Výsledky vyhledávání - "Henning N. Behnken"

Unusual N-type glycosylation of salivary prolactin-inducible protein (PIP): multiple LewisY epitopes generate highly-fucosylated glycan structures

Autor: Bernd Meyer, Alena Wiegandt, Henning N. Behnken

Publikováno v: Glycoconjugate Journal. 35:323-332

Prolactin-inducible protein (PIP) is a glycoprotein found in body secretions from exocrine glands like saliva and seminal plasma. Important biological functions of PIP concentrations have been demonstrated, e.g. in tumor diagnosis and progression. PI

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9b5e58d50dfd1b1fc1558786f59d4cc3
https://doi.org/10.1007/s10719-018-9826-7

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Biotransformation of Dimethenamid-P by the basidiomycete Irpex consors

Autor: Sebastian Schoof, Sabine Leonhardt, Andrea Weil, Heike Hausmann, Astrid Spielmeyer, Nicolai Herold, Holger Zorn, Henning N. Behnken, Adrian Imami, Reinhard Dötzer

Publikováno v: Chemosphere. 165:59-66

Twenty-nine basidiomycetes were screened in surface and liquid cultures for their capability to biotransform the chloroacetamide herbicide Dimethenamid-P (DMTA-P). The basidiomycete Irpex consors converted 70% of the herbicide (0.5 g L-1 DMTA-P) in l

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1cd25ba4a50cdc7c11e3bce884667419
https://doi.org/10.1016/j.chemosphere.2016.09.011

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Unusual N-type glycosylation of salivary prolactin-inducible protein (PIP): multiple Lewis

Autor: Alena, Wiegandt, Henning N, Behnken, Bernd, Meyer

Publikováno v: Glycoconjugate journal. 35(3)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d783d68656ab475b7771ba63c978a43f
https://pubmed.ncbi.nlm.nih.gov/29858715

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Elapid Snake Venom Analyses Show the Specificity of the Peptide Composition at the Level of Genera Naja and Notechis

Autor: Henning N. Behnken, Hartmut Schlüter, Dessislava Georgieva, Diana Hildebrand, Patrick Jack Spencer, Christian Betzel, Raghuvir K. Arni, Maria Trusch, Sönke Harder, Aisha Munawar, Marcel Kwiatkowski

Publikováno v: Toxins, Vol 6, Iss 3, Pp 850-868 (2014)
Web of Science
Repositório Institucional da UNESP
Universidade Estadual Paulista (UNESP)
instacron:UNESP
Toxins
Volume 6
Issue 3
Pages 850-868

Made available in DSpace on 2014-12-03T13:11:08Z (GMT). No. of bitstreams: 0 Previous issue date: 2014-03-01Bitstream added on 2014-12-03T13:22:45Z : No. of bitstreams: 1 WOS000335755700005.pdf: 1237419 bytes, checksum: 63efa3a070a9fc1de02aeccb01a674

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7960b401bf869fa5a25e49ad2c06bf84
http://www.mdpi.com/2072-6651/6/3/850

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Tumor-associated Neu5Ac-Tn and Neu5Gc-Tn antigens bind to C-type lectin CLEC10A (CD301, MGL)

Autor: Naghmeh Mortezai, Bernd Meyer, Friedrich Buck, Henning N. Behnken, Christoph Wagener, Peter Ludewig, Anna-Katharina Kurze

Publikováno v: Glycobiology; Vol 23

In human tumors, glycoproteins often exhibit abnormal glycosylation patterns, e.g. certain Lewis structures, TF antigen, Tn antigen and/or their sialylated forms, creating additional binding sites for glycoreceptors. In the present study, we have ana

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67e63a9d42931ed75fde13ea7978c420
https://doi.org/10.1093/glycob/cwt021

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Resolving the problem of chromatographic overlap by 3D cross correlation (3DCC) processing of LC, MS and NMR data for characterization of complex glycan mixtures

Autor: Tim Nagel, Henning N. Behnken, Miriam P. Koetzler, Meike Fellenberg, Bernd Meyer, Raffael Jirmann

Publikováno v: Analytical and Bioanalytical Chemistry. 404:1427-1437

Chromatographic overlap is a common problem in the analysis of complex mixtures. As a result, it is not possible to identify the components because each resulting NMR or MS spectrum contains multiple components. We introduce three-dimensional cross c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a780fdf02989c6205f29a157f20fefc3
https://doi.org/10.1007/s00216-012-6241-y

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Formation of the immunogenic α1,3-fucose epitope: Elucidation of substrate specificity and of enzyme mechanism of core fucosyltransferase A

Autor: Dirk Alpers, Henning N. Behnken, Bernd Meyer, Frank I. Bantleon, Edzard Spillner, Simon Blank, Miriam P. Kötzler

Publikováno v: Insect Biochemistry and Molecular Biology. 42:116-125

Glycans of glycoproteins are often associated with IgE mediated allergic immune responses. Hymenoptera venoms, e.g., carry α1,3-fucosyl residues linked to the proximal GlcNAc of glycoproteins. This epitope, formed selectively by α1,3-fucosyltransfe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e5af180b69c429d5da698ec8b1f551e
https://doi.org/10.1016/j.ibmb.2011.11.004

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Glycan analysis of Prostate Specific Antigen (PSA) directly from the intact glycoprotein by HR-ESI/TOF-MS

Autor: Bernd Meyer, Henning N. Behnken, Jan-Mirco Schulz, Alexandra Ruthenbeck

Publikováno v: Journal of proteome research. 13(2)

Glycans are important modulators of the biological function of proteins and are normally characterized from proteolytic glycopeptides or from (N-)glycans released enzymatically by glycosidase treatment or chemically by hydrazinolysis. We demonstrate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94d44c603c1a1e3573b61cb957885699
https://pubmed.ncbi.nlm.nih.gov/24393138

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Interlaboratory Study on Differential Analysis of Protein Glycosylation by Mass Spectrometry: The ABRF Glycoprotein Research Multi-Institutional Study 2012

Autor: Uwe Möginger, Carthene R. Bazemore-Walker, Lauren E. Ball, Benjamin F. Mann, Jan Mirco Schulz, Carina Sihlbom, David Horn, Eden P. Go, Jeffrey S. Rohrer, Lipika Basumallick, Gregory O. Staples, Manfred Wuhrer, Detlev Suckau, Jonas Nilsson, Wolfgang Jabs, Richard R. Drake, Deanna C. Hurum, Christian Neusüβ, Christopher W. Cairo, Bernd Meyer, Leena Valmu, F. Altmann, Petr Pompach, William R. Alley, Michael Blank, Nancy Leymarie, Yoshinao Wada, Adnan Halim, Mellisa Ly, Daniel Kolarich, Randy M. Whittal, Yetrib Hathout, Milos V. Novotny, Jennifer T. Aguilan, Rambod Daneshfar, Joseph Zaia, Svenja-Catharina Bunz, Paul J. Hensbergen, Morten Thaysen-Andersen, Kristy J. Brown, John F. Cipollo, Clemens Gruber, Yehia Mechref, Alexandra Ruthenbeck, Megan T. Watson, Anja Resemann, Yiying Zhu, Radoslav Goldman, Markus Windwarder, Chunxia Zou, Yanming An, Henning N. Behnken, Haixu Tang, Rosa Viner, Béla Reiz, Ulrike Schweiger-Hufnagel, Nicolle H. Packer, Heather Desaire, Paula J. Griffin, Kristina Marx, Miloslav Sanda, Ron Orlando, Göran Larson, Julius O. Nyalwidhe, Karen R. Jonscher, Mark E. McComb, Ehwang Song

Publikováno v: Molecular and Cellular Proteomics
Molecular and Cellular Proteomics, 12(10), 2935-2951

One of the principal goals of glycoprotein research is to correlate glycan structure and function. Such correlation is necessary in order for one to understand the mechanisms whereby glycoprotein structure elaborates the functions of myriad proteins.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a5a82d518e0571702f3d264e5c3079f
https://hdl.handle.net/1887/100353

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Glycosylation assists binding of HIV protein gp120 to human CD4 receptor

Autor: Dennis Wilhelm, Bernd Meyer, Henning N. Behnken

Publikováno v: Chembiochem : a European journal of chemical biology. 13(4)

The role of glycosylation of proteins on its binding affinity is not well understood. Even a monosaccharide (magenta) placed at a glycosylation site can significantly enhance binding of peptides to their receptor. If glycosylated, an HIV protein bind

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c31403c1de5e74eb02e97592408e2ff5
https://pubmed.ncbi.nlm.nih.gov/22266649

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