Ac-HHASPRK-NH2
Ref. 3D-PP48024
Tamaño no definido | A consultar |
Información del producto
Peptide Ac-HHASPRK-NH2 is a Research Peptide with significant interest within the field academic and medical research. This peptide is available for purchase at Cymit Quimica in multiple sizes and with a specification of your choice. Recent citations using Ac-HHASPRK-NH2 include the following: Clickable 5'-γ-Ferrocenyl Adenosine Triphosphate Bioconjugates in Kinase-Catalyzed Phosphorylations. Z She , N Wang, YC Lin, HB Kraatz - A European Journal, 2015 - search.ebscohost.comhttps://search.ebscohost.com/login.aspx?direct=true&profile=ehost&scope=site&authtype=crawler&jrnl=09476539&asa=N&AN=101516659&h=gY65k9Qj78xF%2BVgpeyuT%2FDja8q95f4rA9vFMsPxz9Q1kuyqtvrTdQD%2BeS%2Fn%2F8NN%2BAFaaeKIDqxUyKtXniP33UA%3D%3D&crl=c Multiplex isotope dimethyl labeling of substrate peptides for high throughput kinase activity assay via quantitative MALDI MS Z Deng, M Ye , Y Bian , Z Liu , F Liu, C Wang - Chemical , 2014 - pubs.rsc.orghttps://pubs.rsc.org/en/content/articlehtml/2014/cc/c4cc04906c Explaining the inhibition of cyclin-dependent kinase 5 by peptides derived from p25 with molecular dynamics simulations and MM-PBSA VBC Tan , B Zhang, KM Lim , TE Tay - Journal of molecular modeling, 2010 - Springerhttps://link.springer.com/article/10.1007/s00894-009-0514-1 Electrochemical investigations of sarcoma-related protein kinase inhibition S Martic , M Labib , HB Kraatz - Electrochimica acta, 2011 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S001346861100733X Enzymatically modified peptide surfaces: towards general electrochemical sensor platform for protein kinase catalyzed phosphorylations S Martic , M Labib , HB Kraatz - Analyst, 2011 - pubs.rsc.orghttps://pubs.rsc.org/en/content/articlehtml/2011/an/c0an00438c Structural biology of cell-cycle proteins S Major, JA Endicott - Drug Discovery Today: Targets, 2004 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S1741837204024314 The structure of cyclin E1/CDK2: implications for CDK2 activation and CDK2-independent roles R Honda, ED Lowe, E Dubinina, V Skamnaki - The EMBO , 2005 - embopress.orghttps://www.embopress.org/doi/abs/10.1038/sj.emboj.7600554 The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases NR Brown, MEM Noble , JA Endicott , LN Johnson - Nature cell biology, 1999 - nature.comhttps://www.nature.com/articles/ncb1199_438 Cyclin B and cyclin A confer different substrate recognition properties on CDK2 NR Brown, ED Lowe, E Petri, V Skamnaki , R Antrobus - Cell Cycle, 2007 - Taylor & Francishttps://www.tandfonline.com/doi/abs/10.4161/cc.6.11.4278 Use of docking peptides to design modular substrates with high efficiency for mitogen-activated protein kinase extracellular signal-regulated kinase N Fernandes, DE Bailey, DL VanVranken - ACS chemical , 2007 - ACS Publicationshttps://pubs.acs.org/doi/abs/10.1021/cb700158q Evidence that the substrate backbone conformation is critical to phosphorylation by p42 MAP kinase M Weiwad, G Kullertz, M Schutkowski, G Fischer - FEBS letters, 2000 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0014579300017944 Computational study of the phosphoryl transfer catalyzed by a cyclin-dependent kinase M De Vivo , A Cavalli , P Carloni - Chemistry-A European , 2007 - Wiley Online Libraryhttps://chemistry-europe.onlinelibrary.wiley.com/doi/abs/10.1002/chem.200700044 Fluorescent peptide biosensor for probing the relative abundance of cyclin-dependent kinases in living cells L Kurzawa , M Pellerano, JB Coppolani, MC Morris - PloS one, 2011 - journals.plos.orghttps://journals.plos.org/plosone/article?id=10.1371/journal.pone.0026555 The role of the phospho-CDK2/cyclin A recruitment site in substrate recognition KY Cheng, MEM Noble , V Skamnaki , NR Brown - Journal of biological , 2006 - ASBMBhttps://www.jbc.org/article/S0021-9258(19)47657-6/abstract Improved method for the identification and validation of allosteric sites K Song, X Liu, W Huang , S Lu, Q Shen - Journal of chemical , 2017 - ACS Publicationshttps://pubs.acs.org/doi/abs/10.1021/acs.jcim.7b00014 Antibody-free time-resolved terbium luminescence assays designed for cyclin-dependent kinase 5 (CDK5) JL Heier, DJ Boselli, LL Parker - bioRxiv, 2024 - biorxiv.orghttps://www.biorxiv.org/content/10.1101/2024.04.24.590988.abstract The role of Thr160 phosphorylation of Cdk2 in substrate recognition JK Holmes, MJ Solomon - European Journal of Biochemistry, 2001 - Wiley Online Libraryhttps://febs.onlinelibrary.wiley.com/doi/abs/10.1046/j.1432-1327.2001.02392.x Cyclin-dependent kinases: inhibition and substrate recognition JA Endicott , MEM Noble , JA Tucker - Current opinion in structural biology, 1999 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0959440X9900038X Structural prediction of the interaction of the tumor suppressor p27KIP1 with cyclin A/CDK2 identifies a novel catalytically relevant determinant J Li , J Vervoorts, P Carloni , G Rossetti , B Luscher - BMC bioinformatics, 2017 - Springerhttps://link.springer.com/article/10.1186/s12859-016-1411-0 Insight into the mechanism of intramolecular inhibition of the catalytic activity of sirtuin 2 (SIRT2) J Li , F Flick, P Verheugd, P Carloni , B Luscher - PLoS , 2015 - journals.plos.orghttps://journals.plos.org/plosone/article?id=10.1371/journal.pone.0139095 Emerging approaches to cdk inhibitor development, a structural perspective I Hope, JA Endicott , JE Watt - RSC Chemical Biology, 2023 - pubs.rsc.orghttps://pubs.rsc.org/en/content/articlehtml/2023/cb/d2cb00201a mechanism of inhibition of the cyclin-dependent kinase-2 as revealed by the molecular dynamics study on the complex CDK2 with the peptide substrate HHASPRK I Bartova, M Otyepka , Z Kà â¢acaÂà Ÿ, J KoÃÂa - Protein science, 2005 - Wiley Online Libraryhttps://onlinelibrary.wiley.com/doi/abs/10.1110/ps.04959705 Functional flexibility of human cyclin-dependent kinase-2 and its evolutionary conservation I Bartova, J KoÃÂa, M Otyepka - Protein Science, 2008 - Wiley Online Libraryhttps://onlinelibrary.wiley.com/doi/abs/10.1110/ps.072951208 Regulatory phosphorylation of cyclin-dependent kinase 2: insights from molecular dynamics simulations I Bartova, J KoÃÂa, M Otyepka - Journal of molecular modeling, 2008 - Springerhttps://link.springer.com/article/10.1007/s00894-008-0312-1 Influences of phosphorylation on Thr14/Tyr15 in CDK5 in the presence of roscovitine/ATP and HHASPRK HX Jin, B Zhang, YX Jun, JL Xu, VBC Tan - Molecular Simulation, 2012 - Taylor & Francishttps://www.tandfonline.com/doi/abs/10.1080/08927022.2011.616503 Identification and Characterization of an Irreversible Inhibitor of CDK2 E Anscombe, E Meschini, R Mora-Vidal, MP Martin - Chemistry & biology, 2015 - cell.comhttps://www.cell.com/ccbio/pdf/S1074-5521(15)00323-3.pdf Enrichment of peptides containing consensus sequence by an enzymatic approach for targeted analysis ofproteins C Wang , M Ye , G Han , R Chen , M Zhang, X Jiang - , 2011 - Wiley Online Libraryhttps://analyticalsciencejournals.onlinelibrary.wiley.com/doi/abs/10.1002/pmic.201100041 Cyclin-dependent kinase homologues of Plasmodium falciparum C Doerig , J Endicott , D Chakrabarti - International journal for parasitology, 2002 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0020751902001868 The activation and inhibition of cyclin-dependent kinase-5 by phosphorylation B Zhang, VBC Tan , KM Lim , TE Tay - Biochemistry, 2007 - ACS Publicationshttps://pubs.acs.org/doi/abs/10.1021/bi700890t Recent developments in cyclin-dependent kinase biochemical and structural studies A Echalier, JA Endicott , MEM Noble - Biochimica et Biophysica Acta (BBAhttps://www.sciencedirect.com/science/article/pii/S157096390900291X Structural Studies on Phospho-CDK2/Cyclin A Bound to Nitrate, a Transition State Analogue: Implications for the Protein Kinase Mechanism, A Cook , ED Lowe, ED Chrysina , VT Skamnaki - Biochemistry, 2002 - ACS Publicationshttps://pubs.acs.org/doi/abs/10.1021/bi0201724
Propiedades químicas
Consulta técnica sobre: 3D-PP48024 Ac-HHASPRK-NH2
Si desea solicitar un presupuesto o realizar un pedido, por favor añada los productos deseados a su carrito y solicite un presupuesto o pedido desde el carrito. Es más rápido, más barato, y podrá beneficiarse de los descuentos y las ventajas disponibles.