The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of carbohydrate moiety - Wikidata - wikimedia - TriplyDB

The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of carbohydrate moiety

The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of carbohydrate moiety

http://www.wikidata.org/entity/Q24657920

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Proteoglycan form and function: A comprehensive nomenclature of proteoglycans The plasminogen binding site of the C-type lectin tetranectin is located in the carbohydrate recognition domain, and binding is sensitive to both calcium and lysine Expression of CD44 3'-untranslated region regulates endogenous microRNA functions in tumorigenesis and angiogenesis Neuron-Glia Interactions in Neural Plasticity: Contributions of Neural Extracellular Matrix and Perineuronal Nets Proteoglycans and neuronal migration in the cerebral cortex during development and disease Versican and the regulation of cell phenotype in disease The proteoglycans aggrecan and Versican form networks with fibulin-2 through their lectin domain binding Mutational analysis of affinity and selectivity of kringle-tetranectin interaction. Grafting novel kringle affinity ontp the trtranectin lectin scaffold Processing and localization of ADAMTS-1 and proteolytic cleavage of versican during cumulus matrix expansion and ovulation A hyaluronan binding link protein gene family whose members are physically linked adjacent to chondroitin sulfate proteoglycan core protein genes: the missing links High affinity binding and overlapping localization of neurocan and phosphacan/protein-tyrosine phosphatase-zeta/beta with tenascin-R, amphoterin, and the heparin-binding growth-associated molecule Postnatal development of perineuronal nets in wild-type mice and in a mutant deficient in tenascin-R Brevican-deficient mice display impaired hippocampal CA1 long-term potentiation but show no obvious deficits in learning and memory Severe cognitive and motor coordination deficits in tenascin-R-deficient mice Composition of perineuronal net extracellular matrix in rat brain: a different disaccharide composition for the net-associated proteoglycans CALEB binds via its acidic stretch to the fibrinogen-like domain of tenascin-C or tenascin-R and its expression is dynamically regulated after optic nerve lesion Extracellular matrix plasticity and GABAergic inhibition of prefrontal cortex pyramidal cells facilitates relapse to heroin seeking.A missense mutation in the aggrecan C-type lectin domain disrupts extracellular matrix interactions and causes dominant familial osteochondritis dissecans.C-type lectins and sialyl Lewis X oligosaccharides. Versatile roles in cell-cell interaction.Transforming growth factor beta3 regulates the versican variants in the extracellular matrix-rich uterine leiomyomas.Extracellular matrix regulation of inflammation in the healthy and injured spinal cord Versican facilitates chondrocyte differentiation and regulates joint morphogenesis Structure and function of aggrecan.The different roles of aggrecan interaction domains Glial tumor invasion: a role for the upregulation and cleavage of BEHAB/brevican.Versican mediates mesenchymal-epithelial transition.The C-type lectin of the aggrecan G3 domain activates complement.Altered versican cleavage in ADAMTS5 deficient mice; a novel etiology of myxomatous valve disease.Involvement of ADAMTS5 and hyaluronidase in aggrecan degradation and release from OSM-stimulated cartilage Structure-function analysis of endogenous lectin mind-the-gap in synaptogenesis The interaction of versican with its binding partners.Indirect role of Ca2+ in the assembly of extracellular matrix proteins Solution structure and sugar-binding mechanism of mouse latrophilin-1 RBL: a 7TM receptor-attached lectin-like domain Lectican proteoglycans, their cleaving metalloproteinases, and plasticity in the central nervous system extracellular microenvironment.Chondroitin sulfate proteoglycan tenascin-R regulates glutamate uptake by adult brain astrocytes.The crosstalk of hyaluronan-based extracellular matrix and synapses.Aggrecan, link protein and tenascin-R are essential components of the perineuronal net to protect neurons against iron-induced oxidative stress.Casting a net on dendritic spines: the extracellular matrix and its receptors.The perineuronal net and the control of CNS plasticity.Therapeutic targeting of hyaluronan in the tumor stroma.

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P2860

The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of carbohydrate moiety

http://www.wikidata.org/entity/Q24657920

description

1997 nî lūn-bûn

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1997 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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1997 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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1997年論文

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1997年論文

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Proceedings of the National Academy of Sciences of the United States of America

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The C-type lectin domains of l ...... pendent of carbohydrate moiety

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P2860

Multiple domains of the large fibroblast proteoglycan, versican

Calculation of protein extinction coefficients from amino acid sequence data

Distinct effects of recombinant tenascin-R domains in neuronal cell functions and identification of the domain interacting with the neuronal recognition molecule F3/11

Cloning and primary structure of neurocan, a developmentally regulated, aggregating chondroitin sulfate proteoglycan of brain.

The versican C-type lectin domain recognizes the adhesion protein tenascin-R.

A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding.

PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus.

Binding site for IgE of the human lymphocyte low-affinity Fc epsilon receptor (Fc epsilon RII/CD23) is confined to the domain homologous with animal lectins.

Carbohydrate-protein interactions in vascular biology.

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10116-10121

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19

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