Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Richard H. Maier"'
Publikováno v:
BioTechniques, Vol 45, Iss 3, Pp 235-244 (2008)
The yeast two-hybrid (Y2H) system is a powerful method to identify protein-protein inter-actions (PPI) in vivo, requiring minimal prior information of the putative interactors. The time and effort required for each experiment can be significantly red
Externí odkaz:
https://doaj.org/article/1e3a66347f7a4577b37c0f26a63e3e08
Autor:
Jacques Schrenzel, Patrice Francois, Alexandra Dangel, Kamil Önder, Jan Pané-Farré, Carsten W. Müller, Christian Lindermayr, Jürgen Heesemann, Susanne Engelmann, Nikolaus Ackermann, Omar Abdel-Hadi, Richard H. Maier
Publikováno v:
FASEB Journal, Vol. 27, No 11 (2013) pp. 4476-88
Antimicrobial peptides are a promising complement to common antibiotics, development of resistance to which is a growing problem. Here we present a de novo-designed peptide, SP1-1 (RKKRLKLLKRLL-NH2), with antimicrobial activity against multiresistant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef84fac4c0311657dfdebf5f5d907586
https://doi.org/10.1096/fj.13-234575
https://doi.org/10.1096/fj.13-234575
Autor:
Helmut Hintner, Johann W. Bauer, Richard H. Maier, Raphaela Rid, Harald Hundsberger, Julia Herzog, Andreas Eger, Kamil Önder
Publikováno v:
ASSAY and Drug Development Technologies. 11:269-275
The yeast two-hybrid (Y2H) system is one of the most technically straightforward, effective, and widely used tools for the discovery of the binary peptide or protein interactions. However, its exceptional detection sensitivity poses a serious challen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5f8e6a6cb7a967c20ad3b9adaf69d36
https://doi.org/10.1089/adt.2012.496
https://doi.org/10.1089/adt.2012.496
Autor:
Johann W. Bauer, Omar Abdel-Hadi, Harald Hundsberger, Martin Wagner, Richard H. Maier, Kamil Önder, Raphaela Rid, Helmut Hintner
Publikováno v:
ASSAY and Drug Development Technologies. 11:52-57
Recombination-based cloning techniques have in recent times facilitated the establishment of genome-scale single-gene ORFeome repositories. Their further handling and downstream application in systematic fashion is, however, practically impeded becau
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4784660d1ad1bd204031b311e0b19acd
https://doi.org/10.1089/adt.2012.450
https://doi.org/10.1089/adt.2012.450
Publikováno v:
Methods. 58:376-384
Many functional proteomic experiments make use of high-throughput technologies such as mass spectrometry combined with two-dimensional polyacrylamide gel electrophoresis and the yeast two-hybrid (Y2H) system. Currently there are even automated versio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::49183b36a7945b561469005190574f03
https://doi.org/10.1016/j.ymeth.2012.09.001
https://doi.org/10.1016/j.ymeth.2012.09.001
Autor:
M. Haim, Helmut Hintner, Verena Wally, Johann W. Bauer, Andrea Trost, Herbert A. Reitsamer, Kamil Önder, P. Desch, Richard H. Maier
Publikováno v:
Mechanisms of Ageing and Development. 131:346-353
Keratin filaments form obligatory heterodimers consisting of one type I and one type II keratin that build the intermediate filaments. In keratinocytes, type II keratin 6 (K6) interacts with type I keratin 16 (K16). We previously showed that the inte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::036bd994c84f0922317c0c77fe652f03
https://doi.org/10.1016/j.mad.2010.04.002
https://doi.org/10.1016/j.mad.2010.04.002
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1061
The specific regions on proteins which are responsible for protein-protein interaction are called interacting domains, or epitopes in case of antigen-antibody binding. These domains are one feature to characterize proteins and are important in clinic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3e931c4f4a68301425a824dd0c734ded
https://pubmed.ncbi.nlm.nih.gov/23963940
https://pubmed.ncbi.nlm.nih.gov/23963940
Autor:
Frederick J. Monsma, Terry Roemer, Nicholas Murgolo, Paul Mann, Li Xiao, Brad Sherborne, Richard H. Maier, Christine Yang, Stacia Kargman, Amy M. Flattery, Hao Wang, Charles Gill, Todd A. Black, Tanja Schneider, Anna Müller, Sang Ho Lee, Christopher M. Tan, Xinwei She, Margarida Moreira dos Santos, Marc A. Labroli, Kamil Önder, Joanna Trzeciak, Mariana G. Pinho, Pedro M. Pereira, Carl J. Balibar, Jing Su, Jonathan Schneeweis
Publikováno v:
ACS Chemical Biology
Modern medicine is founded on the discovery of penicillin and subsequent small molecules that inhibit bacterial peptidoglycan (PG) and cell wall synthesis. However, the discovery of new chemically and mechanistically distinct classes of PG inhibitors
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::270ccb1657debdfccf3206afefee6e01
Publikováno v:
Methods in Molecular Biology ISBN: 9781627035880
The specific regions on proteins which are responsible for protein-protein interaction are called interacting domains, or epitopes in case of antigen-antibody binding. These domains are one feature to characterize proteins and are important in clinic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::79efd2a951ba4234151a799c33fcc9d3
https://doi.org/10.1007/978-1-62703-589-7_13
https://doi.org/10.1007/978-1-62703-589-7_13
Autor:
Kamil Önder, Johann W. Bauer, Christina J. Maier, Raphaela Rid, Helmut Hintner, Martin Laimer, Martin Wagner, Richard H. Maier
Publikováno v:
Molecular and cellular endocrinology. 361(1-2)
The vitamin D receptor (VDR), an evolutionarily conserved member of the nuclear receptor superfamily, links the metabolically activated vitamin D ligand, calcitriol, with its vitamin D-responsive target genes that are implicated in diverse physiologi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0fd7fe807523ad48a6e5942ce641014
https://pubmed.ncbi.nlm.nih.gov/22476084
https://pubmed.ncbi.nlm.nih.gov/22476084