Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Soha D. Idriss"'
Autor:
Vladimir G. Kharitonov, Tanima Gudi, Soha D. Idriss, Gerry R. Boss, Renate B. Pilz, Dareen E. Casteel
Publikováno v:
Journal of Biological Chemistry. 274:9489-9493
Nitric oxide (NO) regulates the expression of multiple genes but in most cases its precise mechanism of action is unclear. We used baby hamster kidney (BHK) cells, which have very low soluble guanylate cyclase and cGMP-dependent protein kinase (G-kin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93e3d123d92afbaa5ee80d7112e6d0f4
https://doi.org/10.1074/jbc.274.14.9489
https://doi.org/10.1074/jbc.274.14.9489
Publikováno v:
The FASEB Journal. 9:552-558
Nitric oxide (NO) increases cytosolic guanylate cyclase activity and thereby activates the cGMP signal transduction pathway. The cAMP and Ca2+/phospholipid signal transduction pathways activate transcription factors that bind to the cAMP response ele
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52b3bc6fde1db317bc42884aa1784ddb
https://doi.org/10.1096/fasebj.9.7.7737465
https://doi.org/10.1096/fasebj.9.7.7737465
Autor:
Marjaneh Berjis, Gerry R. Boss, Soha D. Idriss, Immo E. Scheffler, Modem Suhasini, Renate B. Pilz, Jürgen Scheele, Lin Gao
Publikováno v:
Journal of Biological Chemistry. 269:32155-32161
Sodium nitroprusside and sodium nitrite, which generate nitric oxide and increase the intracellular cGMP concentration, and 8-bromo-cGMP, a membrane-permeable cGMP analog, induce myelomonocytic differentiation of HL-60 cells (Boss, G. R. (1989) Proc.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::847a9c72e40332cb5f0a3d9caed67474
https://doi.org/10.1016/s0021-9258(18)31614-4
https://doi.org/10.1016/s0021-9258(18)31614-4
Publikováno v:
Biochemical and Biophysical Research Communications. 183:312-320
We have purified the soluble form of guanylate cyclase from human placenta greater than 2400-fold. The enzyme shared several characteristics with the enzyme purified from other sources including molecular mass and subunit composition, activation by d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67689d81ce6482127716c11f846ba60a
https://doi.org/10.1016/0006-291x(92)91645-7
https://doi.org/10.1016/0006-291x(92)91645-7
Publikováno v:
Analytical Biochemistry. 130:283-286
Glutamine phosphoribosylpyrophosphate amidotransferase (EC 2.4.2.14) catalyzes the transfer of the amide group of glutamine to 5-phospho-alpha-D-ribose-1-pyrophosphate. It is the first enzyme committed to the synthesis of purines by the de novo pathw
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ddae0f60c293943a28762ff9d4dbd60a
https://doi.org/10.1016/0003-2697(83)90589-4
https://doi.org/10.1016/0003-2697(83)90589-4
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9781475703924
Phosphoribosylpyrophosphate (PP-ribose-P) is a specific substrate for eight synthetic enzymes in mammalian cells (1). Three of these enzymes, glutamine phosphoribosylpyrophosphate amidotrans-ferase (PP-ribose-P amidotransferase, (EC.2.4.2.14), hypoxa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::42d1b4f43cc650001ca6f29700d4c8bc
https://doi.org/10.1007/978-1-4757-0390-0_3
https://doi.org/10.1007/978-1-4757-0390-0_3
