Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Aaron T. Balana"'
Autor:
Sunhee Hwang, Aaron T. Balana, Bryan Martin, Michael Clarkson, Paola Di Lello, Hao Wu, Yanjie Li, Jakob Fuhrmann, Yavuz Dagdas, Patrick Holder, Christina I. Schroeder, Stephen E. Miller, Xinxin Gao
Publikováno v:
ACS Bio & Med Chem Au, Vol 4, Iss 4, Pp 190-203 (2024)
Externí odkaz:
https://doaj.org/article/1a3d2795bb0a44008daaaed7872dd7d8
Autor:
Paul M. Levine, Timothy W. Craven, Xinting Li, Aaron T. Balana, Gregory H. Bird, Marina Godes, Patrick J. Salveson, Patrick W. Erickson, Mila Lamb, Maggie Ahlrichs, Michael Murphy, Cassandra Ogohara, Meerit Y. Said, Loren D. Walensky, Matthew R. Pratt, David Baker
Publikováno v:
ACS Chem Biol
Peptide and protein bioconjugation technologies have revolutionized our ability to site-specifically or chemoselectively install a variety of functional groups for applications in chemical biology and medicine, including the enhancement of bioavailab
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b694595cf409370fd01594d28a8eb682
https://pubmed.ncbi.nlm.nih.gov/35319882
https://pubmed.ncbi.nlm.nih.gov/35319882
Autor:
Aaron T. Balana, Anne-Laure Mahul-Mellier, Binh A Nguyen, Mian Horvath, Afraah Javed, Eldon R. Hard, Yllza Jasiqi, Preeti Singh, Shumaila Afrin, Rose Pedretti, Virender Singh, Virginia M.-Y. Lee, Kelvin C. Luk, Lorena Saelices, Hilal A. Lashuel, Matthew R. Pratt
Publikováno v:
bioRxiv
The process of amyloid fibril formation remains one of the primary targets for developing diagnostics and treatments for several neurodegenerative diseases (NDDs). Amyloid-forming proteins such α-Synuclein and Tau, which are implicated in the pathog
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e9a9ba932fcb45cc42feb6f11579b5d
https://doi.org/10.1101/2023.03.07.531573
https://doi.org/10.1101/2023.03.07.531573
Autor:
Beat Fierz, Harsh Nagpal, Stuart P. Moon, Matthew R. Pratt, Karen M. Vasquez, Anirban Mukherjee, Aaron T. Balana
Publikováno v:
J Am Chem Soc
Protein O-GlcNAcylation is an essential and dynamic regulator of myriad cellular processes, including DNA replication and repair. Proteomic studies have identified the multifunctional nuclear protein HMGB1 as O-GlcNAcylated, providing a potential lin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d1ef10817a2b9445ab5b6c1230626b2
https://doi.org/10.1021/jacs.1c06192
https://doi.org/10.1021/jacs.1c06192
Autor:
Matthew R. Pratt, Aaron T. Balana
Publikováno v:
Biochem J
Neurodegenerative diseases such as Alzheimer's and Parkinson's remain highly prevalent and incurable disorders. A major challenge in fully understanding and combating the progression of these diseases is the complexity of the network of processes tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f20772af7d136fc812a4347ce599f903
https://doi.org/10.1042/bcj20200609
https://doi.org/10.1042/bcj20200609
Autor:
Aaron T. Balana, Ricardo Palos Pacheco, Matthew R. Pratt, Ananya Rakshit, Ana Galesic, Giuliano Cutolo, Stuart P. Moon
Publikováno v:
ACS Chemical Biology. 16:14-19
O-GlcNAc modification of the microtubule associated protein tau and α-synuclein can directly inhibit the formation of the associated amyloid fibers associated with major classes of neurodegenerative diseases. However, the mechanism(s) by which this
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6cfce5b1c4dabc9d1d8948db793f3bcc
https://doi.org/10.1021/acschembio.0c00716
https://doi.org/10.1021/acschembio.0c00716
Ubiquitination Can Change the Structure of the α-Synuclein Amyloid Fiber in a Site Selective Fashion
Publikováno v:
J Org Chem
Toxic amyloid aggregates are a feature of many neurodegenerative diseases. A number of biochemical and structural studies have demonstrated that not all amyloids of a given protein are equivalent but rather that an aggregating protein can form differ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e354e07fb06e0c5f2b26138a7e5abf8
https://doi.org/10.1021/acs.joc.9b02641
https://doi.org/10.1021/acs.joc.9b02641
Autor:
Antonieta L. Salguero, Maggie Chen, Aaron T. Balana, Nam Chu, Hanjie Jiang, Brad A. Palanski, Hwan Bae, Katharine M. Wright, Sara Nathan, Heng Zhu, Sandra B. Gabelli, Matthew R. Pratt, Philip A. Cole
Publikováno v:
ACS Chem Biol
Akt is a Ser/Thr protein kinase that regulates cell growth and metabolism and is considered a therapeutic target for cancer. Regulation of Akt by membrane recruitment and post-translational modifications (PTMs) has been extensively studied. The most
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c15d36d59b7843dca665dad46ecbbbc
https://europepmc.org/articles/PMC8864695/
https://europepmc.org/articles/PMC8864695/
Publikováno v:
Curr Opin Chem Biol
Alterations to the global levels of certain types of post-translational modifications (PTMs) are commonly observed in neurodegenerative diseases. The net influence of these PTM changes to the progression of these diseases can be deduced from cellular
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab63983f87845c50f073c441a8e7b7b1
https://europepmc.org/articles/PMC8585673/
https://europepmc.org/articles/PMC8585673/
Autor:
Ana, Galesic, Ananya, Rakshit, Giuliano, Cutolo, Ricardo Palos, Pacheco, Aaron T, Balana, Stuart P, Moon, Matthew R, Pratt
Publikováno v:
ACS Chem Biol
O-GlcNAc modification of tau and α-synuclein can directly inhibit the formation of the associated amyloid fibers associated with major classes of neurodegenerative diseases. However, the mechanism(s) by which this posttranslational modification inhi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4ee21f12e436f1b774955fe488b37fa3
https://pubmed.ncbi.nlm.nih.gov/33399442
https://pubmed.ncbi.nlm.nih.gov/33399442