Literatura científica selecionada sobre o tema "Catalabolisme de la proline"
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Artigos de revistas sobre o assunto "Catalabolisme de la proline"
Sarhan, S., e N. Seiler. "Proline and proline derivatives as anticonvulsants". General Pharmacology: The Vascular System 20, n.º 1 (janeiro de 1989): 53–60. http://dx.doi.org/10.1016/0306-3623(89)90060-8.
Texto completo da fonteMyung, Sunnie, Maren Pink, Mu-Hyun Baik e David E. Clemmer. "DL-Proline". Acta Crystallographica Section C Crystal Structure Communications 61, n.º 8 (23 de julho de 2005): o506—o508. http://dx.doi.org/10.1107/s0108270105021001.
Texto completo da fonteOpalka, Suzanne M., Ashley R. Longstreet e D. Tyler McQuade. "Continuous proline catalysis via leaching of solid proline". Beilstein Journal of Organic Chemistry 7 (14 de dezembro de 2011): 1671–79. http://dx.doi.org/10.3762/bjoc.7.197.
Texto completo da fonteGruttadauria, Michelangelo, Francesco Giacalone e Renato Noto. "Supported proline and proline-derivatives as recyclable organocatalysts". Chemical Society Reviews 37, n.º 8 (2008): 1666. http://dx.doi.org/10.1039/b800704g.
Texto completo da fonteCsaba, G., e P. Kovács. "Imprinting Effects of Proline Containing Dipeptides (Proline-Glycine, Proline-Leucine, Proline-Valine and Their Retro Variants) in Tetrahymena. Evolutionary Conclusions". Bioscience Reports 17, n.º 6 (1 de dezembro de 1997): 537–42. http://dx.doi.org/10.1023/a:1027360207238.
Texto completo da fonteRutella, Giuseppina Sefora, Lisa Solieri, Serena Martini e Davide Tagliazucchi. "Release of the Antihypertensive Tripeptides Valine-Proline-Proline and Isoleucine-Proline-Proline from Bovine Milk Caseins during in Vitro Gastrointestinal Digestion". Journal of Agricultural and Food Chemistry 64, n.º 45 (7 de novembro de 2016): 8509–15. http://dx.doi.org/10.1021/acs.jafc.6b03271.
Texto completo da fonteMedha, Sadhna Sharma e Monika Sharma. "Proline-Glutamate/Proline-Proline-Glutamate (PE/PPE) proteins of Mycobacterium tuberculosis: The multifaceted immune-modulators". Acta Tropica 222 (outubro de 2021): 106035. http://dx.doi.org/10.1016/j.actatropica.2021.106035.
Texto completo da fonteMandalapu, Dhanaraju. "l-Proline and d-Proline (Chiral Amino Acid Catalysts)". Synlett 26, n.º 05 (19 de fevereiro de 2015): 707–8. http://dx.doi.org/10.1055/s-0034-1380270.
Texto completo da fonteTritsch, Denis, Hiba Mawlawi e Jean-François Biellmann. "Mechanism-based inhibition of proline dehydrogenase by proline analogues". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1202, n.º 1 (setembro de 1993): 77–81. http://dx.doi.org/10.1016/0167-4838(93)90065-y.
Texto completo da fonteHill, JeffW, e EdwinM Nemoto. "N -acetyl proline-glycine-proline: implications for neurological disorders". Neural Regeneration Research 11, n.º 6 (2016): 0. http://dx.doi.org/10.4103/1673-5374.184478.
Texto completo da fonteTeses / dissertações sobre o assunto "Catalabolisme de la proline"
Zheng, Yao. "Identification of interacting mitochondrial enzymes involved in pyrroline-5-carboxylate metabolism in Arabidopsis thaliana". Electronic Thesis or Diss., Sorbonne université, 2021. https://accesdistant.sorbonne-universite.fr/login?url=https://theses-intra.sorbonne-universite.fr/2021SORUS269.pdf.
Texto completo da fonteThe proteinogenic amino acid proline plays a crucial role for cellular metabolism in living organisms. In mitochondria, proline is oxidized to glutamate by the sequential action of proline dehydrogenase (ProDH) and pyrroline-5-carboxylate (P5C) dehydrogenase (P5CDH). In addition, ornithine δ-aminotransferase (δOAT) also participates in P5C formation through the conversion of ornithine and α-ketoglutarate into glutamate and P5C. Using mutants and biochemical approaches, ProDH1, P5CDH and δOAT were shown to be involved during dark-induced leaf senescence (DIS) in Arabidopsis thaliana. Striking accumulation of P5C and proline was observed in p5cdh mutant and to a lesser extent in prodh1prodh2 mutant, suggesting a putative proline-P5C cycle. Metabolomic analysis indicated that prodh1prodh2 and p5cdh have a similar metabolomic profile, but significantly different from wild-type and oat mutant, demonstrating the role of proline oxidation during DIS. ProDH1 was shown to be preferentially associated to the mitochondrial membrane fraction, while P5CDH and δOAT are more evenly distributed between matrix and membrane fractions. Homo- and hetero-oligomerizations of ProDH1, P5CDH, and δOAT were revealed using Bimolecular Fluorescence Complementation (BiFC) assay of infiltrated tobacco leaves. Interactions between P5C metabolism enzymes were further highlighted in DIS leaves using proteomics approaches coupled with mass spectrometry. Our work demonstrates that these three enzymes form P5C metabolic complex(es) involved in the oxidation of proline to fuel mitochondrial electron transfer chain to support the energy needs of senescent cells
Hsueh, Li-Ching. "Studies on proline hydroxylases". Thesis, University of Oxford, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.365805.
Texto completo da fonteKüllchen, Felix B. "Studies on proline 3-hydroxylase". Thesis, University of Oxford, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.269221.
Texto completo da fonteSchulz, Daniel [Verfasser]. "L-Proline and Glutamatergic Neurotransmission : Clarifying the Modulatory Role of Neuronal L-Proline Transporter / Daniel Schulz". Bonn : Universitäts- und Landesbibliothek Bonn, 2012. http://d-nb.info/1044971096/34.
Texto completo da fonteLawrence, Christopher C. "Studies on bacterial proline 4-hydroxylase". Thesis, University of Oxford, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.358610.
Texto completo da fonteHu, Chien-an Andy. "Osmoregulation and proline biosynthesis in plants /". The Ohio State University, 1993. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487843688956923.
Texto completo da fonteTownsend, David E. Wilkinson Brian J. "Proline transport and biosynthesis in Staphylococcus aureus". Normal, Ill. Illinois State University, 1992. http://wwwlib.umi.com/cr/ilstu/fullcit?p9311291.
Texto completo da fonteTitle from title page screen, viewed February 6, 2006. Dissertation Committee: Brian J. Wilkinson (chair), Radheshyam Jayaswal, Herman E. Brockman, Robert L. Preston, Philip D. Morse. Includes bibliographical references (leaves 107-112) and abstract. Also available in print.
Le, Dinh Thien. "Métabolisme de la proline chez les mammifères". Paris 5, 1988. http://www.theses.fr/1988PA05P216.
Texto completo da fonteHabibi-Najafi, Mohammad B. (Mohammad Bagher). "Proline-specific peptidases from Lactobacillus casei subspecies". Thesis, McGill University, 1994. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=28455.
Texto completo da fonteStorage stability of x-prolyl dipeptidyl peptidase and proline iminopeptidase in crude extract, with and without stabilizers showed no significant loss in activity of these two enzymes at 4$ sp circ$C for 9 days without adding any stabilizers. The levels of x-prolyl dipeptidyl peptidase, proline iminopeptidase, and post proline endopeptidase activities of cells grown in whey did not vary markedly from cells grown in MRS broth. X-prolyl dipeptidyl peptidase and proline iminopeptidase were purified from crude cell-free extract of Lactobacillus casei ssp. casei LLG by Fast Protein Liquid Chromatography (FPLC) equipped with ion-exchange and gel-filtration columns. X-prolyl dipeptidyl peptidase was found to be a serine-dependent enzyme with molecular mass of 79 kDa. The pH and the temperature optima by the purified enzyme were 7.0 and 50$ sp circ$C, respectively. Proline iminopeptidase was sulfhydryl enzyme with molecular mass of 46 kDa. The maximum enzyme activity was observed at pH 7.5 and 40$ sp circ$C. This is the first report describing the purification and characterization of x-prolyl dipeptidyl peptidase and proline iminopeptidase from Lactobacillus casei to homogeneity.
The debittering of tryptic digests from $ beta$-casein by x-prolyl dipeptidyl peptidase was studied by reversed phase high performance liquid chromatography (RP-HPLC) and liquid chromatography/mass spectrometry. The results showed that two bitter peptides (f53-97 and f03-209) containing X-Pro-Y-Pro in their amino acid residues were completely hydrolyzed and many other peptides with high hydrophobicity were decreased in peak area. The addition of purified x-prolyl dipeptidyl peptidase on bitter enzyme-modified cheese (EMC) also showed that at least one bitter peptide with X-Pro-Y derived from $ alpha$-casein hydrolysis was removed.
Walters, Nicola Jane. "Arginine and proline catabolism in Schizosaccharomyces pombe". Thesis, University of Cambridge, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.257192.
Texto completo da fonteLivros sobre o assunto "Catalabolisme de la proline"
Sorrell, Barbara Jane. Conformation of proline residues in bacteriorhodopsin. Ottawa: National Library of Canada, 1990.
Encontre o texto completo da fonteWood, Nicholas James. The role of proline in osmoregulation by a streptomycete. [s.l.]: typescript, 1996.
Encontre o texto completo da fonteClymer Toro proline hydrostatic commercial walk-behind mowers, 1990 & later. Overland Park, Kan: Primedia, 2003.
Encontre o texto completo da fonteDrzymala, Lukasz. Phosphorylation of human salivary proline-rich proteins in cultured cells. Ottawa: National Library of Canada, 1998.
Encontre o texto completo da fonteChan, Maggie Tin Lai. Proteolytic processing of recombinant human salivary proline-rich protein precursors (PRPs). Ottawa: National Library of Canada, 2000.
Encontre o texto completo da fonteChan, John Chi Cheong. Purification and characterization of recombinant human basic proline-rich protien precursor. Ottawa: National Library of Canada, 1996.
Encontre o texto completo da fonteBlankenstein, Petra. Isolierung, Charakterisierung und Lokalisierung der Prolylhydroxylase aus Chlamydomonas reinhardii und Daucus carota. Konstanz: Hartung-Gorre, 1988.
Encontre o texto completo da fonteSpielman, Andrew I. Purification and characterization of the proline-rich proteins from rabbit parotid saliva. [Toronto: University of Toronto, Faculty of Dentistry], 1988.
Encontre o texto completo da fonteLu, Ying. Characterization of the interaction of human salivary proline-rich proteins with tannins. [Toronto: University of Toronto, Faculty of Dentistry], 1997.
Encontre o texto completo da fonteShen, Lixin. The Influence of microwave heating on the rate of racemization of L-proline. Sudbury, Ont: Laurentian University, 1993.
Encontre o texto completo da fonteCapítulos de livros sobre o assunto "Catalabolisme de la proline"
Kobayashi, Kensei. "Proline". In Encyclopedia of Astrobiology, 1344. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-11274-4_1282.
Texto completo da fonteKobayashi, Kensei. "Proline". In Encyclopedia of Astrobiology, 2025. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-44185-5_1282.
Texto completo da fonteSapse, Anne-Marie. "Proline". In Molecular Orbital Calculations for Amino Acids and Peptides, 63–73. Boston, MA: Birkhäuser Boston, 2000. http://dx.doi.org/10.1007/978-1-4612-1354-3_6.
Texto completo da fonteKobayashi, Kensei. "Proline". In Encyclopedia of Astrobiology, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27833-4_1282-4.
Texto completo da fonteKobayashi, Kensei. "Proline". In Encyclopedia of Astrobiology, 2470. Berlin, Heidelberg: Springer Berlin Heidelberg, 2023. http://dx.doi.org/10.1007/978-3-662-65093-6_1282.
Texto completo da fonteZhang, Shilei, e Wei Wang. "Proline Derivatives". In Privileged Chiral Ligands and Catalysts, 409–45. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2011. http://dx.doi.org/10.1002/9783527635207.ch11.
Texto completo da fonteSchomburg, D., M. Salzmann e D. Stephan. "Proline dehydrogenase". In Enzyme Handbook 7, 203–5. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78521-4_42.
Texto completo da fonteHirota, E., K. Kuchitsu, T. Steimle, J. Vogt e N. Vogt. "28 C5H9NO2 Proline". In Molecules Containing Three or Four Carbon Atoms and Molecules Containing Five or More Carbon Atoms, 192. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-41504-3_159.
Texto completo da fonteSchomburg, Dietmar, e Dörte Stephan. "Procollagen-proline dioxygenase". In Enzyme Handbook, 271–78. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-57942-4_57.
Texto completo da fonteDemaison, J. "557 C5H9NO2 Proline". In Asymmetric Top Molecules. Part 2, 519–21. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-10400-8_305.
Texto completo da fonteTrabalhos de conferências sobre o assunto "Catalabolisme de la proline"
Hlaváček, Jan, Jan Mařík, Blanka Bennettová e Richard Tykva. "Proline-rich peptides". In VIth Conference Biologically Active Peptides. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 1999. http://dx.doi.org/10.1135/css199903061.
Texto completo da fonteXu, X., PL Jackson, S. Tanner, M. Hardison, JE Blalock e A. Gaggar. "Acetylated Proline-Glycine-Proline (Ac-PGP) and Interleukin-8 Induce MMP-9 Release from Neutrophils." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a3717.
Texto completo da fonteMoravčíková, Daniela, Dušan Berkeš e Anna Koreňová. "Synthesis of Conformationally Restricted Proline Chimeras". In The 16th International Electronic Conference on Synthetic Organic Chemistry. Basel, Switzerland: MDPI, 2012. http://dx.doi.org/10.3390/ecsoc-16-01056.
Texto completo da fonteCarrillo Fernández, Luisa, Jose Luis Vicario, Iker Riaño, Estibaliz Diaz, Efraim Reyes Martín e Uxue Uria. "Enantioselective Synthesis of Chiral Proline Derivatives". In MOL2NET 2016, International Conference on Multidisciplinary Sciences, 2nd edition. Basel, Switzerland: MDPI, 2016. http://dx.doi.org/10.3390/mol2net-02-h004.
Texto completo da fonteTen, Galina N., e Natalia E. Shcherbakova. "Proline tautomerism in the solid phase". In Laser Physics, Photonic Technologies, and Molecular Modeling, editado por Vladimir L. Derbov. SPIE, 2022. http://dx.doi.org/10.1117/12.2625832.
Texto completo da fonteCARVALHO, Gustavo Almeida de, Ricardo Cambraia PARREIRA, Onésia Cristina Oliveira LIMA, Elis Marra da Madeira FREITAS, Bruno Lemes MARQUES, Thiago Gonçalves BARBOSA, Flávio Silva de CARVALHO et al. "Proline transporter inhibitor affects Swiss mice behavior". In Anais do I Congresso Internacional de Farmacologia Molecular Aplicada. Recife, Brasil: Even3, 2019. http://dx.doi.org/10.29327/16216.1-3.
Texto completo da fonteInforzato, Tatiane, Liane Marcia Rossi, Tiago Venancio e Alcindo A. Dos Santos. "Silica-Supported Proline Derivatives for Catalytic Studies". In 14th Brazilian Meeting on Organic Synthesis. São Paulo: Editora Edgard Blücher, 2013. http://dx.doi.org/10.5151/chempro-14bmos-r0201-1.
Texto completo da fonteAbdurashytova, E. R., S. F. Abdurashytov e E. E. Turin. "Influence of biopreparations on the content of proline and chlorophyll Sorghum bicolor L. in Steppe conditions". In 2nd International Scientific Conference "Plants and Microbes: the Future of Biotechnology". PLAMIC2020 Organizing committee, 2020. http://dx.doi.org/10.28983/plamic2020.006.
Texto completo da fonteMotrich, Artem, Roman Besaga, Iryna Soltys, Mykhailo Slyotov e Olexander V. Galochkin. "Determination of proline concentration in natural biological environments". In Fourteenth International Conference on Correlation Optics, editado por Oleg V. Angelsky. SPIE, 2020. http://dx.doi.org/10.1117/12.2553902.
Texto completo da fonteHancock, Chad N., e James Phang. "Abstract 1119: The oxidation of proline by proline oxidase provides a regulated source of ROS for mitochondria derived cellular signaling". In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-1119.
Texto completo da fonteRelatórios de organizações sobre o assunto "Catalabolisme de la proline"
Sergiev, Iskren, Dessislava Todorova e Lyubomira Atanasova. High Salinityinduced Proline and Polyamine Changes in Organs of Pea (Pisum sativumL. Cv. Ran). "Prof. Marin Drinov" Publishing House of Bulgarian Academy of Sciences, novembro de 2018. http://dx.doi.org/10.7546/crabs.2018.11.06.
Texto completo da fonteTaub, Floyd E., e Richard E. Weller. Proline-Rich Polypeptide 1 and GX-NH2: Molecular and Genetic Mechanisms of Hematopoiesis Regulation. Office of Scientific and Technical Information (OSTI), setembro de 2011. http://dx.doi.org/10.2172/1025686.
Texto completo da fonteZilberstein, Aviah, Bo Liu e Einat Sadot. Studying the Involvement of the Linker Protein CWLP and its Homologue in Cytoskeleton-plasma Membrane-cell Wall Continuum and in Drought Tolerance. United States Department of Agriculture, junho de 2012. http://dx.doi.org/10.32747/2012.7593387.bard.
Texto completo da fonteBray, Elizabeth, Zvi Lerner e Alexander Poljakoff-Mayber. The Role of Phytohormones in the Response of Plants to Salinity Stress. United States Department of Agriculture, setembro de 1994. http://dx.doi.org/10.32747/1994.7613007.bard.
Texto completo da fonteLers, Amnon, Majid R. Foolad e Haya Friedman. genetic basis for postharvest chilling tolerance in tomato fruit. United States Department of Agriculture, janeiro de 2014. http://dx.doi.org/10.32747/2014.7600014.bard.
Texto completo da fonte