Výsledky vyhledávání - "Mark J. Jedrzejas"

Structure, flexibility, and mechanism of the Bacillus stearothermophilus RecU holliday junction resolvase

Autor: Jie Li, Stephen J. Kelly, Mark J. Jedrzejas, Peter Setlow

Publikováno v: Proteins: Structure, Function, and Bioinformatics. 68:961-971

Here we report a high resolution structure of RecU-Holliday junction resolvase from Bacillus stearothermophilus. The functional unit of RecU is a homodimer that contains a “mushroom” like structure with a rigid cap and two highly flexible loops e

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08375428b4b7bea7054b8ce5841ff9e2
https://doi.org/10.1002/prot.21418

Zobrazit plný text záznamu

Genome-based identification and characterization of a putative mucin-binding protein from the surface of Streptococcus pneumoniae

Autor: James E. Littlejohn, Alexander H. Lucas, Michael Y. Galperin, Hannah Nayakanti, Daniel J. Rigden, Daniela Bumbaca, Mark J. Jedrzejas

Publikováno v: Proteins: Structure, Function, and Bioinformatics. 66:547-558

Streptococcus pneumoniae open reading frame SP1492 encodes a surface protein that contains a novel conserved domain similar to the repeated fragments of mucin-binding proteins from lactobacilli and lactococci. To investigate the functional role(s) of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7078b505d903e7076d12857899c86ff6
https://doi.org/10.1002/prot.21205

Zobrazit plný text záznamu

Unveiling molecular mechanisms of pneumococcal surface protein A interactions with antibodies and lactoferrin

Autor: Mark J. Jedrzejas

Publikováno v: Clinica Chimica Acta. 367:1-10

Background Streptococcus pneumoniae is a Gram-positive bacterium and a major human pathogen. The organism displays on its surface a variety of molecules that are involved in many essential processes including interactions with the tissues and molecul

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::37aaec905c06e19232bd9df2a60cc556
https://doi.org/10.1016/j.cca.2005.09.026

Zobrazit plný text záznamu

Design of new benzoxazole-2-thione-derived inhibitors of Streptococcus pneumoniae hyaluronan lyase: structure of a complex with a 2-phenylindole

Autor: Daniel J. Rigden, Mark J. Jedrzejas, R. Brandon Mewbourne, Masatoshi Nukui, Stephan Braun, Günther Bernhardt, Erwin von Angerer, Alexander Botzki, Stefan Dove, Armin Buschauer, Ejvis Lamani

Publikováno v: Glycobiology. 16:757-765

The bacterial hyaluronan lyases (Hyals) that degrade hyaluronan, an important component of the extracellular matrix, are involved in microbial spread. Inhibitors of these enzymes are essential in investigation of the role of hyaluronan and Hyal in ba

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abf3732c287dd8615e3f95e1c12f2581
https://doi.org/10.1093/glycob/cwj116

Zobrazit plný text záznamu

Structural studies and mechanism of Saccharomyces cerevisiae dolichyl-phosphate-mannose synthase: insights into the initial step of synthesis of dolichyl-phosphate-linked oligosaccharide chains in membranes of endoplasmic reticulum

Autor: Vladimir V. Veselovsky, Sergei D. Maltsev, Ejvis Lamani, Natalia Ya. Grigorieva, R. Brandon Mewbourne, Leonid L. Danilov, Vladimir N. Shibaev, Damona S. Fletcher, Mark J. Jedrzejas, W. Thomas Forsee, O. A. Pinsker, John S. Schutzbach, Antonina V. Lozanova, Jun Xing, Herbert C. Cheung

Publikováno v: Glycobiology. 16:666-678

Dolichyl-phosphate-mannose (Dol-P-Man) synthase catalyzes the reversible formation of a key intermediate that is involved as a mannosyl donor in at least three different pathways for the synthesis of glycoconjugates important for eukaryotic developme

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18b6cf571389c316aa31248e917f9080
https://doi.org/10.1093/glycob/cwj104

Zobrazit plný text záznamu

Sequence Analysis and Characterization of a Novel Fibronectin-Binding Repeat Domain from the Surface ofStreptococcus pneumoniae

Autor: Mark J. Jedrzejas, Hannah Nayakanti, Daniel J. Rigden, Michael Y. Galperin, Daniela Bumbaca, James E. Littlejohn

Publikováno v: OMICS: A Journal of Integrative Biology. 8:341-356

Streptococcus pneumoniae open reading frame SP0082 encodes a surface protein that contains four copies of a novel conserved repeat domain that bears no significant sequence similarity to proteins of known function. Homologous sequences from other str

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16fe60c8b1dbbdcc25d3bf3d232477f4
https://doi.org/10.1089/omi.2004.8.341

Zobrazit plný text záznamu

l-Ascorbic Acid 6-Hexadecanoate, a Potent Hyaluronidase Inhibitor

Autor: Stephan Braun, Sunnhild Salmen, Alexander Botzki, Stefan Dove, Mark J. Jedrzejas, Daniel J. Rigden, Julia Hoechstetter, Günther Bernhardt, Armin Buschauer, Masatoshi Nukui

Publikováno v: Journal of Biological Chemistry. 279:45990-45997

Hyaluronidases are enzymes that degrade hyaluronan, an important component of the extracellular matrix. The mammalian hyaluronidases are considered to be involved in many (patho)physiological processes like fertilization, tumor growth, and metastasis

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::41d05ea6ce443377002db167b88b7b2a
https://doi.org/10.1074/jbc.m406146200

Zobrazit plný text záznamu

Structures of Streptococcus pneumoniae Hyaluronate Lyase in Complex with Chondroitin and Chondroitin Sulfate Disaccharides

Autor: Daniel J. Rigden, Mark J. Jedrzejas

Publikováno v: Journal of Biological Chemistry. 278:50596-50606

Streptococcus pneumoniae hyaluronate lyase is a surface enzyme of this Gram-positive bacterium. The enzyme degrades hyaluronan and chondroitin/chondroitin sulfates by cleaving the β1,4-glycosidic linkage between the glycan units of these polymeric s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b1355af7d9041ff946c4a705ecfe0ab3
https://doi.org/10.1074/jbc.m307596200

Zobrazit plný text záznamu

Amidase domains from bacterial and phage autolysins define a family of γ-d,l-glutamate-specific amidohydrolases

Autor: Daniel J. Rigden, Michael Y. Galperin, Mark J. Jedrzejas

Publikováno v: Trends in Biochemical Sciences. 28:230-234

Several phage-encoded peptidoglycan hydrolases have been found to share a conserved amidase domain with a variety of bacterial autolysins (N-acetylmuramoyl-L-alanine amidases), bacterial and eukaryotic glutathionylspermidine amidases, gamma-D-glutamy

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52b8c4aa5418376074c480cfb3d5e0b0
https://doi.org/10.1016/s0968-0004(03)00062-8

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání