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== Referencias ==
== Referencias ==

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== Otras lecturas ==
== Otras lecturas ==
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*{{cite journal | authors=Bank RA, Hettema EH, Arwert F |title=Electrophoretic characterization of posttranslational modifications of human parotid salivary alpha-amylase. |journal=Electrophoresis |volume=12 |issue= 1 |pages= 74–9 |year= 1991 |pmid= 1710976 |doi= 10.1002/elps.1150120114 |s2cid=27328712 |display-authors=etal}}
*{{cite journal | authors=Groot PC, Mager WH, Henriquez NV |title=Evolution of the human alpha-amylase multigene family through unequal, homologous, and inter- and intrachromosomal crossovers. |journal=Genomics |volume=8 |issue= 1 |pages= 97–105 |year= 1991 |pmid= 2081604 |doi=10.1016/0888-7543(90)90230-R |display-authors=etal}}
*{{cite journal | authors=Nishide T, Nakamura Y, Emi M |title=Primary structure of human salivary alpha-amylase gene. |journal=Gene |volume=41 |issue= 2–3 |pages= 299–304 |year= 1986 |pmid= 2423416 |doi=10.1016/0378-1119(86)90110-1 |display-authors=etal}}
*{{cite journal | authors=Davis MM, Hodes ME, Munsick RA |title=Pancreatic amylase expression in human pancreatic development |journal=Hybridoma |volume=5 |issue= 2 |pages= 137–45 |year= 1986 |pmid= 2424823 |doi=10.1089/hyb.1986.5.137 |display-authors=etal}}
*{{cite journal | authors=Handy DE, Larsen SH, Karn RC, Hodes ME |title=Identification of a human salivary amylase gene. Partial sequence of genomic DNA suggests a mode of regulation different from that of mouse, Amy1 |journal=Mol. Biol. Med. |volume=4 |issue= 3 |pages= 145–55 |year= 1987 |pmid= 2442579 }}
*{{cite journal | authors=Horii A, Emi M, Tomita N |title=Primary structure of human pancreatic alpha-amylase gene: its comparison with human salivary alpha-amylase gene |journal=Gene |volume=60 |issue= 1 |pages= 57–64 |year= 1988 |pmid= 2450054 |doi=10.1016/0378-1119(87)90213-7 |display-authors=etal|hdl=11094/36665 |hdl-access=free }}
*{{cite journal | authors=Gumucio DL, Wiebauer K, Caldwell RM |title=Concerted evolution of human amylase genes |journal=Mol. Cell. Biol. |volume=8 |issue= 3 |pages= 1197–205 |year= 1988 |pmid= 2452973 |doi= 10.1128/MCB.8.3.1197| pmc=363264 |display-authors=etal}}
*{{cite journal | authors=Samuelson LC, Wiebauer K, Gumucio DL, Meisler MH |title=Expression of the human amylase genes: recent origin of a salivary amylase promoter from an actin pseudogene |journal=Nucleic Acids Res. |volume=16 |issue= 17 |pages= 8261–76 |year= 1988 |pmid= 2458567 |doi=10.1093/nar/16.17.8261 | pmc=338557 }}
*{{cite journal | authors=Groot PC, Bleeker MJ, Pronk JC |title=The human alpha-amylase multigene family consists of haplotypes with variable numbers of genes |journal=Genomics |volume=5 |issue= 1 |pages= 29–42 |year= 1989 |pmid= 2788608 |doi=10.1016/0888-7543(89)90083-9 |display-authors=etal}}
*{{cite journal | authors=Pronk JC, Frants RR, Jansen W |title=Evidence of duplication of the human salivary amylase gene |journal=Hum. Genet. |volume=60 |issue= 1 |pages= 32–5 |year= 1982 |pmid= 6176528 |doi=10.1007/BF00281260 |s2cid=37322144 |display-authors=etal}}
*{{cite journal | authors=Zabel BU, Naylor SL, Sakaguchi AY |title=High-resolution chromosomal localization of human genes for amylase, proopiomelanocortin, somatostatin, and a DNA fragment (D3S1) by in situ hybridization |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=80 |issue= 22 |pages= 6932–6 |year= 1984 |pmid= 6196780 |doi=10.1073/pnas.80.22.6932 | pmc=390100 |display-authors=etal}}
*{{cite journal | authors=Tricoli JV, Shows TB |title=Regional assignment of human amylase (AMY) to p22----p21 of chromosome 1 |journal=Somat. Cell Mol. Genet. |volume=10 |issue= 2 |pages= 205–10 |year= 1984 |pmid= 6608795 |doi=10.1007/BF01534909 |s2cid=21230969 }}
*{{cite journal | authors=Nishide T, Emi M, Nakamura Y, Matsubara K |title=Corrected sequences of cDNAs for human salivary and pancreatic alpha-amylases [corrected] |journal=Gene |volume=28 |issue= 2 |pages= 263–70 |year= 1984 |pmid= 6610603 |doi=10.1016/0378-1119(84)90265-8 }}
*{{cite journal | authors=Seyama K, Nukiwa T, Takahashi K |title=Amylase mRNA transcripts in normal tissues and neoplasms: the implication of different expressions of amylase isogenes |journal=J. Cancer Res. Clin. Oncol. |volume=120 |issue= 4 |pages= 213–20 |year= 1994 |pmid= 7507116 |doi=10.1007/BF01372559 |s2cid=6897149 |display-authors=etal}}
*{{cite journal | authors=Ragunath C, Sundar K, Ramasubbu N |title=Expression, characterization, and biochemical properties of recombinant human salivary amylase |journal=Protein Expr. Purif. |volume=24 |issue= 2 |pages= 202–11 |year= 2002 |pmid= 11858714 |doi= 10.1006/prep.2001.1559 }}
*{{cite journal | authors=Hokari S, Miura K, Koyama I |title=A restriction endonuclease assay for expression of human alpha-amylase isozymes |journal=Clin. Chim. Acta |volume=322 |issue= 1–2 |pages= 113–6 |year= 2002 |pmid= 12104089 |doi=10.1016/S0009-8981(02)00161-4 |display-authors=etal}}
*{{cite journal | authors=Furusawa M, Taira T, Iguchi-Ariga SM, Ariga H |title=AMY-1 interacts with S-AKAP84 and AKAP95 in the cytoplasm and the nucleus, respectively, and inhibits cAMP-dependent protein kinase activity by preventing binding of its catalytic subunit to A-kinase-anchoring protein (AKAP) complex |journal=J. Biol. Chem. |volume=277 |issue= 52 |pages= 50885–92 |year= 2003 |pmid= 12414807 |doi= 10.1074/jbc.M206387200}}
*{{cite journal | authors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |bibcode=2002PNAS...9916899M |display-authors=etal}}
*{{cite journal | authors=Ramasubbu N, Ragunath C, Mishra PJ |title=Probing the role of a mobile loop in substrate binding and enzyme activity of human salivary amylase |journal=J. Mol. Biol. |volume=325 |issue= 5 |pages= 1061–76 |year= 2003 |pmid= 12527308 |doi=10.1016/S0022-2836(02)01326-8}}
*{{cite journal | authors=Kandra L, Gyémánt G, Remenyik J |title=Subsite mapping of human salivary alpha-amylase and the mutant Y151M |journal=FEBS Lett. |volume=544 |issue= 1–3 |pages= 194–8 |year= 2003 |pmid= 12782315 |doi=10.1016/S0014-5793(03)00495-2 |s2cid=83561963 |display-authors=etal}}
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[[Categoría:Genes del cromosoma 1]]
[[Categoría:Genes del cromosoma 1]]

Revisión actual - 23:00 25 abr 2024

La alfa-amilasa 1 es una enzima que en humanos está codificada por el gen AMY1A. [1]​ Este gen se encuentra en muchos organismos.

Las amilasas son proteínas secretadas que hidrolizan los enlaces 1,4-alfa-glucósido en oligosacáridos y polisacáridos y, por tanto, catalizan el primer paso en la digestión del almidón y el glucógeno de la dieta. El genoma humano tiene un grupo de varios genes de amilasa que se expresan en niveles elevados en las glándulas salivales o en el páncreas. Este gen codifica una isoenzima amilasa producida por la glándula salival. El empalme alternativo da como resultado múltiples variantes de transcripción que codifican la misma proteína. [1]

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