Zobrazeno 1 - 10
of 83
pro vyhledávání: '"Mare, Cudic"'
Publikováno v:
Glycoconjugate Journal. 39:587-597
Lectins, carbohydrate-binding proteins, play important functions in all forms of life from bacteria and viruses to plants, animals, and humans, participating in cell–cell communication and pathogen binding. In an attempt to modify lectin functions,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83518491c6a42a346ac3225182c748b7
https://doi.org/10.1007/s10719-022-10079-3
https://doi.org/10.1007/s10719-022-10079-3
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
Publikováno v:
ACS Chemical Neuroscience. 12:2974-2980
The amyloid-β precursor protein (APP) undergoes proteolytic cleavage by α-, β-, and γ-secretases, to determine its fate in Alzheimer's disease (AD) pathogenesis. Recent findings suggest a possible role of O-glycosylation in APP's proteolytic proc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1a44b132bc59ffcbb68b862a891105eb
https://doi.org/10.1021/acschemneuro.1c00387
https://doi.org/10.1021/acschemneuro.1c00387
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
Autor:
Forrest G FitzGerald, Jürgen Kopitz, Hans-Joachim Gabius, Malwina Michalak, Herbert Kaltner, Donella Beckwith, Anna-Kristin Ludwig, Elizabeth R Mercer, Maria C. Rodriguez Benavente, Mare Cudic
Publikováno v:
Biochemistry. 60:547-558
Human macrophage galactose-type lectin (hMGL, HML, CD301, CLEC10A), a C-type lectin expressed by dendritic cells and macrophages, is a receptor for N-acetylgalactosamine α-linked to serine/threonine residues (Tn antigen, CD175) and its α2,6-sialyla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5bc981b2ac478f60608b4c053f452d4b
https://doi.org/10.1021/acs.biochem.0c00942
https://doi.org/10.1021/acs.biochem.0c00942
Autor:
Mare Cudic, YashoNandini Singh
Publikováno v:
The FASEB Journal. 36
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c2a51b98357348a5d3030c0e48ec5d5a
https://doi.org/10.1096/fasebj.2022.36.s1.r4274
https://doi.org/10.1096/fasebj.2022.36.s1.r4274
Autor:
Francisco J. Medrano, Mare Cudic, Hans-Joachim Gabius, Mark Reihill, Antonio A. Romero, Forrest G FitzGerald, Tammo Diercks, Donella Beckwith, Stefan Oscarson, Martin Jaeger Pedersen, Anna-Kristin Ludwig
Publikováno v:
Chemistry (Weinheim an Der Bergstrasse, Germany)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Digital.CSIC. Repositorio Institucional del CSIC
instname
10 p.-6 fig.-3 tb.
Functional pairing between cellular glyco-con-ju-gates and tissue lectins like galectins has wide (patho)physio-logical significance. Their study is facilitated by non-hydrolyzable deri-va-tives of the natural O-glycans, such
Functional pairing between cellular glyco-con-ju-gates and tissue lectins like galectins has wide (patho)physio-logical significance. Their study is facilitated by non-hydrolyzable deri-va-tives of the natural O-glycans, such
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c376d7f6b08ab469bba1303caa4750ac
https://doi.org/10.1002/chem.202003143
https://doi.org/10.1002/chem.202003143
Autor:
Gregg B. Fields, Mare Cudic, Maria C. Rodriguez Benavente, Forrest G. FitzGerald, Hongjie Wang, Yaima Rivero, Camelia Garcia, YashoNandini Singh
Publikováno v:
Glycoconj J
Aberrant Mucin-1 (MUC1) glycosylation with the Thomsen-Friedenreich (TF) tumor-associated antigen (CD176) is a hallmark of epithelial carcinoma progression and poor patient prognosis. Recognition of TF by glycan-binding proteins, such as galectins, e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2abb4f5917042513d1d577b6d25c6b1e
https://doi.org/10.1007/s10719-020-09951-x
https://doi.org/10.1007/s10719-020-09951-x
Autor:
Mare Cudic, Nicolai V. Bovin, Herbert Kaltner, Joachim C. Manning, Donella Beckwith, Fred Sinowatz, Anna-Kristin Ludwig, Paul V. Murphy, Tanja J Kutzner, Adele Gabba, Hans-Joachim Gabius, Gabriel García Caballero, Nadezhda Shilova
Publikováno v:
Histochemistry and Cell Biology
Histochem Cell Biol
Histochem Cell Biol
The concept of biomedical significance of the functional pairing between tissue lectins and their glycoconjugate counterreceptors has reached the mainstream of research on the flow of biological information. A major challenge now is to identify the p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e6dad1a9ebe9a600041061115a75895
http://europepmc.org/articles/PMC7429544
http://europepmc.org/articles/PMC7429544
Autor:
Gabriel, García Caballero, Joachim C, Manning, Adele, Gabba, Donella, Beckwith, Forrest G, FitzGerald, Tanja J, Kutzner, Anna-Kristin, Ludwig, Herbert, Kaltner, Paul V, Murphy, Mare, Cudic, Hans-Joachim, Gabius
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2442
Dynamic changes of a cell's glycophenotype are increasingly interpreted as shifts in the capacity to interact with tissue (endogenous) lectins. The status of glycan branching or chain length (e.g., core 1 vs core 2 mucin-type O-glycans and polyLacNAc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::74ebb2db8cdcebf054a00e3df5f793e3
https://pubmed.ncbi.nlm.nih.gov/35320533
https://pubmed.ncbi.nlm.nih.gov/35320533