Relevant bibliographies by topics / Proline isomerisation

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  1. Journal articles
  2. Dissertations / Theses

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"

1

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 (August 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, S. Wee, J. Gunaratne, R. C. Robinson, and D. V. Bulavin. "Proline isomerisation as a novel regulatory mechanism for p38MAPK activation and functions." Cell Death & Differentiation 23, no. 10 (May 27, 2016): 1592–601. http://dx.doi.org/10.1038/cdd.2016.45.

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4

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 (June 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 (June 25, 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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6

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 ageing and age-related diseases, including cancer and Alzheimer disease. Pin1 is overexpressed in most human cancers; it activates numerous oncogenes or growth enhancers and also inactivates a large number of tumour suppressors or growth inhibitors. By contrast, ablation of Pin1 prevents cancer, but eventually leads to premature ageing and neurodegeneration. Consistent with its neuroprotective role, Pin1 has been shown to be inactivated in neurons of patients with Alzheimer disease. Therefore, Pin1-mediated phosphorylation-dependent prolyl isomerisation represents a unique signalling mechanism that has a pivotal role in the development of human diseases, and might offer an attractive new diagnostic and therapeutic target.
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Dissertations / Theses on the topic "Proline isomerisation"

1

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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2

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 Threonine 58 becomes phosphorylated leading to that Serine 62 is dephosphorylated and subsequent cis-to-trans isomerisation of Proline 63, and C-Myc is marked for degradation. Cis-trans isomerisation is necessary for regulation of gene expression, and is therefore important to understand. Since N-Myc and C-Myc have identical sequences between residues 47 to residue 69, the hypothesis is that N-Myc is activated in the same manner, but this has not been confirmed. In this project the first 69 amino acids of N-Myc were analysed with NMR spectroscopy. This resulted in a near complete assignment of the major conformation, and of the alternative minor conformations as well. The traditional assignment experiments HNCACB, HN(CO)CACB, HNCO, HN(CA)CO in combination with CCH-TOCSY and HN(CCO)C revealed that the majority of the minor configurations can be explained by cis/trans isomerisation of prolines. In addition, the protein was analysed with direct carbon detected NMR spectroscopy to be able to detect the prolines.
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3

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) experiments show that different amino acid substitutions at histone H3 position 14 cause varying degrees of H3K4me3 loss, indicating that H3K14 is not essential for H3K4me3 but acts as a modulator of H3K4me3 levels. A neighbouring residue, H3P16 is also important for H3K4me3 and may operate in concert with H3K14 to control H3K4me3. These crosstalk pathways have gene-specific effects and the levels of H3K4me3 are influenced to different extents on genes that fall into functionally distinct classes. A model is proposed to explain how H3K14/H3P16 may exert these varying effects on H3K4me3 at individual genes. In addition to its ability to regulate H3K4me3, H3K14 also influences the levels of two modifications on H3K18, acetylation and monomethylation. A ChIP-sequencing experiment has shown that H3K18me1, a previously uncharacterised modification in S. cerevisiae, is widely distributed throughout the genome and correlates strongly with histone H3 levels. The potential for a functional acetyl/methyl switch at H3K18 is explored. Together, these data indicate that, with gene-specific effects, crosstalk between histone modifications may be even more complex than originally thought.
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