PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32262393-6 2015 Platelet-like hydroxyapatite crystals periodically arranged inside the collagen fibrils have been achieved under the function of (MBP)-BSP-HAP. Durapatite 14-28 integrin binding sialoprotein Homo sapiens 135-138 23261880-11 2013 The relationships between hydroxyapatite, collagen and BSP are discussed. Durapatite 26-40 integrin binding sialoprotein Homo sapiens 55-58 22201843-9 2012 The poly glutamic acid sequences of BSP act as possible nucleation sites for hydroxyapatite crystals. Durapatite 77-91 integrin binding sialoprotein Homo sapiens 36-39 20438109-0 2010 How does bone sialoprotein promote the nucleation of hydroxyapatite? Durapatite 53-67 integrin binding sialoprotein Homo sapiens 9-26 20965237-1 2011 Bone sialoprotein (BSP) is a noncollagenous protein of the extracellular matrix in mineralized connective tissues that has been implicated in the nucleation of hydroxyapatite. Durapatite 160-174 integrin binding sialoprotein Homo sapiens 0-17 20965237-1 2011 Bone sialoprotein (BSP) is a noncollagenous protein of the extracellular matrix in mineralized connective tissues that has been implicated in the nucleation of hydroxyapatite. Durapatite 160-174 integrin binding sialoprotein Homo sapiens 19-22 20438109-3 2010 Although BSP has been proposed to be a nucleator of hydroxyapatite (Ca(5)(PO(4))(3)OH), the major mineral component of bone, no detailed mechanism for the nucleation process has been elucidated at the atomic level to date. Durapatite 52-66 integrin binding sialoprotein Homo sapiens 9-12 20438109-4 2010 In the present work, using a peptide model, we apply molecular dynamics (MD) simulations to study the conformational effect of a proposed nucleating motif of BSP (a phosphorylated, acidic, 10 amino-acid residue sequence) on controlling the distributions of Ca(2+) and inorganic phosphate (Pi) ions in solution, and specifically, we explore whether a nucleating template for orientated hydroxyapatite could be formed in different peptide conformations. Durapatite 385-399 integrin binding sialoprotein Homo sapiens 158-161 20438109-8 2010 Therefore, independent of conformations, the BSP nucleating motif is more likely to help nucleate an amorphous calcium phosphate cluster, which ultimately converts to crystalline hydroxyapatite. Durapatite 179-193 integrin binding sialoprotein Homo sapiens 45-48 18620053-0 2008 Bone sialoprotein-collagen interaction promotes hydroxyapatite nucleation. Durapatite 48-62 integrin binding sialoprotein Homo sapiens 0-17 15795688-3 2005 The expression of BSP coincides with initial bone mineralization and is believed to be a center of crystallization for hydroxyapatite formation. Durapatite 119-133 integrin binding sialoprotein Homo sapiens 18-21 12459268-1 2002 Bone sialoprotein (BSP) is a phosphorylated and sulphated glycoprotein with hydroxyapatite nucleating properties that is specifically expressed in association with physiological and pathological mineralization. Durapatite 76-90 integrin binding sialoprotein Homo sapiens 0-17 15004030-1 2004 Addition of an organophosphate source to UMR osteoblastic cultures activates a mineralization program in which BSP localizes to extracellular matrix sites where hydroxyapatite crystals are subsequently nucleated. Durapatite 161-175 integrin binding sialoprotein Homo sapiens 111-114 12459268-1 2002 Bone sialoprotein (BSP) is a phosphorylated and sulphated glycoprotein with hydroxyapatite nucleating properties that is specifically expressed in association with physiological and pathological mineralization. Durapatite 76-90 integrin binding sialoprotein Homo sapiens 19-22 11669636-4 2001 Thus, the proposed role of BSP in hydroxyapatite nucleation and growth may depend on such modifying groups. Durapatite 34-48 integrin binding sialoprotein Homo sapiens 27-30 11696986-0 2001 Binding of bone sialoprotein, osteopontin and synthetic polypeptides to hydroxyapatite. Durapatite 72-86 integrin binding sialoprotein Homo sapiens 11-28 11459848-11 2001 The affinity for hydroxyapatite was higher for bone-derived BSP than for recombinant BSP. Durapatite 17-31 integrin binding sialoprotein Homo sapiens 60-63 11459848-11 2001 The affinity for hydroxyapatite was higher for bone-derived BSP than for recombinant BSP. Durapatite 17-31 integrin binding sialoprotein Homo sapiens 85-88 11696986-1 2001 The phosphorylated acidic glycoproteins bone sialoprotein (BSP) and osteopontin (OPN) bind to hydroxyapatite (HA) crystals and may be involved in the regulation of bone mineralization. Durapatite 94-108 integrin binding sialoprotein Homo sapiens 40-57 11696986-1 2001 The phosphorylated acidic glycoproteins bone sialoprotein (BSP) and osteopontin (OPN) bind to hydroxyapatite (HA) crystals and may be involved in the regulation of bone mineralization. Durapatite 94-108 integrin binding sialoprotein Homo sapiens 59-62 11696986-1 2001 The phosphorylated acidic glycoproteins bone sialoprotein (BSP) and osteopontin (OPN) bind to hydroxyapatite (HA) crystals and may be involved in the regulation of bone mineralization. Durapatite 110-112 integrin binding sialoprotein Homo sapiens 40-57 11696986-1 2001 The phosphorylated acidic glycoproteins bone sialoprotein (BSP) and osteopontin (OPN) bind to hydroxyapatite (HA) crystals and may be involved in the regulation of bone mineralization. Durapatite 110-112 integrin binding sialoprotein Homo sapiens 59-62 9258751-3 1997 Both native BSP and a 47 kD fragment of UMR-BSP (Fragment 1 approximately 133A- approximately 265Y) are more potent inhibitors of seeded hydroxyapatite crystal growth than recombinant human BSP fragments lacking post-translational modifications. Durapatite 137-151 integrin binding sialoprotein Homo sapiens 12-15 10759428-9 1999 In combination, the hydroxyapatite-binding polyglutamic acid sequences and the RGD provide bi-functional entities through which BSP may mediate the targeting and attachment of normal and metastasizing cells to the bone surface. Durapatite 20-34 integrin binding sialoprotein Homo sapiens 128-131 11314517-9 2000 BSP may serve as a nucleator of hydroxyapatite crystal formation. Durapatite 32-46 integrin binding sialoprotein Homo sapiens 0-3 9458353-13 1998 We speculate that the high expression of BSP could create an appropriate microenvironment for the crystallisation of calcium and phosphate into hydroxyapatite. Durapatite 144-158 integrin binding sialoprotein Homo sapiens 41-44 9258751-3 1997 Both native BSP and a 47 kD fragment of UMR-BSP (Fragment 1 approximately 133A- approximately 265Y) are more potent inhibitors of seeded hydroxyapatite crystal growth than recombinant human BSP fragments lacking post-translational modifications. Durapatite 137-151 integrin binding sialoprotein Homo sapiens 44-47 9084640-2 1996 Recent studies on the developmental expression of BSP mRNA and the temporo-spatial appearance of the protein during bone formation in vivo and in vitro have demonstrated that BSP is expressed by differentiated osteoblasts and that it may function in the initial nucleation of hydroxyapatite crystals in de novo bone formation. Durapatite 276-290 integrin binding sialoprotein Homo sapiens 175-178 9181551-0 1997 Attachment of osteoblastic cells to hydroxyapatite crystals by a synthetic peptide (Glu7-Pro-Arg-Gly-Asp-Thr) containing two functional sequences of bone sialoprotein. Durapatite 36-50 integrin binding sialoprotein Homo sapiens 149-166 9181551-1 1997 We investigated activity of bone sialoprotein (BSP) to mediate attachment of cells to hydroxyapatite using a model peptide, Glu7-Pro-Arg-Gly-Asp-Thr, which contains a putative hydroxyapatite-binding site (poly-Glu) and a cell-attachment site. Durapatite 86-100 integrin binding sialoprotein Homo sapiens 28-45 9181551-1 1997 We investigated activity of bone sialoprotein (BSP) to mediate attachment of cells to hydroxyapatite using a model peptide, Glu7-Pro-Arg-Gly-Asp-Thr, which contains a putative hydroxyapatite-binding site (poly-Glu) and a cell-attachment site. Durapatite 86-100 integrin binding sialoprotein Homo sapiens 47-50 9181551-1 1997 We investigated activity of bone sialoprotein (BSP) to mediate attachment of cells to hydroxyapatite using a model peptide, Glu7-Pro-Arg-Gly-Asp-Thr, which contains a putative hydroxyapatite-binding site (poly-Glu) and a cell-attachment site. Durapatite 176-190 integrin binding sialoprotein Homo sapiens 28-45 9181551-1 1997 We investigated activity of bone sialoprotein (BSP) to mediate attachment of cells to hydroxyapatite using a model peptide, Glu7-Pro-Arg-Gly-Asp-Thr, which contains a putative hydroxyapatite-binding site (poly-Glu) and a cell-attachment site. Durapatite 176-190 integrin binding sialoprotein Homo sapiens 47-50 9181551-9 1997 In conclusion, BSP mediated attachment of osteoblastic cells to hydroxyapatite, and this activity could be accomplished only by the poly-Glu sequence and the Arg-Gly-Asp sequence. Durapatite 64-78 integrin binding sialoprotein Homo sapiens 15-18 8797881-1 1996 We have recently demonstrated that bone sialoprotein (BSP), a bone-matrix protein involved in hydroxyapatite crystal formation, is ectopically expressed in human breast cancers. Durapatite 94-108 integrin binding sialoprotein Homo sapiens 35-52 8797881-1 1996 We have recently demonstrated that bone sialoprotein (BSP), a bone-matrix protein involved in hydroxyapatite crystal formation, is ectopically expressed in human breast cancers. Durapatite 94-108 integrin binding sialoprotein Homo sapiens 54-57 9084679-1 1996 Bone sialoprotein (BSP) was shown to be a potent nucleator of hydroxyapatite (HA) in a steady-state agarose gel system (Hunter and Goldberg, 1993, PNAS 90: 8562). Durapatite 62-76 integrin binding sialoprotein Homo sapiens 0-23 9084680-1 1996 Bone sialoprotein (BSP) and osteopontin (OPN) are two extracellular bone matrix proteins that have the ability to modulate the growth of hydroxyapatite in vitro. Durapatite 137-151 integrin binding sialoprotein Homo sapiens 0-23 9084680-2 1996 Studies of BSP/OPN hydroxyapatite interactions in the past have been directed toward the identification of essential structural elements that allow these two proteins to modulate hydroxyapatite growth. Durapatite 19-33 integrin binding sialoprotein Homo sapiens 11-14 9084680-2 1996 Studies of BSP/OPN hydroxyapatite interactions in the past have been directed toward the identification of essential structural elements that allow these two proteins to modulate hydroxyapatite growth. Durapatite 179-193 integrin binding sialoprotein Homo sapiens 11-14 8187059-3 1994 Bone sialoprotein (BSP) is a glycoprotein the expression of which coincides with the appearance of the first hydroxyapatite crystals during bone development. Durapatite 109-123 integrin binding sialoprotein Homo sapiens 0-17 7915111-2 1994 Recent studies in this laboratory have shown that BSP is capable of nucleating the bone mineral hydroxyapatite in a steady-state agarose gel system. Durapatite 96-110 integrin binding sialoprotein Homo sapiens 50-53 7915111-6 1994 These findings suggest that the nucleation of hydroxyapatite by BSP involves one or both of the glutamic acid-rich sequences. Durapatite 46-60 integrin binding sialoprotein Homo sapiens 64-67 7554919-1 1995 During the initial formation of bone, dentine and cementum in tooth morphogenesis, fully differentiated osteoblasts, odontoblasts and cementoblasts express bone sialoprotein (BSP), a mineralized tissue-specific acidic glycoprotein that has been implicated in the nucleation of hydroxyapatite crystal growth. Durapatite 277-291 integrin binding sialoprotein Homo sapiens 156-173 7554919-1 1995 During the initial formation of bone, dentine and cementum in tooth morphogenesis, fully differentiated osteoblasts, odontoblasts and cementoblasts express bone sialoprotein (BSP), a mineralized tissue-specific acidic glycoprotein that has been implicated in the nucleation of hydroxyapatite crystal growth. Durapatite 277-291 integrin binding sialoprotein Homo sapiens 175-178 8187059-3 1994 Bone sialoprotein (BSP) is a glycoprotein the expression of which coincides with the appearance of the first hydroxyapatite crystals during bone development. Durapatite 109-123 integrin binding sialoprotein Homo sapiens 19-22 33610546-3 2021 To learn more, we examined the protein composition of extracellular sites of de novo hydroxyapatite deposition which were enriched in BSP and Col11a1 containing an alternatively spliced "6b" exonal sequence. Durapatite 85-99 integrin binding sialoprotein Homo sapiens 134-137 8489418-2 1993 Although BSP can mediate cell attachment through an RGD sequence and binds selectively to hydroxyapatite, its precise function in mineralized tissues is unknown. Durapatite 90-104 integrin binding sialoprotein Homo sapiens 9-12 8397409-5 1993 By powder x-ray diffraction, the precipitate formed in the presence of BSP was shown to be hydroxyapatite. Durapatite 91-105 integrin binding sialoprotein Homo sapiens 71-74