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Journal articles on the topic 'GXXPG peptides'

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

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Thinnes, Friedrich P. "Alzheimer disease controls cancer — Concerning the apoptogenic interaction of cell membrane-standing type-1 VDAC and amyloid peptides via GxxxG motifs." Molecular Genetics and Metabolism 106, no. 4 (2012): 502–3. http://dx.doi.org/10.1016/j.ymgme.2012.06.004.

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12

Thinnes, Friedrich P. "Apoptogenic interactions of plasmalemmal type-1 VDAC and Aβ peptides via GxxxG motifs induce Alzheimer's disease – a basic model of apoptosis?*". Wiener Medizinische Wochenschrift 161, № 9-10 (2011): 274–76. http://dx.doi.org/10.1007/s10354-011-0887-5.

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13

Liu, Lei, Bianca M. Lauro, Michael S. Wolfe та Dennis J. Selkoe. "Hydrophilic loop 1 of Presenilin-1 and the APP GxxxG transmembrane motif regulate γ-secretase function in generating Alzheimer-causing Aβ peptides". Journal of Biological Chemistry 296 (січень 2021): 100393. http://dx.doi.org/10.1016/j.jbc.2021.100393.

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14

Harmeier, Anja, Manuel Gensler, Christian Barucker, et al. "P2-215: Aggregation of Aß42 is strongly influenced by Gly33 of the GxxxG motif and an inhibitor peptide which mimics Gly33 substitutions." Alzheimer's & Dementia 7 (July 2011): S381. http://dx.doi.org/10.1016/j.jalz.2011.05.1098.

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15

Albert, Isabell, Lisha Zhang, Hannah Bemm, and Thorsten Nürnberger. "Structure-Function Analysis of Immune Receptor AtRLP23 with Its Ligand nlp20 and Coreceptors AtSOBIR1 and AtBAK1." Molecular Plant-Microbe Interactions® 32, no. 8 (2019): 1038–46. http://dx.doi.org/10.1094/mpmi-09-18-0263-r.

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Pattern-triggered immunity is an inherent feature of the plant immune system. Recognition of either microbe-derived surface structures (patterns) or of plant materials released due to the deleterious impact of microbial infection is brought about by plasma membrane pattern recognition receptors (PRRs). PRRs composed of leucine-rich repeat (LRR) ectodomains are thought to mediate sensing of proteinaceous patterns and to initiate signaling cascades culminating in the activation of generic plant defenses. In contrast to LRR receptor kinases, LRR receptor proteins (LRR-RPs) lack a cytoplasmic kina
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16

Rodríguez Nassif, Aslin, Igor de la Arada, José Luis Arrondo, and Belinda Pastrana-Rios. "2D IR Correlation Spectroscopy in the Determination of Aggregation and Stability of KH Domain GXXG Loop Peptide in the Presence and Absence of Trifluoroacetate." Analytical Chemistry 89, no. 11 (2017): 5765–75. http://dx.doi.org/10.1021/acs.analchem.6b04800.

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17

Faingold, Omri, Tomer Cohen, and Yechiel Shai. "A GxxxG-like Motif within HIV-1 Fusion Peptide Is Critical to Its Immunosuppressant Activity, Structure, and Interaction with the Transmembrane Domain of the T-cell Receptor." Journal of Biological Chemistry 287, no. 40 (2012): 33503–11. http://dx.doi.org/10.1074/jbc.m112.370817.

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18

Li, Wei, Douglas Metcalf, Roman Gorelik та ін. "Heteromeric and Homomeric Transmembrane Domain Associations Regulate αIIbβ3 Function." Blood 104, № 11 (2004): 329. http://dx.doi.org/10.1182/blood.v104.11.329.329.

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Abstract The integrin αIIbβ3 resides on the platelet surface in an equilibrium between inactive and active conformations that can be shifted in either direction by altering the distance between the stalks that anchor αIIbβ3 in the platelet membrane. Accordingly, the αIIb and β3 transmembrane (TM) domains, located near the ends of the stalks, are in proximity when αIIbβ3 is inactive and separate upon αIIbβ3 activation. Peptides corresponding to these domains undergo both homomeric and heteromeric interactions in biological membranes. Thus, it is possible that the shift between inactive and acti
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19

Chadwick, Alexandra C., Davin R. Jensen, Francis C. Peterson, Brian F. Volkman, and Daisy Sahoo. "Abstract 104: NMR Analyses of the Structural and Oligomeric Properties of the C-terminal Transmembrane Domain of SR-BI in Detergent Micelles." Arteriosclerosis, Thrombosis, and Vascular Biology 35, suppl_1 (2015). http://dx.doi.org/10.1161/atvb.35.suppl_1.104.

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In the reverse cholesterol transport pathway, high density lipoprotein (HDL) carries cholesterol from peripheral tissues to the liver for excretion via bile formation following interaction of HDL with its receptor, scavenger receptor BI (SR-BI). Due to the absence of a high-resolution structure of SR-BI, our understanding of receptor-ligand interactions between SR-BI and HDL that lead to whole body cholesterol removal remain limited. Our laboratory has demonstrated that oligomerization of SR-BI, likely mediated by its C-terminal transmembrane domain (C-TMD), facilitates delivery of HDL-cholest
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