Bcr-Abl Protein Tyrosine Kinase

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Версія від 06:38, 11 липня 2017, створена Saucemagic56 (обговореннявнесок) (Створена сторінка: 23. Abu-Elheiga L, Matzuk MM, Kordari P, Oh W, Shaikenov T, et al. Mutant mice lacking acetyl-CoA carboxylase 1 are embryonically lethal. Proc Natl Acad Sci 102...)

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23. Abu-Elheiga L, Matzuk MM, Kordari P, Oh W, Shaikenov T, et al. Mutant mice lacking acetyl-CoA carboxylase 1 are embryonically lethal. Proc Natl Acad Sci 102: 1201112016. 24. Park SH, Gammon SR, Knippers JD, Paulsen SR, Rubink DS, et al. Phosphorylation-activity relationships of AMPK and acetyl-CoA carboxylase in muscle. J Appl Physiol 92: 24752482. 25. Magnard C, Bachelier R, Vincent A, Jaquinod M, Kieffer S, et al. BRCA1 interacts with acetyl-CoA carboxylase by way of its tandem of BRCT domains. Oncogene 21: 67296739. 26. Shen Y, Tong L Structural evidence for direct interactions in between the BRCT domains of human BRCA1 in addition to a phospho-peptide from human ACC1. Biochemistry 47: 57675773. 27. Moreau K, Dizin E, Ray H, Luquain C, Lefai E, et al. BRCA1 impacts lipid synthesis by means of its interaction with acetyl-CoA carboxylase. J Biol Chem 281: 31723181. 28. Bandyopadhyay S, Zhan R, Wang Y, Pai SK, Hirota S, et al. Mechanism of apoptosis induced by the inhibition of fatty acid synthase in breast cancer cells. Cancer Res 66: 59345940. 29. Chajes V, Cambot M, Moreau K, Lenoir GM, Joulin V Acetyl-CoA carboxylase alpha is crucial to breast cancer cell survival. Cancer Res 66: 52875294. 30. Brusselmans K, De Schrijver E, Verhoeven G, Swinnen JV RNA interference-mediated silencing of the acetyl-CoA-carboxylase-alpha gene induces growth inhibition and apoptosis of prostate cancer cells. Cancer Res 65: 67196725. 31. Swinnen JV, Brusselmans K, Verhoeven G Enhanced lipogenesis in cancer cells: new players, novel targets. Curr Opin Clin Nutr Metab Care 9: 358365. 32. Kim KH Regulation of mammalian acetyl-coenzyme A carboxylase. Annu Rev Nutr 17: 7799. 33. Frederick MJ, VanMeter AJ, Gadhikar MA, Henderson YC, Yao H, et al. Phosphoproteomic evaluation of 1262238-11-8 web signaling pathways in head and neck squamous cell carcinoma patient samples. Am J Pathol 178: 548571. 34. Chu PY, Hsu NC, Lin SH, Hou MF, Yeh KT Higher nuclear protein kinase CbII expression is often a marker of illness recurrence in oral squamous cell carcinoma. Anticancer Res 32: 39873991. 35. Gapany M, Faust RA, Tawfic S, Davis A, Adams GL, et al. Association of elevated protein kinase CK2 activity with aggressive behavior of squamous cell carcinoma with the head and neck. Mol Med 1: 659666. 36. Mehra R, Cohen RB, Burtness BA The role of cetuximab for the therapy of squamous cell carcinoma on the head and neck. Clin Adv Hematol Oncol 6: 742750. 8 ~~ ~~ The cytosolic domains of CD79a and CD79b are fairly quick intrinsically disordered proteins. Regions in IDPs generally demonstrate transient secondary structure formation and unique segments of a sequence can show a varying degree of secondary structure propensity. These regions, demonstrating local structure formation, are usually involved in protein interactions. It's identified that IDPs 11138725 often show promiscuity and can have a number of interaction partners. Adaption of IDPs to these generally structurally dissimilar partners is usually accomplished by means of a course of action of coupled folding and binding. NMR spectroscopy has confirmed to be just about the most informative scientific tools to study IDPs and new NMR primarily based techniques are continually getting developed for this goal. Chemical shift analysis might be used to probe IDPs for transient secondary structure and hence help in identifying web-sites potentially important for interactions.