Zobrazeno 1 - 10
of 132
pro vyhledávání: '"Jetze J. Tepe"'
Publikováno v:
iScience, Vol 27, Iss 7, Pp 110166- (2024)
Summary: Synucleinopathies are a class of neurodegenerative diseases defined by the presence of α-synuclein inclusions. The location and composition of these α-synuclein inclusions directly correlate to the disease pattern. The inclusions in Multip
Externí odkaz:
https://doaj.org/article/8114e2473a6e4327ac81e2d6d19b3039
Autor:
Evert Njomen, Allison Vanecek, Theresa A. Lansdell, Ya-Ting Yang, Peter Z. Schall, Christi M. Harris, Matthew P. Bernard, Daniel Isaac, Omar Alkharabsheh, Anas Al-Janadi, Matthew B. Giletto, Edmund Ellsworth, Catherine Taylor, Terence Tang, Sarah Lau, Marc Bailie, Jamie J. Bernard, Vilma Yuzbasiyan-Gurkan, Jetze J. Tepe
Publikováno v:
Biomedicines, Vol 10, Iss 5, p 938 (2022)
Despite the addition of several new agents to the armamentarium for the treatment of multiple myeloma (MM) in the last decade and improvements in outcomes, the refractory and relapsing disease continues to take a great toll, limiting overall survival
Externí odkaz:
https://doaj.org/article/5652d0bf98fa41f3bca6c26155ccef6f
Autor:
Dare E. George, Jetze J. Tepe
Publikováno v:
Biomolecules, Vol 11, Iss 12, p 1789 (2021)
The proteasome system is a large and complex molecular machinery responsible for the degradation of misfolded, damaged, and redundant cellular proteins. When proteasome function is impaired, unwanted proteins accumulate, which can lead to several dis
Externí odkaz:
https://doaj.org/article/7b7a255ab8ca42199e9be0cef32c1b97
Autor:
Corey L. Jones, Jetze J. Tepe
Publikováno v:
Molecules, Vol 24, Iss 15, p 2841 (2019)
Loss of proteome fidelity leads to the accumulation of non-native protein aggregates and oxidatively damaged species: hallmarks of an aged cell. These misfolded and aggregated species are often found, and suggested to be the culpable party, in numero
Externí odkaz:
https://doaj.org/article/11a6ac0b4ec74b60a121d624433ca396
Autor:
Evan Savelson, Jetze J. Tepe
Publikováno v:
Organic Letters. 25:3698-3701
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::90f6a1e23dae1c1db360de7d26b00399
https://doi.org/10.1021/acs.orglett.3c01139
https://doi.org/10.1021/acs.orglett.3c01139
Autor:
Sophia D. Staerz, Erika M. Lisabeth, Evert Njomen, Thomas S. Dexheimer, Richard R. Neubig, Jetze J. Tepe
Publikováno v:
ACS Omega. 8:15650-15659
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::68594d4b374e3503ad634e530ac8d11e
https://doi.org/10.1021/acsomega.3c01158
https://doi.org/10.1021/acsomega.3c01158
Publikováno v:
Dalton Transactions. 52:721-730
Metal quinoline complexes were prepared using a quinoline-based proteasome inhibitor (Quin1) and an inactive quinoline ligand (Quin2), and their cytotoxicities are reported towards multiple myeloma-related cell lines.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2809dd84da2c0e86b3e7d4921fa32276
https://doi.org/10.1039/d2dt03484k
https://doi.org/10.1039/d2dt03484k
Publikováno v:
The Journal of Organic Chemistry. 87:16820-16828
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1a02d515285df6df919865816127c857
https://doi.org/10.1021/acs.joc.2c02544
https://doi.org/10.1021/acs.joc.2c02544
Publikováno v:
ACS Chemical Neuroscience.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b038ebe61783499e404c6789b9d5c49b
https://doi.org/10.1021/acschemneuro.2c00732
https://doi.org/10.1021/acschemneuro.2c00732
Publikováno v:
Dalton transactions (Cambridge, England : 2003).
A rare example of a structurally characterized metal quinoline complex was prepared using a non-covalent quinoline-based proteasome inhibitor (Quin1), and a related complex bearing an inactive quinoline ligand (Quin2) was also synthesized. The quinol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ba367029e1fb6c1364baa6a55e540518
https://pubmed.ncbi.nlm.nih.gov/36562335
https://pubmed.ncbi.nlm.nih.gov/36562335