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Autor:
R. Luke Wiseman, Gabriel Kline, Kayla Nutsch, Michael J. Bollong, Jessica D. Rosarda, Kelsey R. Baron, Caroline Stanton, Jeffery W. Kelly
Publikováno v:
ACS Chemical Biology
The extracellular accumulation of glutamate is a pathologic hallmark of numerous neurodegenerative diseases including ischemic stroke and Alzheimer's disease. At high extracellular concentrations, glutamate causes neuronal damage by promoting oxidati
Publikováno v:
ACS Chemical Biology
Malaria remains an endemic tropical disease, and the emergence of Plasmodium falciparum parasites resistant to current front-line medicines means that new therapeutic targets are required. The Plasmodium glideosome is a multiprotein complex thought t
Publikováno v:
ACS Chemical Biology
ACS Chemical Biology, 14(11), 2389-2395
ACS Chemical Biology, 14(11), 2389-2395
SUMOylation is a reversible and highly dynamic post-translational modification of target proteins by small ubiquitin-like modifiers (SUMO). It is orchestrated by SUMO-activating, -conjugating, and -ligating enzymes in a sequential manner and is impor
Publikováno v:
ACS Chemical Biology
Monobodies are small engineered binding proteins that, upon expression in cells, can inhibit signaling of cytosolic oncoproteins with outstanding selectivity. Efficacy may be further increased by inducing degradation of monobody targets through fusio
Autor:
Nicolas Brauckhoff, Hazem Salamon, Marcel Schmidt, Tom N. Grossmann, Petra Janning, Christiane Stiller, Dennis M. Krüger
Publikováno v:
ACS chemical biology, 12(2), 504-509. American Chemical Society
Stiller, C, Krüger, D M, Brauckhoff, N, Schmidt, M, Janning, P, Salamon, H & Grossmann, T N 2017, ' Translocation of an Intracellular Protein via Peptide-Directed Ligation ', ACS chemical biology, vol. 12, no. 2, pp. 504-509 . https://doi.org/10.1021/acschembio.6b01013
Stiller, C, Krüger, D M, Brauckhoff, N, Schmidt, M, Janning, P, Salamon, H & Grossmann, T N 2017, ' Translocation of an Intracellular Protein via Peptide-Directed Ligation ', ACS chemical biology, vol. 12, no. 2, pp. 504-509 . https://doi.org/10.1021/acschembio.6b01013
Ligand-directed reactions allow chemical transformations at very low reactant concentrations and can thus provide access to efficient approaches for the post-translational modification of proteins. The development of these proximity-induced reactions
Autor:
Philipp M. Cromm, Herbert Waldmann, Laura Dietrich, Mathias Wendt, Roger S. Goody, Julia Kriegesmann, Philipp Küchler, Tom N. Grossmann, Jochen Spiegel
Publikováno v:
Cromm, P M, Spiegel, J, Kuchler, P, Dietrich, L, Kriegesmann, J, Wendt, M, Goody, R S, Waldmann, H & Grossmann, T N 2016, ' Protease-resistant and cell-permeable double-stapled peptides targeting the Rab8a GTPase. ', ACS chemical biology, vol. 11, pp. 2375-2382 . https://doi.org/10.1021/acschembio.6b00386
ACS chemical biology, 11, 2375-2382. American Chemical Society
ACS chemical biology, 11, 2375-2382. American Chemical Society
Small GTPases comprise a family of highly relevant targets in chemical biology and medicinal chemistry research and have been considered "undruggable" due to the persisting lack of effective synthetic modulators and suitable binding pockets. As molec
Autor:
Rick T. Dobrowsky, Brian S. J. Blagg, Jeffrey M. Holzbeierlein, George A. Vielhauer, Gaurav Garg, Heather E. Shinogle, Suman Ghosh
Publikováno v:
ACS Chemical Biology
Human Hsp90 isoforms are molecular chaperones that are often up-regulated in malignances and represent a primary target for Hsp90 inhibitors undergoing clinical evaluation. Hsp90α is a stress-inducible isoform of Hsp90 that plays a significant role
Autor:
Alex M. Chapman, Brian R. McNaughton
Publikováno v:
ACS Chemical Biology
Increased cellular levels of protein-protein interactions involving the ankyrin repeat oncoprotein gankyrin are directly linked to aberrant cellular events and numerous cancers. Inhibition of these protein-protein interactions is thus an attractive t
Autor:
Marc B. Cox, Maulik R. Patel, Pallav D. Patel, Liza Shrestha, Yanlong Kang, Tony Taldone, Erica DaGama Gomes, Monica L. Guzman, Alexander Gozman, Gabriela Chiosis, Ronnie Maharaj, Hediye Erdjument-Bromage, Anna Rodina, Cristina Santarossa, Ronald C. Hendrickson, Pengrong Yan, John Koren, Ari Melnick, Chenghua Yang, Stefan O. Ochiana, Leandro Cerchietti
Publikováno v:
ACS Chemical Biology
Heat shock protein 70 (Hsp70) is a family of proteins with key roles in regulating malignancy. Cancer cells rely on Hsp70 to inhibit apoptosis, regulate senescence and autophagy, and maintain the stability of numerous onco-proteins. Despite these imp
Autor:
Sharon M. Louie, Daniel I. Benjamin, Lauryn G Chan, Antonio Sorrentino, Rebecca A. Kohnz, Daniel K. Nomura, Melinda M. Mulvihill, Alyssa J. Cozzo, Shu-Wing Ng, Andrei Goga, Sourav Bandyopadhyay, Anayo Ohiri, Daniel S. Li
Publikováno v:
ACS Chemical Biology
Cancer cells possess fundamentally altered metabolism that supports their pathogenic features, which includes a heightened reliance on aerobic glycolysis to provide precursors for synthesis of biomass. We show here that inositol polyphosphate phospha