Literature DB >> 17942296

Extracellular matrix: from atomic resolution to ultrastructure.

Ioannis Vakonakis1, Iain D Campbell.   

Abstract

The extracellular matrix (ECM) is a highly organized multimolecular structure, essential for life in higher organisms. Although substantial high-resolution structural information is available for relatively small fragments of ECM components, the inherent difficulty in preparing and analyzing samples of large, fibrous polymers impedes structural efforts. Here, we review recent advances in understanding the structure of three important ECM components: collagen, fibrillin and fibronectin. Emphasis is placed on the key role of intermolecular interactions in assembling larger, microm scale, structures.

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Year:  2007        PMID: 17942296      PMCID: PMC4827755          DOI: 10.1016/j.ceb.2007.09.005

Source DB:  PubMed          Journal:  Curr Opin Cell Biol        ISSN: 0955-0674            Impact factor:   8.382


  50 in total

1.  Thermostability gradient in the collagen triple helix reveals its multi-domain structure.

Authors:  Andrzej Steplewski; Ireneusz Majsterek; Erin McAdams; Eileen Rucker; Raymond J Brittingham; Hidetoshi Ito; Kazuya Hirai; Eijiro Adachi; Sergio A Jimenez; Andrzej Fertala
Journal:  J Mol Biol       Date:  2004-05-14       Impact factor: 5.469

2.  Microfibrillar structure of type I collagen in situ.

Authors:  Joseph P R O Orgel; Thomas C Irving; Andrew Miller; Tim J Wess
Journal:  Proc Natl Acad Sci U S A       Date:  2006-06-02       Impact factor: 11.205

3.  Molecular basis of organization of collagen fibrils.

Authors:  Andrzej Steplewski; Vera Hintze; Andrzej Fertala
Journal:  J Struct Biol       Date:  2006-10-21       Impact factor: 2.867

4.  Collagen fibrils: nanoscale ropes.

Authors:  Laurent Bozec; Gert van der Heijden; Michael Horton
Journal:  Biophys J       Date:  2006-10-06       Impact factor: 4.033

Review 5.  The structure and function of hyaluronan: An overview.

Authors:  T C Laurent; U B Laurent; J R Fraser
Journal:  Immunol Cell Biol       Date:  1996-04       Impact factor: 5.126

Review 6.  Mammalian collagen receptors.

Authors:  Birgit Leitinger; Erhard Hohenester
Journal:  Matrix Biol       Date:  2006-11-10       Impact factor: 11.583

7.  Cellular and molecular studies of Marfan syndrome mutations identify co-operative protein folding in the cbEGF12-13 region of fibrillin-1.

Authors:  Pat Whiteman; Antony C Willis; Andrew Warner; James Brown; Christina Redfield; Penny A Handford
Journal:  Hum Mol Genet       Date:  2007-02-26       Impact factor: 6.150

8.  Fibrillin-1 interactions with heparin. Implications for microfibril and elastic fiber assembly.

Authors:  Stuart A Cain; Clair Baldock; John Gallagher; Amanda Morgan; Daniel V Bax; Anthony S Weiss; C Adrian Shuttleworth; Cay M Kielty
Journal:  J Biol Chem       Date:  2005-06-24       Impact factor: 5.157

9.  Structure of the integrin binding fragment from fibrillin-1 gives new insights into microfibril organization.

Authors:  Stephen S J Lee; Vroni Knott; Jelena Jovanović; Karl Harlos; Jonathan M Grimes; Laurence Choulier; Helen J Mardon; David I Stuart; Penny A Handford
Journal:  Structure       Date:  2004-04       Impact factor: 5.006

10.  Dual labeling of the fibronectin matrix and actin cytoskeleton with green fluorescent protein variants.

Authors:  Tomoo Ohashi; Daniel P Kiehart; Harold P Erickson
Journal:  J Cell Sci       Date:  2002-03-15       Impact factor: 5.285

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  27 in total

1.  The evolution of thrombospondins and their ligand-binding activities.

Authors:  Amber A Bentley; Josephine C Adams
Journal:  Mol Biol Evol       Date:  2010-04-28       Impact factor: 16.240

Review 2.  The extracellular matrix at a glance.

Authors:  Christian Frantz; Kathleen M Stewart; Valerie M Weaver
Journal:  J Cell Sci       Date:  2010-12-15       Impact factor: 5.285

3.  A small fibronectin-mimicking protein from bacteria induces cell spreading and focal adhesion formation.

Authors:  Nicole Tegtmeyer; Roland Hartig; Robin M Delahay; Manfred Rohde; Sabine Brandt; Jens Conradi; Seiichiro Takahashi; Adam J Smolka; Norbert Sewald; Steffen Backert
Journal:  J Biol Chem       Date:  2010-05-27       Impact factor: 5.157

Review 4.  Forcing form and function: biomechanical regulation of tumor evolution.

Authors:  Hongmei Yu; Janna Kay Mouw; Valerie M Weaver
Journal:  Trends Cell Biol       Date:  2010-10-01       Impact factor: 20.808

Review 5.  Extracellular matrix degradation and remodeling in development and disease.

Authors:  Pengfei Lu; Ken Takai; Valerie M Weaver; Zena Werb
Journal:  Cold Spring Harb Perspect Biol       Date:  2011-12-01       Impact factor: 10.005

6.  The terminal immunoglobulin-like repeats of LigA and LigB of Leptospira enhance their binding to gelatin binding domain of fibronectin and host cells.

Authors:  Yi-Pin Lin; Sean P McDonough; Yogendra Sharma; Yung-Fu Chang
Journal:  PLoS One       Date:  2010-06-24       Impact factor: 3.240

Review 7.  Running GAGs: myxoid matrix in tumor pathology revisited: what's in it for the pathologist?

Authors:  Stefan M Willems; Malgorzata Wiweger; J Frans Graadt van Roggen; Pancras C W Hogendoorn
Journal:  Virchows Arch       Date:  2009-08-25       Impact factor: 4.064

8.  Implications for collagen binding from the crystallographic structure of fibronectin 6FnI1-2FnII7FnI.

Authors:  Michèle C Erat; Ulrich Schwarz-Linek; Andrew R Pickford; Richard W Farndale; Iain D Campbell; Ioannis Vakonakis
Journal:  J Biol Chem       Date:  2010-08-24       Impact factor: 5.157

9.  iso-DGR sequences do not mediate binding of fibronectin N-terminal modules to adherent fibronectin-null fibroblasts.

Authors:  Jielin Xu; Lisa M Maurer; Brian R Hoffmann; Douglas S Annis; Deane F Mosher
Journal:  J Biol Chem       Date:  2010-01-22       Impact factor: 5.157

10.  Motogenic sites in human fibronectin are masked by long range interactions.

Authors:  Ioannis Vakonakis; David Staunton; Ian R Ellis; Peter Sarkies; Aleksandra Flanagan; Ana M Schor; Seth L Schor; Iain D Campbell
Journal:  J Biol Chem       Date:  2009-04-14       Impact factor: 5.157

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