Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Peter Buzder-Lantos"'
Autor:
Veronika Barta-Bodor, Zsuzsanna Tömösközi, Attila Vasas, Gábor Szeleczky, Peter Buzder-Lantos, György G. Ferenczy, Imre Bata, László Balázs
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 26:5429-5437
A new series of beta amino acids, which act as CXCR3 antagonists, has been identified. The formerly optimized N,N-disubstituted benzylamine derivatives with carboxylic acid function on the N-atom was used as starting point and compounds with carboxyl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::affafb38c0c18e0c11db53fd4e7a4b8e
https://doi.org/10.1016/j.bmcl.2016.10.038
https://doi.org/10.1016/j.bmcl.2016.10.038
Autor:
Sandor Batori, Attila Vasas, Imre Bata, Zsuzsanna Tömösközi, György G. Ferenczy, László Balázs, Veronika Barta-Bodor, Gábor Szeleczky, Peter Buzder-Lantos
Publikováno v:
Bioorganicmedicinal chemistry letters. 26(22)
N,N-Disubstituted benzylamine derivatives have been identified as CXCR3 antagonists. Compounds were optimized to improve affinity and selectivity, to increase metabolic stability in human and mouse liver microsomes, to increase Caco-2 permeability. O
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b97302b387b71ff87021e6251fd0b653
https://pubmed.ncbi.nlm.nih.gov/27789137
https://pubmed.ncbi.nlm.nih.gov/27789137
Publikováno v:
Bioorganicmedicinal chemistry letters. 19(10)
Bacterial type I signal peptidase is a potential target for the development of novel antibacterial agents. In this study we demonstrate that a substrate based peptide aldehyde inhibits signal peptidases with a lower IC50 value than the lipopeptides d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3169bde818035bff33b3e3b39190044
https://pubmed.ncbi.nlm.nih.gov/19362478
https://pubmed.ncbi.nlm.nih.gov/19362478
Autor:
Zoltán Bánóczi, András Szilágyi, Peter Buzder-Lantos, Peter Tompa, Ferenc Hudecz, Peter Friedrich, Attila Farkas, Agnes Tantos
Publikováno v:
The Journal of biological chemistry. 279(20)
The structural clues of substrate recognition by calpain are incompletely understood. In this study, 106 cleavage sites in substrate proteins compiled from the literature have been analyzed to dissect the signal for calpain cleavage and also to enabl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::984f4b35cf106268d0fed432749ba211
https://pubmed.ncbi.nlm.nih.gov/14988399
https://pubmed.ncbi.nlm.nih.gov/14988399
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 19:3693
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6aec04b299b3b835601e85305c907c32
https://doi.org/10.1016/j.bmcl.2009.03.169
https://doi.org/10.1016/j.bmcl.2009.03.169