Zobrazeno 1 - 10
of 33
pro vyhledávání: '"Isomerases/metabolism"'
Autor:
Inês Loureiro, Nuno Santarém, Joana Tavares, Joana Faria, Sandra Macedo-Ribeiro, Pedro Cecílio, Anabela Cordeiro-da-Silva
Publikováno v:
Scientific Reports
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Ribose-5-phosphate isomerase (RPI) belongs to the non-oxidative branch of the pentose phosphate pathway, catalysing the inter-conversion of D-ribose-5-phosphate and D-ribulose-5-phosphate. Trypanosomatids encode a type B RPI, whereas humans have a st
Ribose 5-Phosphate Isomerase B Knockdown Compromises Trypanosoma brucei Bloodstream Form Infectivity
Autor:
Sandra Macedo-Ribeiro, Christine Clayton, Nilanjan Roy, Anabela Cordeiro-da-Siva, Nuno Santarém, Joana Faria, Inês Loureiro, Joana Tavares
Publikováno v:
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
PLoS Neglected Tropical Diseases
PLoS Neglected Tropical Diseases, Vol 9, Iss 1, p e3430 (2015)
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
PLoS Neglected Tropical Diseases
PLoS Neglected Tropical Diseases, Vol 9, Iss 1, p e3430 (2015)
Ribose 5-phosphate isomerase is an enzyme involved in the non-oxidative branch of the pentose phosphate pathway, and catalyzes the inter-conversion of D-ribose 5-phosphate and D-ribulose 5-phosphate. Trypanosomatids, including the agent of African sl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3af85b00ee781bfac34009576d245503
https://repositorio-aberto.up.pt/handle/10216/118188
https://repositorio-aberto.up.pt/handle/10216/118188
Publikováno v:
The Journal of neuroscience, vol. 15, no. 1 Pt 1, pp. 470-476
Homogenates of chick dorsal root ganglia (DRG) and in vitro cultures of DRG neurons are known to synthesize prostaglandin (PG) D2. To specify the PGD synthase isozymes controlling PGD2 synthesis in DRG and to identify the DRG cells responsible for th
Autor:
Nathalie Chamond, Wim Degrave, Paola Minoprio, Alejandro Buschiazzo, Christophe Grégoire, Pedro M. Alzari, Armand Berneman, Nicolas Coatnoan, Maira Goytia, William Shepard, Alain Cosson, Francis Schaeffer
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2006, 103 (6), pp.1705-1710. ⟨10.1073/pnas.0509010103⟩
Proceedings of the National Academy of Sciences of the United States of America, 2006, 103 (6), pp.1705-1710. ⟨10.1073/pnas.0509010103⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2006, 103 (6), pp.1705-1710. ⟨10.1073/pnas.0509010103⟩
Proceedings of the National Academy of Sciences of the United States of America, 2006, 103 (6), pp.1705-1710. ⟨10.1073/pnas.0509010103⟩
Amino acid racemases catalyze the stereoinversion of the chiral C α to produce the d -enantiomers that participate in biological processes, such as cell wall construction in prokaryotes. Within this large protein family, bacterial proline racemases
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79a56dabd710838c99f8ce668bd10bbe
https://hal.archives-ouvertes.fr/hal-02523212
https://hal.archives-ouvertes.fr/hal-02523212
Autor:
Wim Degrave, Catherine Rougeot, José Franco da Silveira, Christophe Grégoire, Nathalie Chamond, Paola Minoprio, Lucio H. Freitas-Junior, Nicolas Coatnoan
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2003, 278 (18), pp.15484-15494. ⟨10.1074/jbc.m210830200⟩
Journal of Biological Chemistry, 2003, 278 (18), pp.15484-15494. ⟨10.1074/jbc.m210830200⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2003, 278 (18), pp.15484-15494. ⟨10.1074/jbc.m210830200⟩
Journal of Biological Chemistry, 2003, 278 (18), pp.15484-15494. ⟨10.1074/jbc.m210830200⟩
International audience; Proline racemase catalyzes the interconversion of L- and D-proline enantiomers and has to date been described in only two species. Originally found in the bacterium Clostridium sticklandii, it contains cysteine residues in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69c2d65048de9a3d2c45682b039b7b99
https://hal.archives-ouvertes.fr/hal-02523188
https://hal.archives-ouvertes.fr/hal-02523188
Publikováno v:
Tsukamoto, K, Jackson, I, Urabe, K, Montague, P M & Hearing, V J 1992, ' A second tyrosinase-related protein, TRP-2, is a melanogenic enzyme termed DOPAchrome tautomerase ', EMBO Journal, vol. 11, no. 2, pp. 519-26 .
Europe PubMed Central
Europe PubMed Central
The production of melanin pigment in mammals requires tyrosinase, an enzyme which hydroxylates the amino acid tyrosine to DOPA (3,4-dihydroxyphenylalanine), thus allowing the cascade of reactions necessary to synthesize that biopolymer. However, ther
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d412fa41434158e4441ff3ee4762555c
https://www.pure.ed.ac.uk/ws/files/11557813/A_second_tyrosinase_related_protein_TRP_2_is_a_melanogenic_enzyme_termed_DOPAchrome_tautomerase.pdf
https://www.pure.ed.ac.uk/ws/files/11557813/A_second_tyrosinase_related_protein_TRP_2_is_a_melanogenic_enzyme_termed_DOPAchrome_tautomerase.pdf
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Autor:
RAO MR, ALTEKAR WW
Publikováno v:
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1961 Feb 24; Vol. 4, pp. 101-5.