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Relevant bibliographies by topics / Proline isomerisation

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Academic literature on the topic 'Proline isomerisation'

Author: Grafiati

Published: 4 June 2021

Last updated: 12 February 2022

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Journal articles on the topic "Proline isomerisation"

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Kaur, Gurpreet, and Vikas Vikas. "Exploring the mechanism of isomerisation and water-migration in the water-complexes of amino-acid l-proline: electrostatic potential and vibrational analysis." RSC Advances 5, no. 100 (2015): 82587–604. http://dx.doi.org/10.1039/c5ra06088e.

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2

Calabrese, Massimo, and Bruno Stancher. "A study of the proline isomerisation in typical Italian wines." Journal of the Science of Food and Agriculture 79, no. 11 (1999): 1357–60. http://dx.doi.org/10.1002/(sici)1097-0010(199908)79:11<1357::aid-jsfa371>3.0.co;2-3.

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Brichkina, A., N. TM Nguyen, R. Baskar, et al. "Proline isomerisation as a novel regulatory mechanism for p38MAPK activation and functions." Cell Death & Differentiation 23, no. 10 (2016): 1592–601. http://dx.doi.org/10.1038/cdd.2016.45.

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Tan, Yee-Joo, Mikael Oliveberg, Daniel E. Otzen, and Alan R. Fersht. "The rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2." Journal of Molecular Biology 269, no. 4 (1997): 611–22. http://dx.doi.org/10.1006/jmbi.1997.1043.

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Annett, Stephanie, and Tracy Robson. "Peptidyl-prolyl cis/trans isomerases in GtoPdb v.2021.2." IUPHAR/BPS Guide to Pharmacology CITE 2021, no. 2 (2021). http://dx.doi.org/10.2218/gtopdb/f845/2021.2.

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Peptidyl-prolyl cis/trans isomerases (PPIases) are an enzyme family which catalyse the cis/trans isomerisation of proline peptide bonds to promote the folding and re-folding of peptides and proteins. Three subfamilies have been identified: cyclophilins, FK506-binding proteins and parvulins. Individual PPIases are overexpressed in a number of cancers [59], and family members have been targetted for immunosuppressant effects.

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Lee, Tae Ho, Lucia Pastorino, and Kun Ping Lu. "Peptidyl-prolyl cis–trans isomerase Pin1 in ageing, cancer and Alzheimer disease." Expert Reviews in Molecular Medicine 13 (June 2011). http://dx.doi.org/10.1017/s1462399411001906.

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Phosphorylation of proteins on serine or threonine residues preceding proline is a key signalling mechanism in diverse physiological and pathological processes. Pin1 (peptidyl-prolyl cis–trans isomerase) is the only enzyme known that can isomerise specific Ser/Thr-Pro peptide bonds after phosphorylation and regulate their conformational changes with high efficiency. These Pin1-catalysed conformational changes can have profound effects on phosphorylation signalling by regulating a spectrum of target activities. Interestingly, Pin1 deregulation is implicated in a number of diseases, notably agei

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Dissertations / Theses on the topic "Proline isomerisation"

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Reader, John S. "Folding studies of the #beta#-sheet protein pseudoazurin." Thesis, University of Oxford, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.284456.

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Haugskott, Frida. "Investigating Minor States of the Oncoprotein N-MYC, with Focus on Proline Cis/Trans Isomerisation using NMR Spectroscopy." Thesis, Linköpings universitet, Institutionen för fysik, kemi och biologi, 2021. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-177936.

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MYC is a family of three regulator genes that codes for transcription factors. Expression of Myc proteins from MYC genes is found to be deregulated in 70 % of all cancer forms. The three human homologs C-Myc, N-Myc and L-Myc are mainly associated with cancer in the lymphatic system, nerve tissues and lung cancer, respectively. Even though N-Myc is associated with Neuroblastoma, the cancer variant that is most common among children, the field is focused towards C-Myc. The activation of C-Myc begins with phosphorylation of Serine 62, followed by trans-to-cis isomerisation of Proline 63. Then Thr

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Howe, Françoise Sara. "Crosstalk between histone modifications in Saccharomyces cerevisiae." Thesis, University of Oxford, 2012. http://ora.ox.ac.uk/objects/uuid:1e2e128e-1ec3-4d41-8ab5-b27e5930a654.

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The N-terminal tails of histone proteins protrude from the nucleosome core and are extensively post-translationally modified. These modifications are proposed to affect many DNA-based processes such as transcription, DNA replication and repair. Post-translational modifications on histone tails do not act independently but are subject to crosstalk. One example of crosstalk is on histone H3 between lysine 14 (H3K14) and trimethylated lysine 4 (H3K4me3), a modification found at the 5’ end of most active or poised genes. In this work, Western blots and chromatin immunoprecipitation (ChIP) experime

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