Výsledky vyhledávání - "Jens Conradi"

Conjugates of Modified Cryptophycins and RGD-Peptides Enter Target Cells by Endocytosis

Autor: Benedikt Sammet, Christine Weiß, Jens Conradi, Soledad Royo Gracia, Markus Nahrwold, Norbert Sewald, Ralf Palmisano, Felix Mertink, Thomas Preuße, Tobias Bogner

Publikováno v: Journal of Medicinal Chemistry. 56:1853-1864

Tumor targeting anticancer drug conjugates that contain a tumor recognition motif (homing device) are of high current relevance. Cryptophycins, naturally occurring cytotoxic cyclo-depsipeptides, have been modified by total synthesis to provide analog

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f5ce4e4972c259e90b93e7603d8df39
https://doi.org/10.1021/jm301346z

Zobrazit plný text záznamu

Cyclic RGD peptides interfere with binding of the Helicobacter pylori protein CagL to integrins αVβ3 and α5β1

Autor: Felix Mertink, Jens Conradi, Sylwia Huber, Katharina Gaus, Ulf Strijowski, Steffen Backert, Norbert Sewald, Soledad Royo Gracia

Publikováno v: Amino Acids. 43:219-232

The human pathogen Helicobacter pylori that may cause different gastric diseases exploits integrins for infection of gastric cells. The H. pylori protein CagL present on the outer region of the type IV secretion pilus contains an RGD sequence (-Arg-G

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2bb5902980c8805bbd710689b393665
https://doi.org/10.1007/s00726-011-1066-0

Zobrazit plný text záznamu

A Small Fibronectin-mimicking Protein from Bacteria Induces Cell Spreading and Focal Adhesion Formation

Autor: Nicole Tegtmeyer, Adam J. Smolka, Jens Conradi, Robin M. Delahay, Seiichiro Takahashi, Sabine Brandt, Norbert Sewald, Steffen Backert, Roland Hartig, Manfred Rohde

Publikováno v: Journal of Biological Chemistry. 285:23515-23526

Fibronectin, a 250-kDa eukaryotic extracellular matrix protein containing an RGD motif plays crucial roles in cell-cell communication, development, tissue homeostasis, and disease development. The highly complex fibrillar fibronectin meshwork orchest

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3839f7dffbc9d69ded9d2f5652f0a943
https://doi.org/10.1074/jbc.m109.096214

Zobrazit plný text záznamu

Structure of a three-dimensional domain-swapped dimer of the Helicobacter pylori type IV secretion system pilus protein CagL

Autor: Benjamin Schomburg, Jens Conradi, Steffen Backert, Hartmut H. Niemann, Norbert Sewald, Stephan Barden

A new crystal form of theHelicobacter pyloritype IV secretion system (T4SS) pilus protein CagL is described here. In contrast to two previously reported monomeric structures, CagL forms a three-dimensional domain-swapped dimer. CagL dimers can arise

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f459741d381d5b91a2d17e9bf7db00f
https://doi.org/10.1107/s1399004714003150

Zobrazit plný text záznamu

A helical RGD motif promoting cell adhesion: crystal structures of the Helicobacter pylori type IV secretion system pilus protein CagL

Autor: Nicole Tegtmeyer, Steffen Backert, Stefanie Lange, Hartmut H. Niemann, Jens Conradi, Norbert Sewald, Stephan Barden

Publikováno v: Structure 21(11), 1931-1941 (2013). doi:10.1016/j.str.2013.08.018

Structure 21(11), 1931 - 1941 (2013). doi:10.1016/j.str.2013.08.018
RGD tripeptide motifs frequently mediate ligand binding to integrins. The type IV secretion system (T4SS) protein CagL of the gastric pathogen Helicobacter pylori also contains

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e9477e3386722fa2b8ba255233ecfe4
https://pubmed.ncbi.nlm.nih.gov/24076404

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání