Studies on the Syntheses of Benzoquinone Ansamycin Antibiotics. Syntheses of the C(5)−C(15) Subunits of Macbecin I, Geldanamycin, and Herbimycin A

2006 ◽  
Vol 8 (11) ◽  
pp. 2409-2412 ◽  
Author(s):  
Justin K. Belardi ◽  
Glenn C. Micalizio
ChemInform ◽  
2010 ◽  
Vol 27 (25) ◽  
pp. no-no
Author(s):  
S. F. MARTIN ◽  
J. A. DODGE ◽  
L. E. BURGESS ◽  
C. LIMBERAKIS ◽  
M. HARTMANN

Tetrahedron ◽  
1996 ◽  
Vol 52 (9) ◽  
pp. 3229-3246 ◽  
Author(s):  
Stephen F. Martin ◽  
Jeffrey A. Dodge ◽  
Laurence E. Burgess ◽  
Chris Limberakis ◽  
Michael Hartmann

2003 ◽  
Vol 474 (1) ◽  
pp. 121-128 ◽  
Author(s):  
Shankar B. Sachidhanandam ◽  
Jia Lu ◽  
Kerwin S.Y. Low ◽  
Shabbir M. Moochhala
Keyword(s):  

2014 ◽  
Vol 85 (6) ◽  
pp. 849-857 ◽  
Author(s):  
Chuan-Hsin Chang ◽  
Derek A. Drechsel ◽  
Russell R. A. Kitson ◽  
David Siegel ◽  
Qiang You ◽  
...  

1986 ◽  
Vol 39 (3) ◽  
pp. 415-423 ◽  
Author(s):  
KIYOSHI SHIBATA ◽  
SADAYOSHI SATSUMABAYASHI ◽  
HIROSHI SANO ◽  
KANKI KOMIYAMA ◽  
AKIRA NAKAGAWA ◽  
...  

1999 ◽  
Vol 19 (12) ◽  
pp. 8422-8432 ◽  
Author(s):  
Olivier Donzé ◽  
Didier Picard

ABSTRACT The protein kinase Gcn2 stimulates translation of the yeast transcription factor Gcn4 upon amino acid starvation. Using genetic and biochemical approaches, we show that Gcn2 is regulated by the molecular chaperone Hsp90 in budding yeast Saccharomyces cerevisiae. Specifically, we found that (i) several Hsp90 mutant strains exhibit constitutive expression of a GCN4-lacZ reporter plasmid; (ii) Gcn2 and Hsp90 form a complex in vitro as well as in vivo; (iii) the specific inhibitors of Hsp90, geldanamycin and macbecin I, enhance the association of Gcn2 with Hsp90 and inhibit its kinase activity in vitro; (iv) in vivo, macbecin I strongly reduces the levels of Gcn2; (v) in a strain expressing the temperature-sensitive Hsp90 mutant G170D, both the accumulation and activity of Gcn2 are abolished at the restrictive temperature; and (vi) the Hsp90 cochaperones Cdc37, Sti1, and Sba1 are required for the response to amino acid starvation. Taken together, these data identify Gcn2 as a novel target for Hsp90, which plays a crucial role for the maturation and regulation of Gcn2.


1995 ◽  
Vol 270 (28) ◽  
pp. 16580-16587 ◽  
Author(s):  
Laura Sepp-Lorenzino ◽  
Zhengping Ma ◽  
David E. Lebwohl ◽  
Alexander Vinitsky ◽  
Neal Rosen

1992 ◽  
Vol 31 (4) ◽  
pp. 333-339 ◽  
Author(s):  
Robert L. Dow ◽  
Bruce M. Bechle ◽  
Phillip M. Chalabi ◽  
James H. Windels ◽  
Robert W. Roth
Keyword(s):  

2001 ◽  
Vol 280 (1) ◽  
pp. G43-G50 ◽  
Author(s):  
Kristina M. Reber ◽  
Gennifer M. Mager ◽  
Charles E. Miller ◽  
Philip T. Nowicki

We studied mesenteric arterial arcades from 3- and 35-day-old swine to determine the relationship between perfusate flow rate and release of nitric oxide (NO) into mesenteric effluent. Mesenteric arterial arcades were perfused under controlled-flow conditions with a peristaltic pump using warm oxygenated Krebs buffer. Basal rates of NO production were 43.6 ± 4.2 vs. 12.1 ± 2.5 nmol/min in 3- vs. 35-day-old mesentery during perfusion at in vivo flow rates (9 vs. 20 ml/min, respectively). Rate of NO production was directly related to flow rate over a wide range of flows (5–40 ml/min) in 3- but not 35-day-old mesentery. Both age groups demonstrated a brisk, albeit brief, increase in NO production in response to infusion of NO-dependent vasodilator substance P (10−8 M/min). Tyrosine kinase inhibitor herbimycin A andl-arginine analog l-NMMA significantly attenuated flow-induced increase in NO production, and phosphatase inhibitor phenylarsine oxide increased magnitude of flow-induced increase in NO production in 3-day-olds. Removal of extracellular Ca2+ and depletion of intracellular Ca2+ stores (Ca2+-free Krebs with EGTA plus thapsigargin) had no effect on NO production in either group. Thus, basal rate of NO production is greater in mesenteric arterial arcades from 3- than from 35-day old swine, a direct relationship between flow rate and NO production rate is present in mesentery from 3- but not 35-day-olds, and phosphorylation events are necessary for this interaction to occur.


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