Journal ArticleDOI
Analysis of the human integrin α11 gene (ITGA11) and its promoter
Wan-Ming Zhang,Svetlana N Popova,Charlotta Bergman,Teet Velling,Marion Kusche Gullberg,Donald Gullberg +5 more
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TLDR
The complete exon structure of ITGA11, including the proximal promoter, was assembled into 30 exons and promoter sequence analysis in silico suggested the presence of multiple binding sites for transcription factors in the region upstream of the transcription start.About:
This article is published in Matrix Biology.The article was published on 2002-10-01. It has received 18 citations till now. The article focuses on the topics: Upstream activating sequence & Promoter.read more
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Alpha10 integrin expression is up-regulated on fibroblast growth factor-2-treated mesenchymal stem cells with improved chondrogenic differentiation potential.
Laura Varas,Lars Bryngelson Ohlsson,Gabriella Honeth,Andreas Olsson,Therése Bengtsson,Charlotte Wiberg,Robert Bockermann,Sofia Järnum,Johan Richter,Douglas Pennington,Brian Johnstone,Brian Johnstone,Evy Lundgren-Åkerlund,Christian Kjellman +13 more
TL;DR: It is demonstrated that improved chondrogenecity as well as increased collagen-dependant migratory potential of FGF-2-treated MSCs having a high alpha10 expression are demonstrated and proposed alpha10 as a potential marker to predict the differentiation state of M SCs are proposed.
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The mesenchymal alpha11beta1 integrin attenuates PDGF-BB-stimulated chemotaxis of embryonic fibroblasts on collagens.
Svetlana N Popova,Belén Rodriguez-Sánchez,Åsa Lidén,Christer Betsholtz,Theo van den Bos,Donald Gullberg +5 more
TL;DR: It is speculated that the PDGF BB-dependent cell migration of mesenchymal cells is tightly regulated by the collagen receptor repertoire, and disturbances of this repertoire might lead to unregulated cell migration that could affect normal embryonic development and tissue structure.
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Research advances on structure and biological functions of integrins.
TL;DR: The purpose of this review is to describe the unique structure of each integrin subunit, primary cytoplasmic association proteins, and transduction signaling pathway of integrins, with an emphasis on their biological functions.
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Physiology and pathology of collagen receptors.
TL;DR: In the current review, the current knowledge about the in vitro and in vivo functions of these integrins is summarized and updated.
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Control of integrin genes expression in the eye.
TL;DR: This review provides an overview of the current state of knowledge about the organization of the regulatory elements and the transcription factors they bind that are used by the cell in order to ensure transcription of each of the integrins gene.
References
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Integrins: versatility, modulation, and signaling in cell adhesion.
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Simplified mammalian DNA isolation procedure.
TL;DR: This work has simplified the standard mammalian DNA isolation procedure with the aim of minimizing the number of manipulations required for each sample.
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Crystal Structure of the Extracellular Segment of Integrin αVβ3
Jian-Ping Xiong,Thilo Stehle,Beate Diefenbach,Rongguang Zhang,Reinhardt Dunker,David L. Scott,Andrzej Joachimiak,Simon L. Goodman,M. Amin Arnaout +8 more
TL;DR: In this paper, the authors solved the crystal structure of the extracellular portion of integrin αVβ3 at 3.1 A resolution, showing that the αβ heterodimeric receptors mediate divalent cation-dependent cell-cell and cell-matrix adhesion through tightly regulated interactions with ligands.
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Structural Basis of Collagen Recognition by Integrin α2β1
Jonas Emsley,C. Graham Knight,Richard W. Farndale,Michael J. Barnes,Robert C. Liddington,Robert C. Liddington +5 more
TL;DR: The crystal structure of a complex between the I domain of integrin alpha2beta1 and a triple helical collagen peptide containing a critical GFOGER motif is determined, suggesting both a basis for affinity regulation and a pathway for signal transduction.
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Differences and similarities in DNA-binding preferences of MyoD and E2A protein complexes revealed by binding site selection
TK Blackwell,Harold Weintraub +1 more
TL;DR: It was shown that homo- and heterooligomers of the helix-loop-helix proteins MyoD and E2A recognize a common consensus sequence, CA--TG, but otherwise bind to flanking and internal positions with different sequence preferences that suggest half-site recognition, suggesting that different combinations of dimeric proteins can have different binding sequence preferences.