PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 28532068-2 2017 In particular, the statherin phosphopeptide DpSpSEEKFLR (DSS) was found to adsorb to enamel-like hydroxyapatite and inhibit plaque-related crystal formation. Durapatite 97-111 statherin Homo sapiens 19-28 33445390-5 2017 Peptide sequence DDDEEKC is a bioinspired sequence of statherin and has the adsorption capacity of hydroxyapatite (HAP). Durapatite 99-113 statherin Homo sapiens 54-63 25054469-2 2014 To further elucidate how the mineral surface impacts molecular properties, we perform a comparative study of the dynamics of nonpolar side chains within the mineral-recognition domain of the biomineralization protein salivary statherin adsorbed onto its native hydroxyapatite (HAP) mineral surface versus the dynamics displayed by the native protein in the hydrated solid state. Durapatite 261-275 statherin Homo sapiens 226-235 28572822-2 2017 Salivary proteins such as statherin inhibit crystal growth of calcium phosphate in supersaturated solutions and interact with several oral bacteria to adsorb on hydroxyapatite. Durapatite 161-175 statherin Homo sapiens 26-35 26116492-0 2015 Hydroxyapatite Growth Inhibition Effect of Pellicle Statherin Peptides. Durapatite 0-14 statherin Homo sapiens 52-61 26116492-4 2015 Here, we assessed the ability of these statherin pellicle peptides to inhibit hydroxyapatite crystal growth. Durapatite 78-92 statherin Homo sapiens 39-48 26116492-10 2015 Our data suggest that the presence of a covalently linked phosphate group (at residues 2 and 3) in statherin peptides modulates the effect of hydroxyapatite growth inhibition. Durapatite 142-156 statherin Homo sapiens 99-108 22563672-0 2012 Direct observation of phenylalanine orientations in statherin bound to hydroxyapatite surfaces. Durapatite 71-85 statherin Homo sapiens 52-61 24055522-1 2013 An epidermal growth factor (EGF) derivative with affinity for apatite and titanium surfaces was designed using a peptide moiety derived from salivary statherin, a protein that adheres to hydroxyapatite. Durapatite 187-201 statherin Homo sapiens 150-159 22563672-1 2012 Extracellular biomineralization proteins such as salivary statherin control the growth of hydroxyapatite (HAP), the principal component of teeth and bones. Durapatite 90-104 statherin Homo sapiens 58-67 22563672-1 2012 Extracellular biomineralization proteins such as salivary statherin control the growth of hydroxyapatite (HAP), the principal component of teeth and bones. Durapatite 106-109 statherin Homo sapiens 58-67 19383454-3 2009 We applied the technique to fold statherin, starting from a fully extended peptide chain in solution, in the presence of hydroxyapatite (HAp) (001), (010), and (100) monoclinic crystals. Durapatite 121-135 statherin Homo sapiens 33-42 20731414-1 2010 Human salivary statherin inhibits both primary and secondary calcium phosphate precipitation and, upon binding to hydroxyapatite, associates with a variety of oral bacteria. Durapatite 114-128 statherin Homo sapiens 15-24 19678690-0 2009 A (13)C{(31)P} REDOR NMR investigation of the role of glutamic acid residues in statherin- hydroxyapatite recognition. Durapatite 91-105 statherin Homo sapiens 80-89 22243221-0 2011 An in vitro scanning microradiography study of the reduction in hydroxyapatite demineralization rate by statherin-like peptides as a function of increasing N-terminal length. Durapatite 64-78 statherin Homo sapiens 104-113 20676391-0 2010 The Role of Basic Amino Acids in the Molecular Recognition of Hydroxyapatite by Statherin using Solid State NMR. Durapatite 62-76 statherin Homo sapiens 80-89 20676391-1 2010 Organisms use proteins such as statherin to control the growth of hydroxyapatite (HAP), which is the principal component of teeth and bone. Durapatite 66-80 statherin Homo sapiens 31-40 18054952-0 2008 Adsorption behavior of statherin and a statherin peptide onto hydroxyapatite and silica surfaces by in situ ellipsometry. Durapatite 62-76 statherin Homo sapiens 23-32 18266360-0 2008 Adsorption of a statherin peptide fragment on the surface of nanocrystallites of hydroxyapatite. Durapatite 81-95 statherin Homo sapiens 16-25 18054952-0 2008 Adsorption behavior of statherin and a statherin peptide onto hydroxyapatite and silica surfaces by in situ ellipsometry. Durapatite 62-76 statherin Homo sapiens 39-48 18054952-1 2008 The salivary protein statherin is known to adsorb selectively onto hydroxyapatite (HA), which constitutes the main mineral of the tooth enamel. Durapatite 67-81 statherin Homo sapiens 21-30 18054952-1 2008 The salivary protein statherin is known to adsorb selectively onto hydroxyapatite (HA), which constitutes the main mineral of the tooth enamel. Durapatite 83-85 statherin Homo sapiens 21-30 17060618-0 2006 Folding of the C-terminal bacterial binding domain in statherin upon adsorption onto hydroxyapatite crystals. Durapatite 85-99 statherin Homo sapiens 54-63 17391007-0 2007 Thermodynamic roles of basic amino acids in statherin recognition of hydroxyapatite. Durapatite 69-83 statherin Homo sapiens 44-53 17391007-1 2007 Salivary statherin is a highly acidic, 43 amino acid residue protein that functions as an inhibitor of primary and secondary crystallization of the biomineral hydroxyapatite. Durapatite 159-173 statherin Homo sapiens 9-18 17391007-2 2007 The acidic domain at the N-terminus was previously shown to be important in the binding of statherin to hydroxyapatite surfaces. Durapatite 104-118 statherin Homo sapiens 91-100 17389930-10 2007 The implications of this sulfation of statherin in hydroxyapatite binding and Actinomyces viscosus interactions are discussed. Durapatite 51-65 statherin Homo sapiens 38-47 18172904-0 2007 The structure, dynamics, and energetics of protein adsorption-lessons learned from adsorption of statherin to hydroxyapatite. Durapatite 110-124 statherin Homo sapiens 97-106 18172904-4 2007 Statherin is an enamel pellicle protein that inhibits hydroxyapatite nucleation and growth, lubricates the enamel surface, and is recognized by oral bacteria in periodontal diseases. Durapatite 54-68 statherin Homo sapiens 0-9 18172904-5 2007 Here, we highlight some of the insights we obtained recently using both thermodynamic and solid state NMR measurements to the adsorption process of statherin to hydroxyapatite. Durapatite 161-175 statherin Homo sapiens 148-157 17929924-0 2007 Structure prediction of protein-solid surface interactions reveals a molecular recognition motif of statherin for hydroxyapatite. Durapatite 114-128 statherin Homo sapiens 100-109 17929924-5 2007 We apply the method to the statherin-hydroxyapatite system, an evolved protein-surface interaction that is likely to have one or a few specific structural solutions. Durapatite 37-51 statherin Homo sapiens 27-36 17929924-8 2007 We also report the discovery of a molecular recognition motif where the N-terminal alpha-helix of statherin places all four of its basic residues to match the periodicity of open phosphate triad clusters across the [001] monoclinic face of the hydroxyapatite surface. Durapatite 244-258 statherin Homo sapiens 98-107 16671751-0 2006 Homonuclear and heteronuclear NMR studies of a statherin fragment bound to hydroxyapatite crystals. Durapatite 75-89 statherin Homo sapiens 47-56 16634639-0 2006 Thermodynamics of statherin adsorption onto hydroxyapatite. Durapatite 44-58 statherin Homo sapiens 18-27 16634639-1 2006 Statherin is a salivary protein that inhibits the nucleation and growth of hydroxyapatite crystals in the supersaturated environment of the oral cavity. Durapatite 75-89 statherin Homo sapiens 0-9 16634639-2 2006 The thermodynamics of adsorption of statherin onto hydroxyapatite crystals have been characterized here by isothermal titration calorimetry and equilibrium adsorption isotherm analysis. Durapatite 51-65 statherin Homo sapiens 36-45 16634639-6 2006 These results are interpreted using a two-site model for adsorption of statherin onto the hydroxyapatite crystals. Durapatite 90-104 statherin Homo sapiens 71-80 15984845-0 2005 A REDOR NMR study of a phosphorylated statherin fragment bound to hydroxyapatite crystals. Durapatite 66-80 statherin Homo sapiens 38-47 16620107-0 2006 A solid-state NMR study of the dynamics and interactions of phenylalanine rings in a statherin fragment bound to hydroxyapatite crystals. Durapatite 113-127 statherin Homo sapiens 85-94 14742521-3 2004 Here we used a hybrid peptide construct (with both a hydroxyapatite-binding portion and a test peptide portion) to map the interaction of Actinomyces species (and Candida albicans) with statherin. Durapatite 53-67 statherin Homo sapiens 186-195 10748043-0 2000 Chimeric peptides of statherin and osteopontin that bind hydroxyapatite and mediate cell adhesion. Durapatite 57-71 statherin Homo sapiens 21-30 12709513-4 2003 In particular, we have used ssNMR dipolar techniques to provide the first high-resolution structural and dynamic characterization of a hydrated biomineralization protein, salivary statherin, adsorbed to its biologically relevant hydroxyapatite (HAP) surface. Durapatite 229-243 statherin Homo sapiens 180-189 14530305-3 2003 Here we review early studies that have utilized solid-state NMR (ssNMR) techniques to provide in situ secondary-structure determination of statherin and statherin peptides on their biologically relevant hydroxyapatite (HAP) surfaces. Durapatite 203-217 statherin Homo sapiens 139-148 14530305-3 2003 Here we review early studies that have utilized solid-state NMR (ssNMR) techniques to provide in situ secondary-structure determination of statherin and statherin peptides on their biologically relevant hydroxyapatite (HAP) surfaces. Durapatite 203-217 statherin Homo sapiens 153-162 11747419-0 2001 Structure and dynamics of hydrated statherin on hydroxyapatite as determined by solid-state NMR. Durapatite 48-62 statherin Homo sapiens 35-44 11747419-3 2001 Here, we have used solid-state NMR techniques to provide the first high-resolution structural and dynamic characterization of a hydrated biomineralization protein, salivary statherin, adsorbed to its biologically relevant hydroxyapatite (HAP) surface. Durapatite 222-236 statherin Homo sapiens 173-182 11747419-3 2001 Here, we have used solid-state NMR techniques to provide the first high-resolution structural and dynamic characterization of a hydrated biomineralization protein, salivary statherin, adsorbed to its biologically relevant hydroxyapatite (HAP) surface. Durapatite 238-241 statherin Homo sapiens 173-182 9048421-8 1996 It appears that the strong binding affinity of statherin for hydroxyapatite can be attributed primarily to the N-terminal sequence, which prefers to adopted helical conformation and provides both electrostatic and hydrogen bonding interactions, thereby inhibiting its mineralization. Durapatite 61-75 statherin Homo sapiens 47-56 10419821-3 1999 Statherin is the only salivary protein currently known to inhibit both the primary and secondary precipitation of hydroxyapatite in the supersaturated environment of saliva. Durapatite 114-128 statherin Homo sapiens 0-9 7980121-1 1994 A constant composition (CC) method was used to compare the influence of statherin-like N-terminal 5-residue fragments having different amino acids in the terminal position on hydroxyapatite (HAP) growth and dissolution. Durapatite 175-189 statherin Homo sapiens 72-81 7980121-1 1994 A constant composition (CC) method was used to compare the influence of statherin-like N-terminal 5-residue fragments having different amino acids in the terminal position on hydroxyapatite (HAP) growth and dissolution. Durapatite 191-194 statherin Homo sapiens 72-81 1741693-0 1991 The effects of human salivary cystatins and statherin on hydroxyapatite crystallization. Durapatite 57-71 statherin Homo sapiens 44-53 8373992-3 1993 Using this model, the hydroxyapatite binding ability of statherin has been explained. Durapatite 22-36 statherin Homo sapiens 56-65 1663737-1 1991 Sequential chromatography of hydroxyapatite-adsorbed salivary proteins from submandibular/sublingual secretions on Sephadex G-50 and reversed-phase HPLC resulted in the purification of statherin and several statherin variants. Durapatite 29-43 statherin Homo sapiens 185-194 1663737-1 1991 Sequential chromatography of hydroxyapatite-adsorbed salivary proteins from submandibular/sublingual secretions on Sephadex G-50 and reversed-phase HPLC resulted in the purification of statherin and several statherin variants. Durapatite 29-43 statherin Homo sapiens 207-216 30994664-0 2019 Computer simulations of the adsorption of an N-terminal peptide of statherin, SN15, and its mutants on hydroxyapatite surfaces. Durapatite 103-117 statherin Homo sapiens 67-76 6429216-7 1984 At concentrations below these values, statherin inhibited spontaneous precipitation of calcium phosphate salts from an assay system which was more supersaturated with respect to dicalcium phosphate dihydrate, and comparably supersaturated with respect to hydroxyapatite, than were human saliva samples. Durapatite 255-269 statherin Homo sapiens 38-47 33118809-0 2020 Single-Molecule Force Spectroscopy Reveals Adhesion-by-Demand in Statherin at the Protein-Hydroxyapatite Interface. Durapatite 90-104 statherin Homo sapiens 65-74 30994664-2 2019 In this work, we investigated the solvent effect on the adsorption of a peptide from the N-terminus of statherin, SN15, and its mutants SNA15 and SNS15 on the (001) face of hydroxyapatite [Ca10(PO4)6(OH)2, or HAP] with molecular dynamics simulations. Durapatite 173-187 statherin Homo sapiens 103-112