Zobrazeno 1 - 10
of 292
pro vyhledávání: '"Eckhart, W"'
Autor:
Eckhart, W.
Publikováno v:
Proceedings of the Royal Society of London. Series B, Biological Sciences, 1971 Feb . 177(1046), 59-63.
Externí odkaz:
https://www.jstor.org/stable/76062
Autor:
Peters, Eckhart W.
Publikováno v:
Erdkunde, 1977 Mar 01. 31(1), 52-64.
Externí odkaz:
https://www.jstor.org/stable/25641831
Publikováno v:
Genome Research
To analyze gene regulatory networks, the sequence-dependent DNA/RNA binding affinities of proteins and noncoding RNAs are crucial. Often, these are deduced from sets of sequences enriched in factor binding sites. Two classes of computational approach
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d051f2979638feb6f54034a797252778
https://doi.org/10.1101/gr.139881.112
https://doi.org/10.1101/gr.139881.112
Publikováno v:
Angewandte Chemie. 118:6733-6736
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c9ac50991c2516b75e47c569df8b520
https://doi.org/10.1002/ange.200601579
https://doi.org/10.1002/ange.200601579
Autor:
Eckhart W. Guthöhrlein, Wolfgang Voelter, Stanka Stoeva, Nicolay Genov, Wojciech Rypniewski, Krassimira Idakieva, Markus Perbandt, Christian Betzel
Publikováno v:
Biochemistry. 42:6341-6346
Structure-function relationships in a molluscan hemocyanin have been investigated by determining the crystal structure of the Rapana thomasiana (gastropod) hemocyanin functional unit RtH2e in deoxygenated form at 3.38 A resolution. This is the first
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80f4f5f2ce40042c068639711c1d618e
https://doi.org/10.1021/bi020672x
https://doi.org/10.1021/bi020672x
Autor:
Eckhart W. Guthöhrlein, Wolfgang Voelter, Roland Wacker, Christian Betzel, Al'bert M. Mikhailov, Stanka Stoeva, R. Krauspenhaar, Mirita Franz
Publikováno v:
Archives of Biochemistry and Biophysics. 392:23-31
From mistletoe Viscum album L. extracts three chitin-binding lectin isoforms, cbML1, cbML2, and cbML3, were isolated and their primary structure determined. All three cbML isoforms are composed of two protein chains of 48 or 49 amino acid residues, l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03ff66039195e650bd5cbe78f6bb5f93
https://doi.org/10.1006/abbi.2001.2429
https://doi.org/10.1006/abbi.2001.2429
While numerous examples of P-peptides-exclusively composed of (beta-amino acids-have been investigated during the past decade, there are only few reports on the conformational preference of a single (beta-amino acid when incorporated into a cyclopept
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02e26fddd5f9d6f46c1473d643a652a2
https://doi.org/10.1002/bip.20859
https://doi.org/10.1002/bip.20859
Publikováno v:
Angewandte Chemie (International ed. in English). 45(39)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24c7e28a6ecd23772ec02c6725e575c0
https://pubmed.ncbi.nlm.nih.gov/16960907
https://pubmed.ncbi.nlm.nih.gov/16960907
Autor:
Guthöhrlein, Eckhart W.
Conformational analysis by NMR spectroscopy and molecular dynamics simulations (MD) is one of the most important techniques for high resolution structure analysis in chemistry and biochemistry. In the frame of this thesis, a torsion angle based clust
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______2294::bd300c22c4792ffc2551613e5a90d160
https://pub.uni-bielefeld.de/record/2305368
https://pub.uni-bielefeld.de/record/2305368
Autor:
Dunja Zimmermann, Lutz Wobbe, Carolin Heggemann, Miroslav Malesevic, Norbert Sewald, Katherina Sewald, Eckhart W. Guthöhrlein
Publikováno v:
Chembiochem : a European journal of chemical biology. 6(2)
Breaking up is easy. Integrin a5b1 is a cell-surface receptor involved in many physiological and pathological processes. Small cyclic peptides can influence the interaction between this receptor and its natural ligand, fibronectin. The peptide shown,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::521d85d99585cb7dd1b6a343ce8ef153
https://pubmed.ncbi.nlm.nih.gov/15645521
https://pubmed.ncbi.nlm.nih.gov/15645521