Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Mare Čudić"'
Publikováno v:
Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy. 56:2479-2489
The conformational differences caused by N-glycation of the amide bond in endogenous opioid pentapeptide leucine–enkephalin (Tyr–Gly–Gly–Phe–Leu) have been explored in solution using FTIR spectroscopy, NMR and molecular modelling. The compo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d175f665245218e18976ec90956d4794
https://doi.org/10.1016/s1386-1425(00)00336-x
https://doi.org/10.1016/s1386-1425(00)00336-x
Autor:
Mare Čudić, Jaroslav Horvat, Lidija Varga-Defterdarović, Štefica Horvat, Laszlo Otvos, László Ürge
Publikováno v:
Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy. 55:2347-2352
The conformational preferences of enkephalins and the related glycoconjugates in which free or protected carbohydrate moieties were linked to the opioid peptides through an ether, ester or amide bond were investigated by circular dichroism spectrosco
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::848785182326f5862cb1515c8fd5615f
https://doi.org/10.1016/s1386-1425(99)00132-8
https://doi.org/10.1016/s1386-1425(99)00132-8
Autor:
Jan Kihlberg, Štefica Horvat, Karl-Erik Bergquist, Jaroslav Horvat, Mikael Elofsson, Mare Čudić
Publikováno v:
Scopus-Elsevier
The influence of a new peptoid residue on amide-bond stereochemistry has been explored via the synthesis and NMR analysis of novel peptidomimetics related to the endogenous opioid pentapeptide Leu-enkephalin (H-Tyr-Gly-Gly-Phe-Leu-OH). The compounds
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::195ce24eba16d5e06ccd0c9cc0982c64
https://doi.org/10.1039/a801472h
https://doi.org/10.1039/a801472h
Autor:
Biserka Kojić-Prodić, Mikael Elofsson, Vjekoslav Milinković, Mare Čudić, Štefica Horvat, Jaroslav Horvat, Jan Kihlberg
Publikováno v:
Carbohydrate Research. 287:1-19
N-Glycated derivatives of glycine, glycylglycine, and 2,5-piperazinedione, containing the 6-deoxy-1,2:3,4-di-O-isopropylidene-α-d-galactos-6-yl moiety, were synthesized and studied by X-ray crystallography and NMR spectroscopy. The crystal structure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d32b98b386ebcf24bedc71230e0b4837
https://doi.org/10.1016/0008-6215(96)00061-4
https://doi.org/10.1016/0008-6215(96)00061-4
Autor:
YashoNandini Singh, Deepika Regmi, David Ormaza, Ramya Ayyalasomayajula, Nancy Vela, Gustavo Mundim, Deguo Du, Dmitriy Minond, Maré Cudic
Publikováno v:
Frontiers in Chemistry, Vol 10 (2022)
The amyloid-β precursor protein (APP) undergoes proteolysis by β- and γ-secretases to form amyloid-β peptides (Aβ), which is a hallmark of Alzheimer’s disease (AD). Recent findings suggest a possible role of O-glycosylation on APP’s proteoly
Externí odkaz:
https://doaj.org/article/75168e7857ee4144bf9fbeeb27b90c16
Autor:
Franck Madoux, Daniela Dreymuller, Jean-Phillipe Pettiloud, Radleigh Santos, Christoph Becker-Pauly, Andreas Ludwig, Gregg B. Fields, Thomas Bannister, Timothy P. Spicer, Mare Cudic, Louis D. Scampavia, Dmitriy Minond
Publikováno v:
Scientific Reports, Vol 6, Iss 1, Pp 1-17 (2016)
Abstract ADAM10 and ADAM17 have been shown to contribute to the acquired drug resistance of HER2-positive breast cancer in response to trastuzumab. The majority of ADAM10 and ADAM17 inhibitor development has been focused on the discovery of compounds
Externí odkaz:
https://doaj.org/article/c6750ea01d4646cda1fe10c04ac5d8b2
Autor:
Xuan Zhang, Jamee Bresee, Philip P. Cheney, Baogang Xu, Manishabrata Bhowmick, Mare Cudic, Gregg B. Fields, Wilson Barry Edwards
Publikováno v:
Molecules, Vol 19, Iss 6, Pp 8571-8588 (2014)
Matrix metalloproteinases (MMP) 2 and 9, the gelatinases, have consistently been associated with tumor progression. The development of gelatinase-specific probes will be critical for identifying in vivo gelatinoic activity to understand the molecular
Externí odkaz:
https://doaj.org/article/118caaa70e2e418aabbd0b8580604fa4