Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Kim Y.P. Apperley"'
Publikováno v:
Trends in Pharmacological Sciences. 36:32-40
Tissue transglutaminase (TG2) catalyzes the cross-linking of proteins by the formation of isopeptide bonds between glutamine (Gln) and lysine (Lys) side chains. Although TG2 is essential for the stabilization of the extracellular matrix, its unregula
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6fc85c5488884fb746cbca98753d2dd3
https://doi.org/10.1016/j.tips.2014.10.014
https://doi.org/10.1016/j.tips.2014.10.014
Autor:
Amina Mulani, Kim Y.P. Apperley, Jeffrey W. Keillor, Christopher M. Clouthier, Abdullah Akbar
Publikováno v:
Bioorganic Chemistry. 57:186-197
Tissue transglutaminase (TG2) is a calcium-dependent enzyme that catalyses several acyl transfer reactions. The most biologically relevant of these involve protein-bound Gln residues as an acyl-donor substrate, and either water or a primary amine as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c838de73f2a48b98baca3772031ab9b
https://doi.org/10.1016/j.bioorg.2014.06.003
https://doi.org/10.1016/j.bioorg.2014.06.003
Autor:
Luca Valgimigli, Kim Y.P. Apperley, Huan Huan Chen, Ondrej Soukup, Jeffrey W. Keillor, Melissa Guardigni, Andrea Baschieri, Tereza Kobrlova, Manuela Bartolini, Andrea Milelli, Manuela Basso, Serena Montanari, Angela De Simone, Vincenza Andrisano
none 14 si Alzheimer's disease (AD) is a multifactorial pathology that requires multifaceted agents able to address its peculiar nature. In recent years, a plethora of proteins and biochemical pathways has been proposed as possible targets to counter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a8093a0ba9315b68cb9be88e4a130d6
http://hdl.handle.net/11585/606454
http://hdl.handle.net/11585/606454
Autor:
Nicholas Brunet-Filion, Jeffrey W. Keillor, Kim Y.P. Apperley, Sara-Pier Piscopo, Élise De Francesco, Isabelle Roy, Catherine Hao, Vincent Saucier, Christophe Pardin
Publikováno v:
MedChemComm. 8(2)
Previous studies within our group have yielded a class of cinnamoyl-based competitive reversible inhibitors for tissue transglutaminase (TG2), with Ki values as low as 1.0 μM (compound CP4d). However, due to the electrophilic nature of their alkene
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a809ebab109f6df30081a7a1edefa55f
https://pubmed.ncbi.nlm.nih.gov/30108749
https://pubmed.ncbi.nlm.nih.gov/30108749
Autor:
Kim Y.P. Apperley, Jeffrey W. Keillor
Publikováno v:
Expert opinion on therapeutic patents. 26(1)
Introduction: Transglutaminases (TGases) are a class of enzymes that play multifunctional roles. Their protein-crosslinking activity has been linked to fibrosis and Huntington’s disease, their glutamine deamidation activity has been related to celi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a29e03b1ea46c78ec87eb6c89147aba5
https://pubmed.ncbi.nlm.nih.gov/26560530
https://pubmed.ncbi.nlm.nih.gov/26560530
Publikováno v:
Trends in Pharmacological Sciences. 36:417
The KI value shown for KCC009 (on page 34, line 8 and in Figure 2) is actually the value reported for the diastereomeric mixture, see [45]. In contrast, the enantiomerically pure form of KCC009 (as drawn in Figure 2) was reported to have an inhibitio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7e3f4b4fba6102ff8cf74eb87e2d9588
https://doi.org/10.1016/j.tips.2015.04.009
https://doi.org/10.1016/j.tips.2015.04.009