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Relevant bibliographies by topics / Peptidyl-prolyl cis

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Academic literature on the topic 'Peptidyl-prolyl cis'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "Peptidyl-prolyl cis"

1

Schiene-Fischer, Cordelia. "Multidomain Peptidyl Prolyl cis/trans Isomerases." Biochimica et Biophysica Acta (BBA) - General Subjects 1850, no. 10 (October 2015): 2005–16. http://dx.doi.org/10.1016/j.bbagen.2014.11.012.

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Maruyama, Tadashi. "Archaeal peptidyl prolyl cis-trans isomerases (PPIases)." Frontiers in Bioscience 5, no. 1 (2000): d821. http://dx.doi.org/10.2741/maruyama.

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Maruyama, Tadashi. "Archaeal peptidyl prolyl cis-trans isomerases PPIases." Frontiers in Bioscience 5, no. 3 (2000): d821–836. http://dx.doi.org/10.2741/a554.

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Paillares, Eléa, Maud Marechal, Léa Swistak, Landry Tsoumtsa Meda, Emmanuel Lemichez, and Thérèse E. Malliavin. "Conformational Insights into the Control of CNF1 Toxin Activity by Peptidyl-Prolyl Isomerization: A Molecular Dynamics Perspective." International Journal of Molecular Sciences 22, no. 18 (September 20, 2021): 10129. http://dx.doi.org/10.3390/ijms221810129.

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The cytotoxic necrotizing factor 1 (CNF1) toxin from uropathogenic Escherichia coli constitutively activates Rho GTPases by catalyzing the deamidation of a critical glutamine residue located in the switch II (SWII). In crystallographic structures of the CNF1 catalytic domain (CNF1CD), surface-exposed P768 and P968 peptidyl-prolyl imide bonds (X-Pro) adopt an unusual cis conformation. Here, we show that mutation of each proline residue into glycine abrogates CNF1CD in vitro deamidase activity, while mutant forms of CNF1 remain functional on RhoA in cells. Using molecular dynamics simulations coupled to protein-peptide docking, we highlight the long-distance impact of peptidyl-prolyl cis-trans isomerization on the network of interactions between the loops bordering the entrance of the catalytic cleft. The energetically favorable isomerization of P768 compared with P968, induces an enlargement of loop L1 that fosters the invasion of CNF1CD catalytic cleft by a peptide encompassing SWII of RhoA. The connection of the P968 cis isomer to the catalytic cysteine C866 via a ladder of stacking interactions is alleviated along the cis-trans isomerization. Finally, the cis-trans conversion of P768 favors a switch of the thiol side chain of C866 from a resting to an active orientation. The long-distance impact of peptidyl-prolyl cis-trans isomerizations is expected to have implications for target modification.

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Galat, Andrzej. "Introduction to Peptidyl-Prolyl cis/trans Isomerase (PPIase) Series." Biomolecules 9, no. 2 (February 20, 2019): 74. http://dx.doi.org/10.3390/biom9020074.

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About 30 years after the discovery of peptidyl-prolyl cis/trans isomerases (PPIases), research on this group of proteins has become somewhat calmer than it used to be, but it still generates lots of interest [...]

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Troilo, Francesca, Francesca Malagrinò, Lorenzo Visconti, Angelo Toto, and Stefano Gianni. "The Effect of Proline cis-trans Isomerization on the Folding of the C-Terminal SH2 Domain from p85." International Journal of Molecular Sciences 21, no. 1 (December 23, 2019): 125. http://dx.doi.org/10.3390/ijms21010125.

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SH2 domains are protein domains that modulate protein–protein interactions through a specific interaction with sequences containing phosphorylated tyrosines. In this work, we analyze the folding pathway of the C-terminal SH2 domain of the p85 regulatory subunit of the protein PI3K, which presents a proline residue in a cis configuration in the loop between the βE and βF strands. By employing single and double jump folding and unfolding experiments, we demonstrate the presence of an on-pathway intermediate that transiently accumulates during (un)folding. By comparing the kinetics of folding of the wild-type protein to that of a site-directed variant of C-SH2 in which the proline was replaced with an alanine, we demonstrate that this intermediate is dictated by the peptidyl prolyl cis-trans isomerization. The results are discussed in the light of previous work on the effect of peptidyl prolyl cis-trans isomerization on folding events.

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Maruyama, Tadashi. "Archaeal peptidyl prolyl cis-trans isomerases (PPIases) update 2004." Frontiers in Bioscience 9, no. 1-3 (2004): 1680. http://dx.doi.org/10.2741/1361.

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8

Schiene, Cordelia, Ulf Reimer, Mike Schutkowski, and Gunter Fischer. "Mapping the stereospecificity of peptidyl prolyl cis/trans isomerases." FEBS Letters 432, no. 3 (August 7, 1998): 202–6. http://dx.doi.org/10.1016/s0014-5793(98)00871-0.

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Yli-Kauhaluoma, Jari T., Jon A. Ashley, Chih-Hung L. Lo, Julie Coakley, Peter Wirsching, and Kim D. Janda. "Catalytic Antibodies with Peptidyl−Prolyl Cis−Trans Isomerase Activity." Journal of the American Chemical Society 118, no. 23 (January 1996): 5496–97. http://dx.doi.org/10.1021/ja954206p.

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Caporale, Andrea, Fabiola Mascanzoni, Biancamaria Farina, Mattia Sturlese, Gianluigi Di Sorbo, Roberto Fattorusso, Menotti Ruvo, and Nunzianna Doti. "FRET-Protease-Coupled Peptidyl-Prolyl cis-trans Isomerase Assay." Journal of Biomolecular Screening 21, no. 7 (July 10, 2016): 701–12. http://dx.doi.org/10.1177/1087057116650402.

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In this work, a sensitive and convenient protease-based fluorimetric high-throughput screening (HTS) assay for determining peptidyl-prolyl cis-trans isomerase activity was developed. The assay was based on a new intramolecularly quenched substrate, whose fluorescence and structural properties were examined together with kinetic constants and the effects of solvents on its isomerization process. Pilot screens performed using the Library of Pharmacologically Active Compounds (LOPAC) and cyclophilin A (CypA), as isomerase model enzyme, indicated that the assay was robust for HTS, and that comparable results were obtained with a CypA inhibitor tested both manually and automatically. Moreover, a new compound that inhibits CypA activity with an IC50 in the low micromolar range was identified. Molecular docking studies revealed that the molecule shows a notable shape complementarity with the catalytic pocket confirming the experimental observations. Due to its simplicity and precision in the determination of extent of inhibition and reaction rates required for kinetic analysis, this assay offers many advantages over other commonly used assays.

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Dissertations / Theses on the topic "Peptidyl-prolyl cis"

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Fanghänel, Jörg. "Untersuchungen zum Katalysemechanismus von Peptidyl-Prolyl-cis- trans-Isomerasen." [S.l.] : [s.n.], 2005. http://deposit.ddb.de/cgi-bin/dokserv?idn=980152100.

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Edvardsson, Anna. "Peptidyl-prolyl cis-trans Isomerases in the Chloroplast Thylakoid Lumen." Doctoral thesis, Linköping : Univ, 2007. http://www.bibl.liu.se/liupubl/disp/disp2007/med983s.pdf.

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Chaturvedi, Vandana. "Structure and function relationship among the peptidyl prolyl cis/trans isomerases." Diss., Mississippi State : Mississippi State University, 2007. http://sun.library.msstate.edu/ETD-db/theses/available/etd-11062007-111918.

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Féaux, de Lacroix Boris. "Synthese von Inhibitoren der humanen Peptidyl-Prolyl-cis-trans-Isomerase Pin1." [S.l.] : [s.n.], 2006. http://deposit.ddb.de/cgi-bin/dokserv?idn=98362643X.

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Reimer, Tatiana. "Cellular localization and function of peptidyl-prolyl cis-trans isomerase hPar14." [S.l. : s.n.], 2003. http://deposit.ddb.de/cgi-bin/dokserv?idn=969411618.

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Rulten, Stuart. "Identification and characterisation of novel human peptidyl-prolyl cis/trans isomerases." Thesis, University of Sussex, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.324152.

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Bose, Suchira. "The characterisation of an endoplasmic reticulum luminal peptidyl prolyl cis-trans isomerase." Thesis, University of Kent, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.386080.

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Stoller, Gerlind. "Charakterisierung des Triggerfaktors - einer ribosomenassoziierten Peptidyl-Prolyl-cis-trans-Isomerase aus Escherichia coli." [S.l. : s.n.], 1998. http://deposit.ddb.de/cgi-bin/dokserv?idn=960869263.

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Pirkl, Franziska. "Funktionelle Analyse der grossen Peptidyl-Prolyl-cis/trans-Isomerasen FKBP51, FKBP52 und Cyp40." [S.l.] : [s.n.], 2001. http://deposit.ddb.de/cgi-bin/dokserv?idn=96279127X.

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Kamphausen, Thilo. "Charakterisierung von AtFKBP42 und weiteren Peptidyl-Prolyl-cis/trans-Isomerasen aus Arabidopsis thaliana." [S.l. : s.n.], 2002. http://deposit.ddb.de/cgi-bin/dokserv?idn=967124409.

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Books on the topic "Peptidyl-prolyl cis"

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Sylvie, Rivière, ed. Peptidyl-prolyl cis/trans isomerases. Oxford: Oxford University Press, 1998.

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Lim, Jormay, Tae Ho Lee, and Futoshi Suizu, eds. Phosphorylation-Dependent Peptidyl-Prolyl Cis/Trans Isomerase PIN1. Frontiers Media SA, 2021. http://dx.doi.org/10.3389/978-2-88966-381-1.

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Book chapters on the topic "Peptidyl-prolyl cis"

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Donato, Dominique M., Steven K. Hanks, Kenneth A. Jacobson, M. P. Suresh Jayasekara, Zhan-Guo Gao, Francesca Deflorian, John Papaconstantinou, et al. "Peptidyl-Prolyl cis-trans Isomerase Pin1." In Encyclopedia of Signaling Molecules, 1364. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101020.

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Dugave, Christophe. "Peptidyl Prolyl Isomerases: New Targets for Novel Therapeutics?" In cis-transIsomerization in Biochemistry, 261–94. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2006. http://dx.doi.org/10.1002/9783527609338.ch12.

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Donato, Dominique M., Steven K. Hanks, Kenneth A. Jacobson, M. P. Suresh Jayasekara, Zhan-Guo Gao, Francesca Deflorian, John Papaconstantinou, et al. "Peptidyl-Prolyl cis-trans Isomerase NIMA-Interacting 1." In Encyclopedia of Signaling Molecules, 1364. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101019.

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4

Erdmann, Frank, and Gunter Fischer. "The Nickel-Regulated Peptidyl Prolyl cis/trans Isomerase SlyD." In Nickel and Its Surprising Impact in Nature, 501–18. Chichester, UK: John Wiley & Sons, Ltd, 2007. http://dx.doi.org/10.1002/9780470028131.ch13.

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5

Kuzmič, Petr, James L. Kofron, Vimal Kishore, and Daniel H. Rich. "Mathematical models for the kinetics of peptidyl-prolyl cis-trans isomerases." In Peptides, 470–71. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2264-1_180.

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6

Barth, Holger. "Role of Peptidyl-Prolyl cis/trans Isomerases in Cellular Uptake of Bacterial Protein Toxins." In Heat Shock Proteins, 251–65. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-6787-4_16.

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Kundu, Manikuntala. "Helicobacter pylori Peptidyl Prolyl cis, trans Isomerase: A Modulator of the Host Immune Response." In Heat Shock Proteins, 81–91. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-6787-4_5.

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García-Echeverría, Carlos, James L. Kofron, Petr Kuzmic, Vimal Kishore, and Daniel H. Rich. "Intramolecularly quenched fluorescent peptide substrates of peptidyl-prolyl cis-trans isomerases: The first direct fluorimetric assay for PPIases." In Peptides 1992, 479–80. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-1470-7_212.

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9

Ernst, Katharina, Leonie Schnell, and Holger Barth. "Host Cell Chaperones Hsp70/Hsp90 and Peptidyl-Prolyl Cis/Trans Isomerases Are Required for the Membrane Translocation of Bacterial ADP-Ribosylating Toxins." In Current Topics in Microbiology and Immunology, 163–98. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/82_2016_14.

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Steinert, Michael, and Can Ünal. "Macrophage Infectivity Potentiator Mip Exhibits Peptidyl-Prolyl-cis/trans-Isomerase Activity, Binds Collagen IV and Enables Legionella pneumophila to Transmigrate Across Tissue Barriers." In Heat Shock Proteins, 93–99. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-6787-4_6.

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Conference papers on the topic "Peptidyl-prolyl cis"

1

Hensel, A., S. Esch, B. Bopp, J. Jose, and S. Brandt. "Cryptotanshinone from Salvia miltiorriza roots reduces Cytokeratin 1/10 expression in keratinocytes by activation of peptidyl-prolyl-cis-trans-isomerase FKBPO1A." In 67th International Congress and Annual Meeting of the Society for Medicinal Plant and Natural Product Research (GA) in cooperation with the French Society of Pharmacognosy AFERP. © Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-3400022.

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Xu, Meng, Chit Chow, Chartia Ching Mei Cheung, Grace Tin-Yun Chung, and Kwok Wai Lo. "Abstract B238: PIN1 (Peptidyl-prolyl cis/trans-isomerase, NIMA-interacting 1) is a potential therapeutic target for EBV-associated nasopharyngeal carcinoma." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Oct 19-23, 2013; Boston, MA. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1535-7163.targ-13-b238.

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Tai, Yu-Ling, and Tang-Long Shen. "Abstract LB-026: Pin1 negatively regulated Grb7 protein stability via the ubiquitin-proteasome cascade requires the peptidyl-prolyl cis/trans isomerase activity of Pin1." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-lb-026.

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