biology.The article was published on 2011-05-01. It has received 23 citations till now. The article focuses on the topics: Integrin binding & Integrin, beta 6.

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Journal ArticleDOI

Unusual biophysics of intrinsically disordered proteins

TL;DR: In this review, some key biophysical features of IDPs are covered and it is proposed that the heterogeneous spatiotemporal structure of IDP/IDPRs can be described as a set of foldons, inducible foldon, semi-foldons, non-foldon, and unfoldons.
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Finding the weakest link: exploring integrin-mediated mechanical molecular pathways.

TL;DR: This work reconstructs the mechanical pathway followed by these forces from matrix proteins to actin through integrins and adaptor proteins, and examines which of the proteins in the network can participate in mechanotransduction and which are simply responsible for transmitting forces in a dynamic network.
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Sensing the mechano-chemical properties of the extracellular matrix.

TL;DR: Recent progress is summarized that indicates how cell adhesion, mechanotransduction and chemical signaling are coordinated in cells, and how the combination of novel experimental approaches with theoretical studies is currently utilized to unravel the molecular mechanisms governing mechano-chemical coupling during cellAdhesion.
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Integrin diversity brings specificity in mechanotransduction.

TL;DR: How the expression of particular integrin subtypes affects cellular adaptation to substrate rigidity is described and the role of integrins and associated proteins in mechanotransduction is explained, focusing on their specificity in mechanosensing and force transmission.
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Focal adhesion dynamics in cellular function and disease.

TL;DR: The major integrin adhesion complexes (IACs) characterised are focal adhesions (FAs), invadosomes (podosomes and invadopodia), hemidesmosomes (HDs) and reticular adhesion (RAs).
References
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Journal ArticleDOI

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa.

TL;DR: A discontinuous sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) system for the separation of proteins in the range from 1 to 100 kDa is described, and the omission of glycine and urea prevents disturbances which might occur in the course of subsequent amino acid sequencing.
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Biochemistry and Genetics of von Willebrand Factor

TL;DR: Growing body of information about VWF synthesis, structure, and function has allowed the reclassification of VWD based upon distinct pathophysiologic mechanisms that appear to correlate with clinical symptoms and the response to therapy.
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Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics

TL;DR: Developing a calibrated biosensor that measures forces across specific proteins in cells with piconewton (pN) sensitivity reveals that FA stabilization under force requires both vinculin recruitment and force transmission, and that, surprisingly, these processes can be controlled independently.
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Collagens, modifying enzymes and their mutations in humans, flies and worms

TL;DR: Vertebrates have at least 27 collagen types with 42 distinct polypeptide chains, >20 additional proteins with collagen-like domains and approximately 20 isoenzymes of various collagen-modifying enzymes.
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The Collagen-binding A-domains of Integrins α1β1 and α2β1Recognize the Same Specific Amino Acid Sequence, GFOGER, in Native (Triple-helical) Collagens

TL;DR: It is shown that the sequence GFOGER represents a high-affinity binding site in collagens I and IV for α2β1 and in collagen I for α1β1, and that the same sequence binds integrin α1 A-domain and supports integrin β-mediated cell adhesion.
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