Localization of transglutaminase-reactive glutamine residues in bovine osteopontin.
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Osteopontin undergoes polymerization in vivo and gains chemotactic activity for neutrophils mediated by integrin alpha9beta1.Tissue transglutaminase and its substrates in boneIdentification of transglutaminase reactive residues in human osteopontin and their role in polymerizationPlasma membrane factor XIIIA transglutaminase activity regulates osteoblast matrix secretion and deposition by affecting microtubule dynamics.Cross-linking of osteopontin by tissue transglutaminase increases its collagen binding properties.Secreted osteopontin is highly polymerized in human airways and fragmented in asthmatic airway secretionsPre- and post-translational regulation of osteopontin in cancer.Mammalian transglutaminases. Identification of substrates as a key to physiological function and physiopathological relevance.Facile coupling of synthetic peptides and peptide-polymer conjugates to cartilage via transglutaminase enzymeTransglutaminase-catalyzed matrix cross-linking in differentiating cartilage: identification of osteonectin as a major glutaminyl substrate.Posttranslational modifications of bovine osteopontin: identification of twenty-eight phosphorylation and three O-glycosylation sites.Posttranslational modification in rat bone osteopontin.Transglutaminases and their substrates in biology and human diseases: 50 years of growing.Bone sialoprotein and osteopontin in bone metastasis of osteotropic cancersFactor XIII: a coagulation factor with multiple plasmatic and cellular functions.Substrates of Factor XIII-A: roles in thrombosis and wound healing.Transglutaminase-mediated oligomerization promotes osteoblast adhesive properties of osteopontin and bone sialoproteinOsteopontin induces increased invasiveness and plasminogen activator expression of human mammary epithelial cells.Osteopontin at the Crossroads of Inflammation and Tumor Progression.Importance of phosphorylation for osteopontin regulation of biomineralization.Tertiary structure prediction and identification of druggable pocket in the cancer biomarker - Osteopontin-c.Role of the cross-linking enzyme tissue transglutaminase in the biological recognition of synthetic biodegradable polymers.Mechanically strained cells of the osteoblast lineage organize their extracellular matrix through unique sites of alphavbeta3-integrin expression.Secretion of Osteopontin by macrophages and its accumulation at tissue surfaces during wound healing in mineralized tissues: a potential requirement for macrophage adhesion and phagocytosis.Progesterone and placentation increase secreted phosphoprotein one (SPP1 or osteopontin) in uterine glands and stroma for histotrophic and hematotrophic support of ovine pregnancy.Mice lacking osteopontin show normal development and bone structure but display altered osteoclast formation in vitro.Protein cross-linking mediated by tissue transglutaminase correlates with the maturation of extracellular matrices during lung development.The Phylogeny of Osteopontin-Analysis of the Protein Sequence
P2860
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P2860
Localization of transglutaminase-reactive glutamine residues in bovine osteopontin.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Localization of transglutaminase-reactive glutamine residues in bovine osteopontin.
@en
type
label
Localization of transglutaminase-reactive glutamine residues in bovine osteopontin.
@en
prefLabel
Localization of transglutaminase-reactive glutamine residues in bovine osteopontin.
@en
P2093
P2860
P356
P1433
P1476
Localization of transglutaminase-reactive glutamine residues in bovine osteopontin
@en
P2093
E S Sørensen
L K Rasmussen
T E Petersen
P2860
P356
10.1042/BJ3040013
P407
P478
304 ( Pt 1)
P577
1994-11-01T00:00:00Z