Gonzalez, F.J. (1994) A novel cis-acting element controlling therat CYP2D5 gene and requiring cooperativity between C/EBPbandanSp1factor.MolCellBiol.14, 1383–1394.22. Lee, Y.H., Williams, S.C., Baer, M., Sterneck, E., Gonzalez,F.J. & Johnson, P.F. (1997) The ability of C/EBP beta but notC/EB[r]
E-mail: bkcc@hkusua.hku.hk(Received 18 April 2008, revised 4 August2008, accepted 29 August 2008)doi:10.1111/j.1742-4658.2008.06676.xAs the key regulator of reproduction, gonadotropin-releasing hormone(GnRH) is released by neurons in the hypothalamus, and transported viathe hypothalamo-hypophyseal p[r]
Chẳng hạn, những trình tự nhất định có thể được khuyếch đại hoặc cấu trúc lại trong genome hoặc các base có thể bị biến đổi về mặt hóa học. Một vài biến đổi được phục hồi, những biến đổi khác lại bền vững. Tuy nhiên những thay đổi bền vững này thường xảy ra ở tế bào sinh dưỡng, vì vậy chúng không đư[r]
qand G12 ⁄ 13signaling, ultimatelyleading to cellular proliferation, whilst strongly inhibiting pathwaysinvolved in cellular differentiation through the activation of Gisignaling.The resulting cellular outcomes account for the global physiological effectsobserved during infection with toxinogenic P.[r]
NF-κB at physiological levels is needed for learning, but inhibition of pathologicalNF-κB hyperactivation in elder age might enhance learning. Overall, a consensus ofbehavioral studies in both crabs and mice suggests that, in most settings, NF-κBplays a positive role in learning and memory and that[r]
transcription factor. One example of this is seen in theobservation that the apolipoprotein AI gene expressionin liver depends on the interactions between HNF-4and HNF-3 within a hepatocyte-specific enhancer inthe 5¢ flanking region of the gene. It has been proposedthat an intermediary factor n[r]
may be responsible for cell-type-specific restrictions(upregulation) in pseudoexon splicing. This hasconsiderable importance when considering potentialmethods for the control of aberrant splicing (seebelow). Indeed, PTB ⁄ nPTB expression levels in differ-ent tissues may be the cause of the patient’s[r]
CCHC zinc fingers are domains that bind single-stran-ded RNA [9,10]. The PABP and the WW domains [11]are protein–protein interaction domains involved intranslation [12,13] and pre-spliceosome formation,respectively [14]. By association with different types ofprotein domains, the RRM dom[r]
ments, performed in duplicate (with the exception of R60A/R101Athat was performed twice in duplicate). (B) d, Wild-type; h, H108A;m, F114A/I116A; s, L105A. (C) d, Wild type; j, R60A/R101A; n,D66A; s, plasma purified C4BP.98 J. H. Webb et al.(Eur. J. Biochem. 270) Ó FEBS 2003Taken together, the data o[r]
Flavoproteins are ubiquitous proteins that use flavins asprosthetic groups. The common flavin cofactors are FMNand FAD, which are synthesized in vivo from riboflavin(vitamin B1) by the action of riboflavin kinase [1,2] andFAD synthetase [3]. The redox active isoalloxazine moietyof the flavin cofactor may[r]
41 Qin K, Yang DS, Yang Y, Chishti MA, Meng LJ,Kretzschmar HA, Yip CM, Fraser PE & Westaway D(2000) Copper (II)-induced conformational changes andCopper binds to cystatin B E. Zˇerovnik et al.4262 FEBS Journal 273 (2006) 4250–4263 ª 2006 The Authors Journal compilation ª 2006 FEBSprotease re[r]
tional complex or adherens junction to the actin cyto-skeleton via the cytoplasmic catenins.Therefore to characterize 14-3-3 ⁄ d–catenin inter-actions in a defined culture system where adhesivejunctions are prominent, we used Madin–Darby caninekidney (MDCK) epithelial cells. Lysates were preparedfrom[r]
its fast transition between an open and a closed stateare well known [55]. Finally, the molecular structure ofthis putative protein should ideally feature Ca2+-bind-ing sites, reactive thiol groups to facilitate channel for-mation upon oxidation, and conformationally criticalb-sheets, as sugg[r]
5to generate protein C variants. Theoligonucleotide primers used to generate the protein Cvariant constructs R9H, E16D, E26K, Q32A, V34Aand D35A are available upon request. Preparation ofthe H10Q ⁄ S11G ⁄ S12N ⁄ D23S ⁄ Q32E ⁄ N33D ⁄ H44Y constructhas been described previously [37]. The[r]
ands were extracted from Papilio RBP purified from the solublefraction of the dark-adapted retina. Extraction and analysis werecarried out under dim red light as follows. Purified protein was firstmixedwith2Mhydroxylamine and cold 90% methanol to convertaldehydes, if any, to oximes. Retinoids an[r]
whilst the 4B2 antibody, which binds to the N-terminaldomain of MDM2, marginally attenuated MDM2function (Fig. 6A, lane 4 versus lane 2). The ability ofall three monoclonal antibodies to attenuate MDM2function suggests that multiple domains of MDM2play a mechanistic role in binding to E2F1 an[r]
covalently linked to a target protein and the corre-sponding modified tryptic peptide is then sorted usingthe principles of diagonal chromatography. The exam-ple given here is a global activity-based proteomeCOFRADIC and protein modifications K. Gevaert et al.6278 FEBS Journal 274 (2007)[r]
4. Nustad, K., Onsrud, M., Jansson, B. & Warren, D. (1998) CA125 ± epitopes and molecular size. Int. J. Biol. Markers. 13,196±199.5. Lenk, U ., Oexle, K., Voit, T., Ancker, U., Hellner, K.A., Speer, A.& Hubner, C. (1996) A cy steine 3340 substitution in the dystro-glycan-binding[r]
different vesicles by the separation medium. In a ddition,smaller v esicles m ight become entrapped in l arger v esicles.Different membrane systems might aggregate nonspecifi-cally, or bind to or entrap abundant solubilized proteins.Hence, to avoid these p roblems and to unequivocally showabundance d[r]