Serveur d'exploration sur la rapamycine et les champignons - Exploration (Accueil)

Index « KwdFr.i » - entrée « Protéines de liaison au tacrolimus (MeSH) »
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Protéines de liaison au poly(A) (métabolisme) < Protéines de liaison au tacrolimus (MeSH) < Protéines de liaison au tacrolimus (antagonistes et inhibiteurs)  Facettes :

List of bibliographic references indexed by Protéines de liaison au tacrolimus (MeSH)

Number of relevant bibliographic references: 47.
[0-20] [0 - 20][0 - 47][20-40]
Ident.Authors (with country if any)Title
001A49 (1999) N S Cutler [États-Unis] ; J. Heitman ; M E CardenasTOR kinase homologs function in a signal transduction pathway that is conserved from yeast to mammals.
001A54 (1999) M C Cruz [États-Unis] ; L M Cavallo ; J M Görlach ; G. Cox ; J R Perfect ; M E Cardenas ; J. HeitmanRapamycin antifungal action is mediated via conserved complexes with FKBP12 and TOR kinase homologs in Cryptococcus neoformans.
001A55 (1999) C M Alarcon [États-Unis] ; J. Heitman ; M E CardenasProtein kinase activity and identification of a toxic effector domain of the target of rapamycin TOR proteins in yeast.
001A57 (1999) K J Dolinski [États-Unis] ; J. HeitmanHmo1p, a high mobility group 1/2 homolog, genetically and physically interacts with the yeast FKBP12 prolyl isomerase.
001A62 (1998) G. Wiederrecht [États-Unis] ; J J SiekierkaYeast immunophilins: purification and assay of yeast FKBP12.
001A63 (1998) T. Noda [Japon] ; Y. OhsumiTor, a phosphatidylinositol kinase homologue, controls autophagy in yeast.
001A66 (1998) P G Bertram [États-Unis] ; C. Zeng ; J. Thorson ; A S Shaw ; X F ZhengThe 14-3-3 proteins positively regulate rapamycin-sensitive signaling.
001A67 (1998) L D Walensky [États-Unis] ; P. Gascard ; M E Fields ; S. Blackshaw ; J G Conboy ; N. Mohandas ; S H SnyderThe 13-kD FK506 binding protein, FKBP13, interacts with a novel homologue of the erythrocyte membrane cytoskeletal protein 4.1.
001A73 (1998) R T Abraham [États-Unis]Mammalian target of rapamycin: immunosuppressive drugs uncover a novel pathway of cytokine receptor signaling.
001A81 (1997) R. Banholzer [Suisse] ; A P Nair ; H H Hirsch ; X F Ming ; C. MoroniRapamycin destabilizes interleukin-3 mRNA in autocrine tumor cells by a mechanism requiring an intact 3' untranslated region.
001A87 (1997) C M Alarc N [États-Unis] ; J. HeitmanFKBP12 physically and functionally interacts with aspartokinase in Saccharomyces cerevisiae.
001A94 (1996) A. Bell [Irlande (pays)] ; H C Roberts ; L H ChappellThe antiparasite effects of cyclosporin A: possible drug targets and clinical applications.
001A97 (1996) S. Luan [États-Unis] ; J. Kudla ; W. Gruissem ; S L SchreiberMolecular characterization of a FKBP-type immunophilin from higher plants.
001B01 (1996) C S Hemenway [États-Unis] ; J. HeitmanImmunosuppressant target protein FKBP12 is required for P-glycoprotein function in yeast.
001B04 (1996) S N Ho [États-Unis] ; S R Biggar ; D M Spencer ; S L Schreiber ; G R CrabtreeDimeric ligands define a role for transcriptional activation domains in reinitiation.
001B05 (1996) H. Kitagawa [Japon] ; Y. Hotta ; K. Fujiki ; A. KanaiCloning and high expression of rabbit FKBP25 in cornea.
001B08 (1995) L K Wilson [États-Unis] ; B M Benton ; S. Zhou ; J. Thorner ; G S MartinThe yeast immunophilin Fpr3 is a physiological substrate of the tyrosine-specific phosphoprotein phosphatase Ptp1.
001B09 (1995) M A Santos [Royaume-Uni] ; M F TuiteThe CUG codon is decoded in vivo as serine and not leucine in Candida albicans.
001B10 (1995) M C Lorenz [États-Unis] ; J. HeitmanTOR mutations confer rapamycin resistance by preventing interaction with FKBP12-rapamycin.
001B11 (1995) X F Zheng [États-Unis] ; D. Florentino ; J. Chen ; G R Crabtree ; S L SchreiberTOR kinase domains are required for two distinct functions, only one of which is inhibited by rapamycin.
001B12 (1995) J I Luengo [États-Unis] ; D S Yamashita ; D. Dunnington ; A K Beck ; L W Rozamus ; H K Yen ; M J Bossard ; M A Levy ; A. Hand ; T. Newman-TarrStructure-activity studies of rapamycin analogs: evidence that the C-7 methoxy group is part of the effector domain and positioned at the FKBP12-FRAP interface.

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