Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Nikolay V. Kukushkin"'
Publikováno v:
Proceedings of the National Academy of Sciences. 119
Two-trial learning in Aplysia reveals nonlinear interactions between training trials: A single trial has no effect, but two precisely spaced trials induce long-term memory. Extracellularly regulated kinase (ERK) activity is essential for intertrial i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a3f45a5c633df2648abdf87fff75b89
https://doi.org/10.1073/pnas.2210478119
https://doi.org/10.1073/pnas.2210478119
Publikováno v:
Scientific Reports
Scientific Reports, Vol 9, Iss 1, Pp 1-12 (2019)
Scientific Reports, Vol 9, Iss 1, Pp 1-12 (2019)
Insulin-like growth factor II (IGF2) enhances memory in rodents via the mannose-6-phosphate receptor (M6PR), but the underlying mechanisms remain poorly understood. We found that human IGF2 produces an enhancement of both synaptic transmission and ne
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b8bd631557f7feaf76fb418ace1bd27
https://doi.org/10.1038/s41598-019-50923-5
https://doi.org/10.1038/s41598-019-50923-5
Autor:
Alfred L. Goldberg, Natura Myeku, Nikolay V. Kukushkin, Wai Haung Yu, Sheina Emrani, Karen Duff, Catherine L. Clelland
Publikováno v:
Nature Medicine. 22:46-53
The ubiquitin proteasome system (UPS) degrades misfolded proteins including those implicated in neurodegenerative diseases. We investigated the effects of tau accumulation on proteasome function in a mouse model of tauopathy and in a cross to a UPS r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3935a715b5c64adff0d10ce3ba4f1aa2
https://doi.org/10.1038/nm.4011
https://doi.org/10.1038/nm.4011
Autor:
Nagaranjan Chandramouli, Hermann Steller, Alfred L. Goldberg, J.F. Glickman, Nikolay V. Kukushkin, Henrik Molina, Cristinel Sandu, Chueh-Ling Kuo
Publikováno v:
Journal of Cellular and Molecular Medicine
Here, we report a novel mechanism of proteasome inhibition mediated by Thiostrepton (Thsp), which interacts covalently with Rpt subunits of the 19S proteasome and proteasome substrates. We identified Thsp in a cell-based high-throughput screen using
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97bb9ab57231ff2a1355217205e883e2
http://europepmc.org/articles/PMC4568923
http://europepmc.org/articles/PMC4568923
Autor:
Nikolay V. Kukushkin
Publikováno v:
Neurobiology of learning and memory. 153
Memory is typically defined through animal behavior, but this point of view may limit our understanding of many related processes in diverse biological systems. The concept of memory can be broadened meaningfully by considering it from the perspectiv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e552e9265880e9438af11d6f4873bd7a
https://pubmed.ncbi.nlm.nih.gov/29396326
https://pubmed.ncbi.nlm.nih.gov/29396326
Autor:
Eva‐Maria Hock, Alfred L. Goldberg, Steven P. Gygi, Juan A Gutierrez, Nikolay V. Kukushkin, Lawrence Dick, Woong Kim, Hua Liao, Zhe Sha, Andreas Peth, Henrike C. Besche
Publikováno v:
The EMBO Journal. 33:1159-1176
Degradation rates of most proteins in eukaryotic cells are determined by their rates of ubiquitination. However, possible regulation of the proteasome's capacity to degrade ubiquitinated proteins has received little attention, although proteasome inh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f50027d5569869faf1a099db12572a2
https://doi.org/10.1002/embj.201386906
https://doi.org/10.1002/embj.201386906
Removal of α-glucose residues from nascent glycoproteins in the early secretory pathway is a requirement for further N-glycan maturation. Although deglucosylation is a stepwise process mediated by endoplasmic reticulum-associated glucosidases I and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03ee644ca7de6846c458ea76f0ce78c9
https://doi.org/10.1093/glycob/cws088
https://doi.org/10.1093/glycob/cws088
Autor:
Sammi Tsegay, Dominic S. Alonzi, Spencer J. Williams, Nikolay V. Kukushkin, Tim Quach, Andrew J. Thompson, Terry D. Butters, Gideon J. Davies
Publikováno v:
Tetrahedron: Asymmetry. 23:992-997
3- O -α- d -Glucopyranosyl-swainsonine was originally proposed 17 as a potential inhibitor of the mammalian enzyme endo -α-mannosidase, but its synthesis has not been reported. Herein we report the total synthesis of this enigmatic compound, utiliz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::db48fb1f7c25c223ddb19070d0dd4c63
https://doi.org/10.1016/j.tetasy.2012.06.011
https://doi.org/10.1016/j.tetasy.2012.06.011
Publikováno v:
Proceedings of the National Academy of Sciences. 112
Although rates of protein degradation by the ubiquitin-proteasome pathway (UPS) are determined by their rates of ubiquitination, we show here that the proteasome's capacity to degrade ubiquitinated proteins is also tightly regulated. We studied the e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::291938be7d53367531de50dec2d4dfa0
https://doi.org/10.1073/pnas.1522332112
https://doi.org/10.1073/pnas.1522332112
Autor:
Marjan Huizing, Katherine Patzel, Erell Le Poëc-Celic, Yongmin Zhang, Heidi Dorward, William A. Gahl, Petcharat Leoyklang, Nikolay V. Kukushkin, Bixue Xu, Matthieu Sollogoub, Tal Yardeni, Terry D. Butters, Yves Blériot, Dominic S. Alonzi
Publikováno v:
Journal of Inherited Metabolic Disease
Journal of Inherited Metabolic Disease, 2014, 37 (2), pp.297--308. ⟨10.1007/s10545-013-9655-6⟩
Journal of Inherited Metabolic Disease, 2014, 37 (2), pp.297--308. ⟨10.1007/s10545-013-9655-6⟩
UDP-GlcNAc 2-epimerase/ManNAc 6-kinase (GNE) is a bifunctional enzyme responsible for the first committed steps in the synthesis of sialic acid, a common terminal monosaccharide in both protein and lipid glycosylation. GNE mutations are responsible f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4073b5af815b150bad0e49128aeb190
https://pubmed.ncbi.nlm.nih.gov/24136589
https://pubmed.ncbi.nlm.nih.gov/24136589