About: The major non-integrin laminin binding protein of macrophages is identical to carbohydrate binding protein 35 (Mac-2)

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About: The major non-integrin laminin binding protein of macrophages is identical to carbohydrate binding protein 35 (Mac-2) Goto Sponge NotDistinct Permalink

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scientific article published on 01 May 1990

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в травні 1990 (uk) article scientifique publié en 1990 (fr) im Mai 1990 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en mayu de 1990 (ast) scientific article published on 01 May 1990 (en)
publication date	wds:Q68768239-252DE05C-23AD-4D31-8EBF-90D4BADF54F8
publication date	1990-05-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q68768239-8C8FC855-AA7E-410C-B2B2-C7F02BE8B196
language of work or name	English
author name string	wds:Q68768239-06BCDD70-52E3-4B1F-B879-38F4E709D6AF wds:Q68768239-4AD52B01-DB71-4BED-A2F0-7D1A1793EDA2 wds:Q68768239-AB10DCBF-E804-4810-8ABD-4A00E1279914 wds:Q68768239-DE413D01-E416-4BBB-AC67-3FA721C48367
author name string	Shaw LM Mercurio AM Woo HJ Messier JM
rdfs:label	The major non-integrin laminin binding protein of macrophages is identical to carbohydrate binding protein 35 (nl) The major non-integrin laminin binding protein of macrophages is identical to carbohydrate binding protein 35 (Mac-2) (en)
skos:prefLabel	The major non-integrin laminin binding protein of macrophages is identical to carbohydrate binding protein 35 (nl) The major non-integrin laminin binding protein of macrophages is identical to carbohydrate binding protein 35 (Mac-2) (en)
name	The major non-integrin laminin binding protein of macrophages is identical to carbohydrate binding protein 35 (nl) The major non-integrin laminin binding protein of macrophages is identical to carbohydrate binding protein 35 (Mac-2) (en)
title	wds:Q68768239-35D6A28B-D931-4A29-9158-F74083653947
title	The major non-integrin laminin binding protein of macrophages is identical to carbohydrate binding protein 35 (Mac-2) (en)
page(s)	wds:Q68768239-DE64FA4B-3DF1-48A0-BD09-1A9D7CBBFF7A
page(s)	7097-7099
instance of	wds:Q68768239-980AF0D0-B875-46FA-B61C-8AA57D2FF6C1
instance of	scholarly article
PubMed ID	wds:Q68768239-D25D57AA-1079-417B-901E-FE6F7FDED320
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/2332426
PubMed ID	2332426
published in	wds:Q68768239-D7B8B10D-8B6C-4559-903D-D345C048B600
published in	Journal of Biological Chemistry
issue	wds:Q68768239-F85729D5-9C98-44AB-AA5A-12EEA2360FC6
volume	wds:Q68768239-53F5EB6D-0CE6-44A9-A1B4-3A643D452583
issue	13
volume	265
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q68768239
is cites work of	Effects of natural complex carbohydrate (citrus pectin) on murine melanoma cell properties related to galectin-3 functions Interaction of laminin with Entamoeba histolytica cysteine proteinases and its effect on amebic pathogenesis Human keratinocytes release the endogenous beta-galactoside-binding soluble lectin immunoglobulin E (IgE-binding protein) which binds to Langerhans cells where it modulates their binding capacity for IgE glycoforms Galectins as inflammatory mediators Expression of galectins on microvessel endothelial cells and their involvement in tumour cell adhesion Extracellular matrix molecules and their receptors: functions in neural development 90K (Mac-2 BP) and galectins in tumor progression and metastasis Galectin-3 and metastasis Regulation of prostate cancer progression by galectin-3 Maintenance of granulocyte numbers during acute peritonitis is defective in galectin-3-null mutant mice Decreased expression of Mac-2 (carbohydrate binding protein 35) and loss of its nuclear localization are associated with the neoplastic progression of colon carcinoma Galectin-3 expression in human atherosclerotic lesions. Galectin-1, -2, and -3 exhibit differential recognition of sialylated glycans and blood group antigens Endogenous muscle lectin inhibits myoblast adhesion to laminin Dimeric Galectin-8 induces phosphatidylserine exposure in leukocytes through polylactosamine recognition by the C-terminal domain. Identification of galectin-3 as a high-affinity binding protein for advanced glycation end products (AGE): a new member of the AGE-receptor complex Human T lymphotropic virus-I infection of human T lymphocytes induces expression of the beta-galactoside-binding lectin, galectin-3 Expression and function of galectin-3, a beta-galactoside-binding lectin, in human monocytes and macrophages. Molecular cloning of a human macrophage lectin specific for galactose The integrin alpha 6 beta 4 is a laminin receptor Up-regulation of galectin-3 in acute renal failure of the rat Kinetic measurements of binding of galectin 3 to a laminin substratum Tissue biology perspective on macrophages Increased LAMP-2 polylactosamine glycosylation is associated with its slower Golgi transit during establishment of a polarized MDCK epithelial monolayer Galectin-3, a beta-galactoside-binding animal lectin, is a marker of anaplastic large-cell lymphoma. Evidence for IgG autoantibodies to galectin-3, a beta-galactoside-binding lectin (Mac-2, epsilon binding protein, or carbohydrate binding protein 35) in human serum Human milk 90K (Mac-2 BP): possible protective effects against acute respiratory infections Galectins in parasite infection and allergic inflammation. Epigenetic regulation of galectin-3 expression by β1 integrins promotes cell adhesion and migration. Intra- and intermolecular interactions of human galectin-3: assessment by full-assignment-based NMR Galectin-9 is a high affinity IgE-binding lectin with anti-allergic effect by blocking IgE-antigen complex formation Clinical implication of the serum galectin-1 expression in epithelial ovarian cancer patients Changes in S-type lectin localization in neuroblastoma cells (N1E115) upon differentiation Cell surface beta 1,4-galactosyltransferase functions during neural crest cell migration and neurulation in vivo TGFβ regulates Galectin-3 expression through canonical Smad3 signaling pathway in nucleus pulposus cells: implications in intervertebral disc degeneration Galectin-3 alters the lateral mobility and clustering of β1-integrin receptors On the possible role of endogenous lectins in early animal development Galectin-3: One Molecule for an Alphabet of Diseases, from A to Z. Role of Galectin-3 in Bone Cell Differentiation, Bone Pathophysiology and Vascular Osteogenesis. Galectin 3: an extraordinary multifunctional protein in dermatology. Current knowledge and perspectives The high affinity IgE receptor Fc epsilonRI is expressed by human intestinal epithelial cells An Impermeant Ganetespib Analog Inhibits Extracellular Hsp90-Mediated Cancer Cell Migration that Involves Lysyl Oxidase 2-like Protein Expression of ganglioside GM3 and H-2 antigens in clones with different metastatic and growth potentials isolated from Lewis lung carcinoma (3LL) cell line Expression of the endogenous 14-kDa beta-galactoside-binding lectin galectin in normal human skin Different immunoreactivities of anti-soluble lactose lectin antisera to tissues from early chick embryos: a histochemical study Changes in expression of two endogenous beta-galactoside-binding isolectins in the dermis of chick embryonic skin during development in ovo and in vitro Elevated levels of circulating immunostimulatory 90K in Henoch-Schoenlein purpura Immunohistochemical and in situ hybridization analysis of galectin-3, a beta-galactoside binding lectin, in the urinary system of adult mice. Expression of galectin-3 in gastric adenocarcinoma Galectin binding to cells and glycoproteins with genetically modified glycosylation reveals galectin-glycan specificities in a natural context Mechanisms of the epithelial-to-mesenchymal transition in sea urchin embryos Immunolocalization of galectin-3 in mouse testicular tissue. The novel monoclonal antibody 9F5 reveals expression of a fragment of GPNMB/osteoactivin processed by furin-like protease(s) in a subpopulation of microglia in neonatal rat brain Expression of the 14 kDa and 16 kDa galactoside-binding lectins during differentiation of the chick yolk sac.
is cites work of	wds:Q28570793-F9110FE5-8922-4367-9617-B7214F6339AD wds:Q46130366-D48AD164-CF44-48B0-9C8A-53A458667897 wds:Q41058851-EAC0F682-F2A6-41FF-94A5-1104F7EE6F4F wds:Q92312918-BAB3A8FE-91A6-47E8-AFED-103178F71CBA wds:Q35646658-810EE057-F04B-4C98-A888-D60520968E08

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