Relevant bibliographies by topics / GXXPG peptides

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  2. Dissertations / Theses

Academic literature on the topic 'GXXPG peptides'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "GXXPG peptides"

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Sellami, Mehdi, Aïda Meghraoui-Kheddar, Christine Terryn, et al. "Induction and regulation of murine emphysema by elastin peptides." American Journal of Physiology-Lung Cellular and Molecular Physiology 310, no. 1 (2016): L8—L23. http://dx.doi.org/10.1152/ajplung.00068.2015.

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Emphysema is the major component of chronic obstructive pulmonary disease (COPD). During emphysema, elastin breakdown in the lung tissue originates from the release of large amounts of elastase by inflammatory cells. Elevated levels of elastin-derived peptides (EP) reflect massive pulmonary elastin breakdown in COPD patients. Only the EP containing the GXXPG conformational motif with a type VIII β-turn are elastin receptor ligands inducing biological activities. In addition, the COOH-terminal glycine residue of the GXXPG motif seems a prerequisite to the biological activity. In this study, we
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Yin, Hang, Hua Zhu, Gaston Vilaire та ін. "Activation of Platelet α Iibβ 3 by Exogenous Peptides Corresponding to the Transmembrane Domains of α Iib and β 3." Blood 106, № 11 (2005): 384. http://dx.doi.org/10.1182/blood.v106.11.384.384.

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Abstract The platelet fibrinogen receptor α IIbβ 3 exists in an equilibrium between inactive and active conformations. In its inactive conformation, the transmembrane (TM) domains of α IIb and β 3 interact, but they separate when α IIbβ 3 assumes its active conformation. Peptides corresponding to the α IIb TM domain form homodimers in vitro and in bacterial membranes and the interface that mediates this interaction overlaps with the interface that mediates the heteromeric association of the α IIb TM domain with that of β 3. Because the homomeric association of α IIb TM domain is relatively str
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Roth, Lise, Cécile Nasarre, Sylvie Dirrig-Grosch, et al. "Transmembrane Domain Interactions Control Biological Functions of Neuropilin-1." Molecular Biology of the Cell 19, no. 2 (2008): 646–54. http://dx.doi.org/10.1091/mbc.e07-06-0625.

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Neuropilin-1 (NRP1) is a transmembrane receptor playing a pivotal role in the control of semaphorins and VEGF signaling pathways. The exact mechanism controlling semaphorin receptor complex formation is unknown. A structural analysis and modeling of NRP1 revealed a putative dimerization GxxxG motif potentially important for NRP1 dimerization and oligomerization. Our data show that this motif mediates the dimerization of the transmembrane domain of NRP1 as demonstrated by a dimerization assay (ToxLuc assay) performed in natural membrane and FRET analysis. A synthetic peptide derived from the tr
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Oppegård, Camilla, Gunnar Fimland, Lisbeth Thorbæk, and Jon Nissen-Meyer. "Analysis of the Two-Peptide Bacteriocins Lactococcin G and Enterocin 1071 by Site-Directed Mutagenesis." Applied and Environmental Microbiology 73, no. 9 (2007): 2931–38. http://dx.doi.org/10.1128/aem.02718-06.

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ABSTRACT The two peptides (Lcn-α and Lcn-β) of the two-peptide bacteriocin lactococcin G (Lcn) were changed by stepwise site-directed mutagenesis into the corresponding peptides (Ent-α and Ent-β) of the two-peptide bacteriocin enterocin 1071 (Ent), and the potencies and specificities of the various hybrid constructs were determined. Both Lcn and, to a lesser extent, Ent were active against all the tested lactococcal strains, but only Ent was active against the tested enterococcal strains. The two bacteriocins thus differed in their relative potencies to various target cells, despite their sequ
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Moroy, Gautier, Alain J. P. Alix, and Stéphanie Héry-Huynh. "Structural characterization of human elastin derived peptides containing the GXXP sequence." Biopolymers 78, no. 4 (2005): 206–20. http://dx.doi.org/10.1002/bip.20276.

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Escamilla-Martínez, E. E., Y. M. Álvarez Cisneros, F. J. Fernández, M. Quirasco-Baruch, and E. Ponce-Alquicira. "Identification of Structural and Immunity Genes of a Class IIb Bacteriocin Encoded in the Enterocin A Operon of Enterococcus faecium Strain MXVK29." Journal of Food Protection 80, no. 11 (2017): 1851–56. http://dx.doi.org/10.4315/0362-028x.jfp-17-039.

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ABSTRACT The Enterococcus faecium strain MXVK29, isolated from fermented sausages, produces a bacteriocin with a molecular mass of 3.5 kDa that belongs to the class of enterocins II.1, according to the terminal amino acid sequence, and has been identified as enterocin A. This bacteriocin is active against selected strains of Listeria, Staphylococcus, Pediococcus, and Enterococcus. In this study, we identified the genes adjacent to the structural gene for this bacteriocin, such as the immunity gene (entI) and the inducer gene (entF). Accessory genes for this bacteriocin, such as entK, entR, and
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Yin, Hang, Joanna S. Slusky, Bryan W. Berger та ін. "Regulation of the Function of αvβ3 in Platelets by a Designed Peptide Targeting the αv Transmembrane Domain." Blood 108, № 11 (2006): 1504. http://dx.doi.org/10.1182/blood.v108.11.1504.1504.

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Abstract Integrins reside on cell surfaces in an equilibrium between inactive and active conformations. When inactive, the transmembrane (TM) domains of integrin α and β subunits interact, but the domains separate when integrins assume their active conformation. Although this conformational change has not been shown for αvβ3, we hypothesized that a peptide designed to bind to the αv TM domain might activate αvβ3 in platelets by disrupting the TM domain heterodimer of the inactive molecule. To design such a peptide, we used CHAMP (Computed Helical Anti-Membrane Protein) methodology. In the CHAM
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Sarkar, Dibakar, Ipsita Chakraborty, Marcello Condorelli та ін. "Self‐Assembly and Neurotoxicity of β‐Amyloid (21–40) Peptide Fragment: The Regulatory Role of GxxxG Motifs". ChemMedChem 15, № 3 (2019): 293–301. http://dx.doi.org/10.1002/cmdc.201900620.

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Carlier, Ludovic, Pierre Joanne, Lucie Khemtémourian, et al. "Investigating the role of GXXXG motifs in helical folding and self-association of plasticins, Gly/Leu-rich antimicrobial peptides." Biophysical Chemistry 196 (January 2015): 40–52. http://dx.doi.org/10.1016/j.bpc.2014.09.004.

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Oppegård, Camilla, Juliane Schmidt, Per Eugen Kristiansen, and Jon Nissen-Meyer. "Mutational Analysis of Putative Helix−Helix Interacting GxxxG-Motifs and Tryptophan Residues in the Two-Peptide Bacteriocin Lactococcin G†." Biochemistry 47, no. 18 (2008): 5242–49. http://dx.doi.org/10.1021/bi800289w.

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Dissertations / Theses on the topic "GXXPG peptides"

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Robinet, Julien. "Les peptides GXXPG : nouvelles molécules thérapeutiques à visée régénératrice osseuse ?" Thesis, Reims, 2014. http://www.theses.fr/2014REIMS009/document.

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La cicatrisation de défauts osseux permet tout au plus une réparation de l'os et dans peu de cas, une régénération ad integrum. Le développement de biomatériaux issus de l'ingénierie tissulaire en vue d'une régénération osseuse est donc un enjeu majeur. Le but de cette étude a été d'évaluer si des peptides GXXPG issus de l'élastine sont capables de favoriser la différenciation ostéoblastique de cellules mésenchymateuses dérivées de la moelle osseuse humaine (CMMO) ainsi que la formation de la matrice osseuse et sa minéralisation. Pour y répondre, nous avons utilisés les lattis de collagène de
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Harmeier, Anja [Verfasser]. "Aggregation, Struktur und pathologische Wirkung des Amyloid-ß-Peptides : die Rolle des GxxxG-Motivs / Anja Harmeier." Berlin : Freie Universität Berlin, 2009. http://d-nb.info/1023404060/34.

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Joanne, Pierre. "Les plasticines, peptides antibactériens de la peau de grenouille : versatilité fonctionnelle, adaptabilité des structures et des interactions membranaires." Paris 6, 2009. http://www.theses.fr/2009PA066464.

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La famille des plasticines se compose de peptides antibactériens issus de la peau de grenouilles arboricoles d’Amérique du Sud. Ces peptides se distinguent par une séquence riche en glycine et en leucine et par la présence de motifs GXXXG, connus pour favoriser les interactions entre hélices transmembranaires. Leur plasticité structurale permet peut expliquer les subtiles différences de propriétés biologiques ainsi que la versatilité fonctionnelle de ces peptides. En conséquence, pour mieux comprendre les mécanismes d’actions de ces peptides, trois axes ont été développés, (1) études des activ
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