Zobrazeno 1 - 10
of 48
pro vyhledávání: '"Verónica I. Dodero"'
Publikováno v:
Molecules, Vol 24, Iss 13, p 2508 (2019)
Transcription factors are proteins lying at the endpoint of signaling pathways that control the complex process of DNA transcription. Typically, they are structurally disordered in the inactive state, but in response to an external stimulus, like a s
Externí odkaz:
https://doaj.org/article/4a99cbdea2944de49af4eb11a1ee66aa
Publikováno v:
ARKIVOC, Vol 2005, Iss 12, Pp 88-97 (2005)
Externí odkaz:
https://doaj.org/article/0d3d57ddcad54e849b7c2b6d7684c9c4
Autor:
Verónica I. Dodero, Nelda N. Giagante, Sandra D. Mandolesi, Adriana E. Zúñiga, Julio C. Podestá
Publikováno v:
ARKIVOC, Vol 2003, Iss 10, Pp 335-346 (2003)
Externí odkaz:
https://doaj.org/article/b50e49948b984258a75e929856225af9
Autor:
Nicolo Tonali, Julia Kaffy, Vadim Le Joncour, David C. Schröder, Pirjo Laakkonen, Loreen Hericks, Antoine Marion, Norbert Sewald, Verónica I. Dodero, Sandrine Ongeri, Oliver Kracker, Radosław Krzemieniecki
Publikováno v:
ChemPlusChem. 86:840-851
In peptidotriazolamers every second peptide bond is replaced by a 1H-1,2,3-triazole. Such foldamers are expected to bridge the gap in molecular weight between small-molecule drugs and protein-based drugs. Amyloid beta (Abeta) aggregates play an impor
Autor:
Isabell Kemker, Elmira Ghabraie, Verónica I. Dodero, Nicolo Tonali, Norbert Sewald, Mohamed Ismail
Publikováno v:
Chemistry (Weinheim an Der Bergstrasse, Germany)
Cyclic RGD peptides are well‐known ligands of integrins. The integrins αVβ3 and α5β1 are involved in angiogenesis, and integrin αVβ3 is abundantly present on cancer cells, thus representing a therapeutic target. Hence, synthetic and biophysic
Autor:
Loreen Hericks, Nicolo Tonali, Verónica I. Dodero, Sandrine Ongeri, Julia Kaffy, Norbert Sewald
Publikováno v:
Chembiochem
Misfolding and aggregation of amyloid β1–42 peptide (Aβ1–42) play a central role in the pathogenesis of Alzheimer's disease (AD). Targeting the highly cytotoxic oligomeric species formed during the early stages of the aggregation process repres
Autor:
Verónica I. Dodero, Jannik Paulus, Heiko Ihmels, Norbert Sewald, Jochen Mattay, Sabrina Müller
Publikováno v:
Beilstein Journal of Organic Chemistry, Vol 16, Iss 1, Pp 60-70 (2020)
Beilstein Journal of Organic Chemistry
Beilstein Journal of Organic Chemistry
Azobenzenes are photoswitchable molecules capable of generating significant structural changes upon E-to-Z photoisomerization in peptides or small molecules, thereby controlling geometry and functionality. E-to-Z photoisomerization usually is achieve
Autor:
Nicolo Tonali, Karen M Lammers, Andreas Hütten, Maria Georgina Herrera, Verónica I. Dodero, Philipp W Dörfler, Marion Gras, Inga Ennen, Francesco Nicoletti, Yvonne Hannappel, Thomas Hellweg
Publikováno v:
Molecular nutritionfood research. 65(16)
SCOPE: Proteolysis-resistant gliadin peptides are intensely investigated in biomedical research related to Celiac Disease and gluten-related disorders. Herein, the first integrated supramolecular investigation of pepsin-digested gliadin peptides, p-g
Autor:
Martin A Lauxmann, Verónica I. Dodero, Karen M. Lammers, Diego S. Vazquez, Pia R. Neubauer, Hanna Marie Schilbert
Zonulin is a physiological modulator of intercellular tight junctions, which upregulation is involved in several diseases like celiac disease (CeD). The polyQ gliadin fragment binds to the CXCR3 chemokine receptor that activates zonulin upregulation,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1ee4b77078b557eda0f926786e6e1e9
https://doi.org/10.1002/bies.202100101
https://doi.org/10.1002/bies.202100101
Publikováno v:
Biophysical Reviews
In recent years, the evaluation of the structural properties of food has become of crucial importance in the understanding of food-related disorders. One of the most exciting systems is gliadin, a protein in wheat gluten, that plays a protagonist rol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9593711f0d6f861dab3f6e1fed24f219
https://pub.uni-bielefeld.de/record/2960861
https://pub.uni-bielefeld.de/record/2960861