Zobrazeno 1 - 10
of 114
pro vyhledávání: '"Suren A. Tatulian"'
Autor:
Abhijith G. Karkisaval, Rowan Hassan, Andrew Nguyen, Benjamin Balster, Faisal Abedin, Ratnesh Lal, Suren A. Tatulian
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-13 (2024)
Abstract Amyloid β (Aβ) ion channels destabilize cellular ionic homeostasis, which contributes to neurotoxicity in Alzheimer’s disease. The relative roles of various Aβ isoforms are poorly understood. We use bilayer electrophysiology, AFM imagin
Externí odkaz:
https://doaj.org/article/34b1fdc52ba14d6ab28ab5b80004d6f0
Autor:
Albert Serrano, Jessica L. Guyette, Joel B. Heim, Michael Taylor, Patrick Cherubin, Ute Krengel, Ken Teter, Suren A. Tatulian
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-13 (2022)
Abstract Cholera toxin (CT) and Escherichia coli heat-labile enterotoxin (LT) are structurally similar AB5-type protein toxins. They move from the cell surface to the endoplasmic reticulum where the A1 catalytic subunit is separated from its holotoxi
Externí odkaz:
https://doaj.org/article/db9466b3103b44358adb5e591046c56c
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
Abstract Amyloid β (Aβ) peptide aggregation plays a central role in Alzheimer’s disease (AD) etiology. AD drug candidates have included small molecules or peptides directed towards inhibition of Aβ fibrillogenesis. Although some Aβ-derived pept
Externí odkaz:
https://doaj.org/article/2af0e39adc3a49bca758d8f9304b214d
Autor:
Albert Serrano, Xin Qiao, Jason O. Matos, Lauren Farley, Lucia Cilenti, Bo Chen, Suren A. Tatulian, Ken Teter
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 8 (2020)
Aggregates of α-synuclein contribute to the etiology of Parkinson’s Disease. Protein disulfide isomerase (PDI), a chaperone and oxidoreductase, blocks the aggregation of α-synuclein. An S-nitrosylated form of PDI that cannot function as a chapero
Externí odkaz:
https://doaj.org/article/2d251f86f84b4b4ea4970e424a2bfcff
Autor:
Jessica Guyette, Patrick Cherubin, Albert Serrano, Michael Taylor, Faisal Abedin, Morgan O’Donnell, Helen Burress, Suren A. Tatulian, Ken Teter
Publikováno v:
Toxins, Vol 11, Iss 8, p 458 (2019)
Protein disulfide isomerase (PDI) is mainly located in the endoplasmic reticulum (ER) but is also secreted into the bloodstream where its oxidoreductase activity is involved with thrombus formation. Quercetin-3-rutinoside (Q3R) blocks this activity,
Externí odkaz:
https://doaj.org/article/d670959300094e5d9e1f4845591967e3
Autor:
G. Robb Huhn, Celine Sparkes, Isabel Silva, Carla Reyes, Gisselle Perez, Fatema Khondker, Teriana Jones, Ashley Fragoso, Paula Contreras, Michelle Alvarez, Maria C. Zabala-Rodriguez, Suren A. Tatulian, Ken Teter
Publikováno v:
Biochemical and Biophysical Research Communications. 636:57-63
The cytolethal distending toxins (CDTs) produced by many Gram-negative pathogens are tripartite genotoxins with a single catalytic subunit (CdtB) and two cell-binding subunits (CdtA + CdtC). CDT moves by vesicle carriers from the cell surface to the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::722167416546bc2c21d7864f57112a21
https://doi.org/10.1016/j.bbrc.2022.10.068
https://doi.org/10.1016/j.bbrc.2022.10.068
Autor:
Suren A, Tatulian
Publikováno v:
Drug Discovery Today. 27:1027-1043
Recent drug development efforts targeting Alzheimer's disease (AD) have failed to produce effective disease-modifying agents for many reasons, including the substantial presymptomatic neuronal damage that is caused by the accumulation of the amyloid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::529b3dc89d9fc5fcaaf49100be38216a
https://doi.org/10.1016/j.drudis.2022.01.016
https://doi.org/10.1016/j.drudis.2022.01.016
Autor:
Ute Krengel, Albert Serrano, Ken Teter, Michael Prentice Taylor, Jessica Guyette, Joel B. Heim, Suren A. Tatulian, Patrick Cherubin
Publikováno v:
Scientific Reports
Scientific Reports, Vol 12, Iss 1, Pp 1-13 (2022)
Scientific Reports, Vol 12, Iss 1, Pp 1-13 (2022)
Cholera toxin (CT) and Escherichia coli heat-labile enterotoxin (LT) are structurally similar AB5-type protein toxins. They move from the cell surface to the endoplasmic reticulum where the A1 catalytic subunit is separated from its holotoxin by prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95f9bff8f0cb3b900c19b9b862dcd8f9
http://europepmc.org/articles/PMC8741891
http://europepmc.org/articles/PMC8741891
Autor:
Suren A. Tatulian
Publikováno v:
Biophysical Journal. 122:367a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6cf92ec5cbfa2d88a9e4a66e67858580
https://doi.org/10.1016/j.bpj.2022.11.2023
https://doi.org/10.1016/j.bpj.2022.11.2023
Publikováno v:
Scientific Reports, Vol 9, Iss 1, Pp 1-12 (2019)
Scientific Reports
Scientific Reports
The amyloid β (Aβ) peptide and its shorter variants, including a highly cytotoxic Aβ25–35 peptide, exert their neurotoxic effect during Alzheimer’s disease by various mechanisms, including cellular membrane permeabilization. The intrinsic poly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::273c21c02921a059931e1fe454091105
http://link.springer.com/article/10.1038/s41598-019-38749-7
http://link.springer.com/article/10.1038/s41598-019-38749-7