PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 3910310-13 1985 Arterial smooth muscle cells increase their uptake of elastin precursors (particularly proline) when subjected to intermittent distension (Leung et al, 1976) and this may form a common link in the changes generated in vascular and colonic muscle tissue with time. Proline 87-94 elastin Homo sapiens 54-61 7228489-0 1981 Conformation characterization of cyclopentapeptide, L.Val-L.Pro-Gly-L.Val-Gly: a repeating analogue of elastin. Proline 60-63 elastin Homo sapiens 103-110 7104383-8 1982 The change in elastin concentration was accompanied by high hydroxyproline/proline or hydroxylysine/lysine ratios which indicates that the proteins of the aneurysmatic aortic wall contained more collagen than the proteins of the control aortic wall. Proline 67-74 elastin Homo sapiens 14-21 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. Proline 40-47 elastin Homo sapiens 0-7 27180175-8 2016 The fact that the highest hydroxylation degrees of proline residues were found for elastin from the intervertebral disc and knowledge of elastin arrangement in this tissue suggest that hydroxylation plays a biomechanical role. Proline 51-58 elastin Homo sapiens 83-90 31433165-0 2019 Detection of Labile Conformations of Elastin"s Prolines by Solid-State Nuclear Magnetic Resonance and Fourier Transform Infrared Techniques. Proline 47-55 elastin Homo sapiens 37-44 29461832-2 2018 We find that the alanine-rich cross-linking domains of elastin have a partially helical structure, but only when capped by proline-rich hydrophobic domains. Proline 123-130 elastin Homo sapiens 55-62 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. Proline 124-127 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. Proline 124-127 elastin Homo sapiens 91-98 31278967-9 2019 Pro, Gly and Ala were preferably found at P1-P4 and P2"-P4" in both tropoelastin and elastin. Proline 0-3 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. Proline 0-3 elastin Homo sapiens 73-80 27180175-9 2016 Interestingly, a proline-rich domain of tropoelastin (domain 24), which contains several repeats of bioactive motifs, does not show any hydroxyproline residues in the mammals studied. Proline 17-24 elastin Homo sapiens 40-52 27311421-8 2016 With respect to the molecular-level structure, it was found that the proline hydroxylation degree differed between WBS and healthy elastin, while the tropoelastin isoform appeared to be the same. Proline 69-76 elastin Homo sapiens 131-138 25636538-4 2015 Of the 20 MMPs identified, MMP-1, MMP-2, MMP-8, MMP-9, and MMP-12 have been implicated in regulating the matrikines Val-Gly-Val-Ala-Pro-Gly (elastin peptide) and proline-glycine-proline (PGP). Proline 162-169 elastin Homo sapiens 141-148 26763595-3 2016 While structural disorder of hydrophobic sequences is controlled by a high proline and glycine residue composition, hydrophobic domain 30 of human tropoelastin is atypically proline-poor, and forms beta-sheet amyloid-like fibrils as an individual peptide. Proline 174-181 elastin Homo sapiens 147-159 26110966-1 2015 The solubility-enhancing power of covalent attachment to solvent-swollen cross-linked resin supports was illustrated by syntheses of the highly aggregating elastin-derived 10-residue peptide sequence Pro-Gly-Val-Gly-Val-Pro-Gly-Val-Gly-Val using standard protocols for both Boc and Fmoc chemistry SPPS. Proline 200-204 elastin Homo sapiens 156-163 25924982-0 2015 Proline-poor hydrophobic domains modulate the assembly and material properties of polymeric elastin. Proline 0-7 elastin Homo sapiens 92-99 25924982-4 2015 However, the native sequence of hydrophobic elastin domain 30 is uncharacteristically proline-poor and, as an isolated polypeptide, is susceptible to formation of amyloid-like structures comprised of stacked beta-sheet. Proline 86-93 elastin Homo sapiens 44-51 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. Proline 115-122 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. Proline 115-122 elastin Homo sapiens 171-178 24106871-8 2013 The ability of FKBP65 to modulate the self-assembly of tropoelastin is independent of its enzymatic activity to promote the cis-trans isomerization of proline residues in proteins. Proline 151-158 elastin Homo sapiens 55-67 24127724-5 2013 Here we show that Hyp-containing elastin polypeptides have flexible molecular structures, analogously to proline-containing polypeptides. Proline 105-112 elastin Homo sapiens 33-40 24127724-9 2013 Furthermore, our results could contribute in defining the subtle role of proline structural variants in the folding and self-assembly of elastin-inspired peptides, helping the rational design of elastin biomaterials. Proline 73-80 elastin Homo sapiens 137-144 24127724-9 2013 Furthermore, our results could contribute in defining the subtle role of proline structural variants in the folding and self-assembly of elastin-inspired peptides, helping the rational design of elastin biomaterials. Proline 73-80 elastin Homo sapiens 195-202 22356513-6 2012 Of particular interest was the Val variant commonly found in the protein elastin, which contained a 25% population of irregular beta turns containing two peptide hydrogen bonds to the proline C O. Proline 184-191 elastin Homo sapiens 73-80 20947499-0 2010 Proline periodicity modulates the self-assembly properties of elastin-like polypeptides. Proline 0-7 elastin Homo sapiens 62-69 21487760-0 2011 Defect in proline synthesis: pyrroline-5-carboxylate reductase 1 deficiency leads to a complex clinical phenotype with collagen and elastin abnormalities. Proline 10-17 elastin Homo sapiens 132-139 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. Proline 174-181 elastin Homo sapiens 25-37 20947499-3 2010 In fact, proline-poor elastin-like sequences are known to form amyloid-like fibrils, rich in beta-structure, from solution. Proline 9-16 elastin Homo sapiens 22-29 20947499-5 2010 However, a small number of hydrophobic domains near the C terminus of tropoelastin are substantially depleted of proline residues. Proline 113-120 elastin Homo sapiens 70-82 20947499-6 2010 Here we investigated the specific contribution of proline number and spacing to the structure and self-assembly propensities of elastin-like polypeptides. Proline 50-57 elastin Homo sapiens 128-135 20947499-10 2010 These data strongly support a model where proline-poor regions of the elastin monomer provide a unique contribution to assembly and suggest a role for localized beta-sheet in mediating self-assembly interactions. Proline 42-49 elastin Homo sapiens 70-77 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. Proline 144-151 elastin Homo sapiens 54-61 20681719-1 2010 Prolyl 4-hydroxylases install a hydroxyl group in the 4R configuration on the gamma-carbon atom of certain (2S)-proline (Pro) residues in tropocollagen, elastin, and other proteins to form (2S,4R)-4-hydroxyproline (Hyp). Proline 0-3 elastin Homo sapiens 153-160 18972488-0 2008 Conformational dynamics of minimal elastin-like polypeptides: the role of proline revealed by molecular dynamics and nuclear magnetic resonance. Proline 74-81 elastin Homo sapiens 35-42 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. Proline 119-126 elastin Homo sapiens 142-149 16161116-6 2005 The cleavage sites of the enzyme and, for the first time, the extent and location of proline hydroxylation in human skin elastin were determined. Proline 85-92 elastin Homo sapiens 121-128 16366565-0 2005 A stereoelectronic effect on turn formation due to proline substitution in elastin-mimetic polypeptides. Proline 51-58 elastin Homo sapiens 75-82 16366565-4 2005 Calorimetric and spectroscopic investigations of these three polypeptides indicate that the incorporation of the substituted proline residues had a dramatic effect upon the self-assembly of the corresponding elastin peptide. Proline 125-132 elastin Homo sapiens 208-215 16366565-6 2005 These results suggest that stereoelectronic effects could either enhance or hinder the self-assembly of elastin-mimetic polypeptides, depending on the influence of the proline analogue on the energetics of the beta-turn conformation that develops within the pentapeptide structural repeats above the phase transition. Proline 168-175 elastin Homo sapiens 104-111 16366565-8 2005 The results of the these calculations suggested a similar outcome to the experimental data for the elastin-mimetic polypeptides, in that type II beta-turn structures were stabilized for peptide segments containing (2S,4R)-fluoroproline and destabilized for segments containing (2S,4S)-fluoroproline relative to the canonical proline residue. Proline 228-235 elastin Homo sapiens 99-106 12031628-2 2002 beta-spirals using canonical proline-nucleated beta-turns in diverse proteins allow for vital functions including structural (mucin and amelogenin), respiratory (elastin), muscular (titin), and that of genetic expression (RNA polymerase II). Proline 29-36 elastin Homo sapiens 162-169 14625282-12 2004 This view is supported by recent studies of recombinant elastin polypeptides with systematic proline substitutions. Proline 93-100 elastin Homo sapiens 56-63 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. Proline 205-208 elastin Homo sapiens 146-153 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. Proline 88-95 elastin Homo sapiens 200-207 1742165-1 1991 Poly(X-Gly-Gly), simple structural models for the hydrophobic, proline-devoid, regions of elastin, have been synthesized and studied by circular dichroism and NMR spectroscopies. Proline 63-70 elastin Homo sapiens 90-97 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. Proline 208-211 elastin Homo sapiens 23-35 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). Proline 93-101 elastin Homo sapiens 34-46 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. Proline 90-97 elastin Homo sapiens 4-16 11723825-1 2001 Elastin is the main protein of elastic fibers and confers the property of elastic recoil to the tissues such as arteries, lung, elastic cartilage,... Elastin synthesis goes through several steps: gene transcription, alternative splicing of pre-mRNA, mRNA translation, hydroxylation of some proline residues of the newly synthesized protein-tropoelastin-, association of with a 67 kDa chaperone protein, secretion of tropoelastin molecules in the extracellular space, and their deposition on the microfibrillar scaffold which contains fibrillin 1, fibrillin 2, MAGP 1 and MAGP 2,.... After the synthesis of cross-links-lysinonorleucine, desmosine, isodesmosine-, elastin becomes insoluble and elastic. Proline 290-297 elastin Homo sapiens 0-7 11723825-1 2001 Elastin is the main protein of elastic fibers and confers the property of elastic recoil to the tissues such as arteries, lung, elastic cartilage,... Elastin synthesis goes through several steps: gene transcription, alternative splicing of pre-mRNA, mRNA translation, hydroxylation of some proline residues of the newly synthesized protein-tropoelastin-, association of with a 67 kDa chaperone protein, secretion of tropoelastin molecules in the extracellular space, and their deposition on the microfibrillar scaffold which contains fibrillin 1, fibrillin 2, MAGP 1 and MAGP 2,.... After the synthesis of cross-links-lysinonorleucine, desmosine, isodesmosine-, elastin becomes insoluble and elastic. Proline 290-297 elastin Homo sapiens 150-157 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. Proline 114-121 elastin Homo sapiens 0-7 1913589-8 1991 The results focused on the importance of efficient proline re-utilization for normal collagen and elastin synthesis and deposition. Proline 51-58 elastin Homo sapiens 98-105 1848551-12 1991 The binding of apo(a) to proline and hydroxyproline could be responsible for the binding of apo(a) to the subendothelial extracellular matrix, i.e. domains of proteins rich in proline or hydroxyproline (e.g. collagen and elastin). Proline 25-32 elastin Homo sapiens 221-228 1848551-12 1991 The binding of apo(a) to proline and hydroxyproline could be responsible for the binding of apo(a) to the subendothelial extracellular matrix, i.e. domains of proteins rich in proline or hydroxyproline (e.g. collagen and elastin). Proline 44-51 elastin Homo sapiens 221-228 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. Proline 140-143 elastin Homo sapiens 46-53 34424695-0 2021 Proline Isomerization Regulates the Phase Behavior of Elastin-Like Polypeptides in Water. Proline 0-7 elastin Homo sapiens 54-61 35124875-0 2022 The Effects of Proline Isomerization on the Solvation Behavior of Elastin-Like Polypeptides in Water-Ethanol Mixtures. Proline 15-22 elastin Homo sapiens 66-73