2.50
Hdl Handle:
http://hdl.handle.net/10541/72683
Title:
Multiprotein signalling complexes: regional assembly on heparan sulphate.
Authors:
Gallagher, John T
Abstract:
Heparan sulphate (HS) is an abundant component of cell surfaces and the extracellular matrix. It binds to a wide variety of peptide growth factors, morphogens, chemokines and extracellular matrix proteins (e.g. fibronectin) and many of these interactions are essential for these effector proteins to transduce signals across the plasma membrane. The unique molecular design and flexibility of HS are essential for its ability to exert control over the cellular response to proteinaceous ligands. The clustering of sulphated sugar residues in a series of complex domains with variable sulphation patterns generates considerable diversity in the molecular fine structure of HS. This diversity reflects a high degree of selectivity in protein recognition and in the assembly of functional multiprotein complexes on the HS polymer chain.
Affiliation:
CRUK Department of Medical Oncology, University of Manchester, Paterson Institute for Cancer Research, UK. jgallagher@picr.man.ac.uk
Citation:
Multiprotein signalling complexes: regional assembly on heparan sulphate. 2006, 34 (Pt 3):438-41 Biochem. Soc. Trans.
Journal:
Biochemical Society Transactions
Issue Date:
Jun-2006
URI:
http://hdl.handle.net/10541/72683
DOI:
10.1042/BST0340438
PubMed ID:
16709181
Type:
Article
Language:
en
ISSN:
0300-5127
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorGallagher, John T-
dc.date.accessioned2009-07-07T10:24:32Z-
dc.date.available2009-07-07T10:24:32Z-
dc.date.issued2006-06-
dc.identifier.citationMultiprotein signalling complexes: regional assembly on heparan sulphate. 2006, 34 (Pt 3):438-41 Biochem. Soc. Trans.en
dc.identifier.issn0300-5127-
dc.identifier.pmid16709181-
dc.identifier.doi10.1042/BST0340438-
dc.identifier.urihttp://hdl.handle.net/10541/72683-
dc.description.abstractHeparan sulphate (HS) is an abundant component of cell surfaces and the extracellular matrix. It binds to a wide variety of peptide growth factors, morphogens, chemokines and extracellular matrix proteins (e.g. fibronectin) and many of these interactions are essential for these effector proteins to transduce signals across the plasma membrane. The unique molecular design and flexibility of HS are essential for its ability to exert control over the cellular response to proteinaceous ligands. The clustering of sulphated sugar residues in a series of complex domains with variable sulphation patterns generates considerable diversity in the molecular fine structure of HS. This diversity reflects a high degree of selectivity in protein recognition and in the assembly of functional multiprotein complexes on the HS polymer chain.en
dc.language.isoenen
dc.subject.meshAnimals-
dc.subject.meshHeparitin Sulfate-
dc.subject.meshHumans-
dc.subject.meshMultiprotein Complexes-
dc.subject.meshSignal Transduction-
dc.titleMultiprotein signalling complexes: regional assembly on heparan sulphate.en
dc.typeArticleen
dc.contributor.departmentCRUK Department of Medical Oncology, University of Manchester, Paterson Institute for Cancer Research, UK. jgallagher@picr.man.ac.uken
dc.identifier.journalBiochemical Society Transactionsen

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