PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32486091-3 2020 This sensory material is exploited in the selectivity detection of glycine in complex mixtures of amino acids mimicking elastin, collagen and epidermis, and also in following the protease activity in a beefsteak and chronic human wounds. Glycine 67-74 elastin Homo sapiens 120-127 33351193-2 2021 The rs2071307 genomic polymorphism, resulting in the substitution of a serine for a glycine residue in a VPG motif in tropoelastin, has an unusually high minor allele frequency in humans. Glycine 84-91 elastin Homo sapiens 118-130 6150137-6 1984 Elastin is composed largely of glycine, proline, and other hydrophobic residues and contains multiple lysine-derived cross-links, such as the desmosines, which link the individual polypeptide chains into a rubber-like network. Glycine 31-38 elastin Homo sapiens 0-7 15637-4 1976 The specificity of elastase is probably the same, since in elastin both enzymes hydrolyze the peptide bonds, formed by the NH2-group of glycine and alanine residues, found in elastin in large amounts. Glycine 136-143 elastin Homo sapiens 59-66 15637-4 1976 The specificity of elastase is probably the same, since in elastin both enzymes hydrolyze the peptide bonds, formed by the NH2-group of glycine and alanine residues, found in elastin in large amounts. Glycine 136-143 elastin Homo sapiens 175-182 29196110-6 2018 With regards to the cleavage behavior of neprilysin, a strong preference for Gly at P1 was found, while Gly, Ala and Val were well accepted at P1" upon cleavage of tropoelastin and skin elastin. Glycine 104-107 elastin Homo sapiens 164-176 31278967-9 2019 Pro, Gly and Ala were preferably found at P1-P4 and P2"-P4" in both tropoelastin and elastin. Glycine 5-8 elastin Homo sapiens 68-80 31278967-9 2019 Pro, Gly and Ala were preferably found at P1-P4 and P2"-P4" in both tropoelastin and elastin. Glycine 5-8 elastin Homo sapiens 73-80 29886015-5 2018 Monomeric elastin is a non-polar, glycine-rich, low-complexity, modular protein that remains predominantly disordered even in the crosslinked polymeric state, consistent with its function as an entropic elastomer. Glycine 34-41 elastin Homo sapiens 10-17 24127292-3 2014 Previously, Val-Pro-Gly-Val-Gly peptides have been conjugated to a dendrimer for designing an elastin-mimetic dendrimer. Glycine 20-23 elastin Homo sapiens 94-101 25363567-1 2015 A "double-hydrophobic" elastin-like triblock polypeptide GPG has been constructed by mimicking the localization of proline- and glycine-rich hydrophobic domains of native elastin, a protein that provides elasticity and resilience to connective tissues. Glycine 128-135 elastin Homo sapiens 23-30 25363567-1 2015 A "double-hydrophobic" elastin-like triblock polypeptide GPG has been constructed by mimicking the localization of proline- and glycine-rich hydrophobic domains of native elastin, a protein that provides elasticity and resilience to connective tissues. Glycine 128-135 elastin Homo sapiens 171-178 27736076-6 2016 We apply these methods to a family of short elastin-like peptides (ELPs), fragments of the elastin protein based around the Pro-Gly turn motif characteristic of the elastomeric segments of the full protein. Glycine 128-131 elastin Homo sapiens 44-51 27736076-6 2016 We apply these methods to a family of short elastin-like peptides (ELPs), fragments of the elastin protein based around the Pro-Gly turn motif characteristic of the elastomeric segments of the full protein. Glycine 128-131 elastin Homo sapiens 91-98 27028208-3 2016 Although elastin-derived polypeptide (Val-Pro-Gly-Val-Gly)n also has been known to demonstrate coacervation property, a sufficiently high (VPGVG)n repetition number (n>40) is required for coacervation. Glycine 46-49 elastin Homo sapiens 9-16 24127292-3 2014 Previously, Val-Pro-Gly-Val-Gly peptides have been conjugated to a dendrimer for designing an elastin-mimetic dendrimer. Glycine 28-31 elastin Homo sapiens 94-101 20947499-2 2010 The monomeric precursor, tropoelastin, is highly hydrophobic yet remains substantially disordered and flexible in solution, due in large part to a high combined threshold of proline and glycine residues within hydrophobic sequences. Glycine 186-193 elastin Homo sapiens 25-37 22899363-2 2012 Here, the results of variable-temperature (2) H NMR spectra are reported for hydrated elastin that has been enriched at the Halpha position in its abundant glycines. Glycine 156-164 elastin Homo sapiens 86-93 21509743-0 2011 Influence of amino acid specificities on the molecular and supramolecular organization of glycine-rich elastin-like polypeptides in water. Glycine 90-97 elastin Homo sapiens 103-110 21509743-4 2011 These sequences contain the repeat XxxGlyGlyZzzGly (Xxx, Zzz = Val, Leu) motif belonging to the hydrophobic glycine-rich domain of elastin and represent a simplified model from which to obtain information on molecular interactions functional to elastin itself. Glycine 108-115 elastin Homo sapiens 131-138 17098192-4 2006 The analysis of diverse sequences, including those of elastin, amyloids, spider silks, wheat gluten, and insect resilin, reveals a threshold in proline and glycine composition above which amyloid formation is impeded and elastomeric properties become apparent. Glycine 156-163 elastin Homo sapiens 54-61 20934468-5 2010 Here we fused the elastin derived peptide Ala-Pro-Gly-Val-Gly-Val (APGVGV) with the cell adhesive peptides, Pro-His-Ser-Arg-Asn (PHSRN) and Arg-Gly-Asp (RGD). Glycine 50-53 elastin Homo sapiens 18-25 17917856-1 2007 Extensive hydrogen bonding of dyes to connective tissue fibers is made possible by the high content of the amino acids proline and glycine in elastin and collagens. Glycine 131-138 elastin Homo sapiens 142-149 16081882-2 2005 Transfection studies with elastin cDNAs demonstrate that the glycine to aspartate change compromises the ability of the mutant protein to undergo normal elastin assembly. Glycine 61-68 elastin Homo sapiens 26-33 16081882-2 2005 Transfection studies with elastin cDNAs demonstrate that the glycine to aspartate change compromises the ability of the mutant protein to undergo normal elastin assembly. Glycine 61-68 elastin Homo sapiens 153-160 11179971-4 2001 To understand if its elastolytic activity results from a preference for glycine-rich substrates, we studied its ability to hydrolyse the 65 pentapeptides of human tropoelastin containing at least three glycines. Glycine 202-210 elastin Homo sapiens 163-175 16020665-1 2005 Elastin-like polypeptides are biopolymers composed of the pentapeptide repeat Val-Pro-Gly-Xaa-Gly. Glycine 86-89 elastin Homo sapiens 0-7 14606895-1 2003 The concentration dependence of the pressure- and temperature-induced cloud point transition (Pc and Tc, respectively) of aqueous solutions of an elastin-like polypeptide with a repeating pentapeptide Val-Pro-Gly-Ile-Gly sequence (MGLDGSMG(VPGIG)40VPLE) was investigated by using apparent light scattering, differential scanning calorimetry, and circular dichroism methods. Glycine 209-212 elastin Homo sapiens 146-153 12059197-0 2002 Observation of the glycines in elastin using (13)C and (15)N solid-state NMR spectroscopy and isotopic labeling. Glycine 19-27 elastin Homo sapiens 31-38 12059197-1 2002 We report the solid-state 13C and 15N NMR of insoluble elastin which has been synthesized in vitro with isotopically enriched glycine. Glycine 126-133 elastin Homo sapiens 55-62 12785105-2 2002 Its soluble precursor (tropoelastin) has two major types of alternating domains: (1) hydrophilic cross-linked domains rich in Lys and Ala and (2) hydrophobic domains (responsible for elasticity) rich in Val, Pro, and Gly, which often occur in repeats of VPGVG or VGGVG. Glycine 217-220 elastin Homo sapiens 23-35 11343278-2 2001 In the attempt to synthesize cross-linked elastin-mimetic polypeptides, the repeating sequence VGGVG (V: valine; G: glycine), typical of elastin, was modified to incorporate lysine residues, yielding the polymer poly(KGGVG) (K: lysine). Glycine 116-123 elastin Homo sapiens 42-49 11343278-2 2001 In the attempt to synthesize cross-linked elastin-mimetic polypeptides, the repeating sequence VGGVG (V: valine; G: glycine), typical of elastin, was modified to incorporate lysine residues, yielding the polymer poly(KGGVG) (K: lysine). Glycine 116-123 elastin Homo sapiens 137-144 11911775-5 2002 It has been suggested that these hydrophobic domains, predominantly containing glycine, proline, leucine and valine, often occurring in tandemly repeated sequences, are responsible for the ability of elastin to align monomeric chains for covalent cross-linking. Glycine 79-86 elastin Homo sapiens 200-207 10825173-3 2000 The tropoelastin-binding site was localized to a region beginning at the glycine-rich and proline-rich regions of fibrillin-2 and fibrillin-1, respectively, and continuing through the second 8-cysteine domain. Glycine 73-80 elastin Homo sapiens 4-16 11727705-5 2001 It is particularly true for human tropoelastin, because its sequence is rich in glycines and prolines, and these residues are frequently met in beta-turns (a beta-turn is made of four consecutive residues which are stabilized by an hydrogen bond). Glycine 80-88 elastin Homo sapiens 34-46 7669266-0 1995 Conformational modeling of elastin tetrapeptide Boc-Gly-Leu-Gly-Gly-NMe by molecular dynamics simulations with improvements to the thermalization procedure. Glycine 52-55 elastin Homo sapiens 27-34 9092525-10 1997 N-terminal amino acid sequencing of two fragments derived from soluble elastin indicated that both resulted from cleavages of Gly-Ala peptide bonds located within similar sequences, Pro-Gly-Val-Gly-Gly-Ala-Xaa (where Xaa is Phe or Gly). Glycine 126-129 elastin Homo sapiens 71-78 9092525-10 1997 N-terminal amino acid sequencing of two fragments derived from soluble elastin indicated that both resulted from cleavages of Gly-Ala peptide bonds located within similar sequences, Pro-Gly-Val-Gly-Gly-Ala-Xaa (where Xaa is Phe or Gly). Glycine 186-189 elastin Homo sapiens 71-78 9092525-13 1997 The present results suggest that LasA is a zinc metalloendopeptidase selective for Gly-Ala peptide bonds within Gly-Gly-Ala sequences in elastin. Glycine 83-86 elastin Homo sapiens 137-144 9092525-13 1997 The present results suggest that LasA is a zinc metalloendopeptidase selective for Gly-Ala peptide bonds within Gly-Gly-Ala sequences in elastin. Glycine 112-115 elastin Homo sapiens 137-144 9092525-13 1997 The present results suggest that LasA is a zinc metalloendopeptidase selective for Gly-Ala peptide bonds within Gly-Gly-Ala sequences in elastin. Glycine 112-115 elastin Homo sapiens 137-144 9218437-5 1997 The predominant amino acids detected by protein sequence analysis following cleavage of insoluble elastin with HME, MME, and 92-kDa gelatinase were Leu, Ile, Ala, Gly, and Val. Glycine 163-166 elastin Homo sapiens 98-105 9218437-8 1997 The amino acid residues detected in insoluble elastin following hydrolysis with porcine pancreatic elastase and human neutrophil elastase were predominantly Gly and Ala, with lesser amounts of Val, Phe, Ile, and Leu. Glycine 157-160 elastin Homo sapiens 46-53 8405806-4 1993 Elastin is found throughout the vertebrate kingdom and possesses an unusual chemical composition rich in glycine, proline, and hydrophobic amino acids, consonant with its characteristic physical properties. Glycine 105-112 elastin Homo sapiens 0-7 1492919-2 1992 Poly (Val-Gly-Gly-Leu-Gly), a polypeptide mimicking the physico-chemical properties of the glycine-rich regions of elastin, has been synthesized and studied both in solution and in the aggregated state. Glycine 91-98 elastin Homo sapiens 115-122 8344932-6 1993 Analysis of the amino acid composition of elastin-derived peptide indicates the presence of alanine, glycine, and richness in hydrophobic residues, suggesting that these residues are involved in elastase interaction(s). Glycine 101-108 elastin Homo sapiens 42-49 8472268-8 1993 Elastin from dissected aortas had a higher content of aspartate, threonine, serine, glutamate, and lysine and a lower content of glycine, alanine, and valine than elastin from controls (p < 0.05). Glycine 129-136 elastin Homo sapiens 0-7 35207427-0 2022 A Rationalization of the Effect That TMAO, Glycine, and Betaine Exert on the Collapse of Elastin-like Polypeptides. Glycine 43-50 elastin Homo sapiens 89-96 2386811-9 1990 We propose that in the repeating sequences of elastin an equilibrium exists between a gamma-turn structure and a beta-turn structure in the Pro-Gly segment resulting in a structure that combines flexibility with strong conformational preferences. Glycine 144-147 elastin Homo sapiens 46-53 34676744-2 2021 On the other hand, glycine-rich sequences, mainly present in tropoelastin terminal domains, are responsible for the elastin self-assembly. Glycine 19-26 elastin Homo sapiens 116-123 34676744-3 2021 In a previous study, we have recombinantly expressed a chimeric polypeptide, named resilin, elastin, and collagen (REC), inspired by glycine-rich motifs of elastin and containing resilin and collagen sequences as well. Glycine 133-140 elastin Homo sapiens 92-99 34676744-3 2021 In a previous study, we have recombinantly expressed a chimeric polypeptide, named resilin, elastin, and collagen (REC), inspired by glycine-rich motifs of elastin and containing resilin and collagen sequences as well. Glycine 133-140 elastin Homo sapiens 156-163