Zobrazeno 1 - 10
of 76
pro vyhledávání: '"Martin Sax"'
Autor:
Sultan Abdulaziz Alturki, Anja Sautmann, Rachel Yuting Fan, Daniel Lederman, Roberta Gatti, Joseph Martin Sax, Arian Hatefi, Christina Wood, Claudio J. Rojas, Ha Minh Nguyen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::702232ddf0552f1b5dadc37fa9deea76
https://doi.org/10.1596/978-1-4648-1798-4
https://doi.org/10.1596/978-1-4648-1798-4
Autor:
Jingxian Yang, Janine Zara Bowring, Janes Krusche, Esther Lehmann, Benjamin Svejdal Bejder, Stephanie Fulaz Silva, Martin Saxtorph Bojer, Tom Grunert, Andreas Peschel, Hanne Ingmer
Publikováno v:
Cell Reports, Vol 42, Iss 9, Pp 113154- (2023)
Summary: Bacteria use quorum sensing (QS) to coordinate group behavior in response to cell density, and some bacterial viruses (phages) also respond to QS. In Staphylococcus aureus, the agr-encoded QS system relies on accumulation of auto-inducing cy
Externí odkaz:
https://doaj.org/article/52c716498f3e4e238f31aedf7ad675e1
Autor:
Natalia S. Nemeria, Frank Jordan, Palaniappa Arjunan, Krishnamoorthy Chandrasekhar, William Furey, Martin Sax, Andrew Brunskill
Publikováno v:
Biochemistry. 43:2405-2411
Thiamin thiazolone diphosphate (ThTDP), a potent inhibitor of the E1 component from the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc), binds to the enzyme with greater affinity than does the cofactor thiamin diphosphate (ThDP). T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3bc23fbe5eeffe76522354b3ada03409
https://doi.org/10.1021/bi030200y
https://doi.org/10.1021/bi030200y
Autor:
Martin Sax, William Furey, Subramanyam Swaminathan, James J. Schmidt, Lavinia M. Wingert, Timothy C. Umland
Publikováno v:
Natural Structural Biology. 4:788-792
The 2.7 A structure of the tetanus neurotoxin receptor binding fragment Hc reveals a jelly-roll domain and a beta-trefoil domain. Hc retains the unique transport properties of the holotoxin and is capable of eliciting a protective immunological respo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5de07766db7d7cf95f8f06e0d5f93af1
https://doi.org/10.1038/nsb1097-788
https://doi.org/10.1038/nsb1097-788
Publikováno v:
Nature Structural Biology. 2:680-686
The three-dimensional structure of staphylococcal enterotoxin C2 has been determined at 2.7 A resolution by x-ray diffraction, while the structures of enterotoxins A and E have been modelled based on their sequence homology to other staphylococcal en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::229ebc18c4b88756c43a8850f033c493
https://doi.org/10.1038/nsb0895-680
https://doi.org/10.1038/nsb0895-680
Autor:
Toshiaki Taura, Michinobu Kato, Yoneichiro Muto, Shih-Chi Chang, C. S. Yoo, Omar W. Steward, J. Pletcher, Chong-Hwan Chang, C. Frederick Jury, Tadashi Tokii, Martin Sax
Publikováno v:
Bulletin of the Chemical Society of Japan. 64:3046-3058
The synthesis and characterization of three copper(II) triphenylacetate-pyridine complexes are reported along with their magnetic and spectral properties: [Cu2(O2CCPh3)4(py)2]·C6H6 (1), [Cu2(O2CCPh3)4(py)2] (2), and Cu(O2CCPh3)2·2py (3). Crystal st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cac6fe109a27f7d018898c764563ce78
https://doi.org/10.1246/bcsj.64.3046
https://doi.org/10.1246/bcsj.64.3046
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 54:273-275
Two crystal forms of recombinant tetanus neurotoxin C fragment have been obtained. The C fragment corresponds to the C-terminal 451 amino-acid residues of tetanus neurotoxin and is the subunit responsible for receptor binding by the toxin. Both forms
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a150a0286a41fbc1ac71cc59178ac399
https://doi.org/10.1107/s0907444997009025
https://doi.org/10.1107/s0907444997009025
Botulinum Neurotoxin type E was crystallized and an electron density map was analyzed at 3 alpha resolution. A new crystal form was also obtained, and may be helpful in improving the phasing. Co-crystallization experiments with gangliosides have also
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c12ac7f38c671621d31c83b2d78568ce
https://doi.org/10.21236/ada413858
https://doi.org/10.21236/ada413858
Autor:
Frank Jordan, Andrew Brunskill, Yan Yan, John R. Guest, Palaniappa Arjunan, William Furey, Martin Sax, Krishnamoorthy Chandrasekhar, Natalia S. Nemeria
Publikováno v:
Biochemistry. 41(16)
The crystal structure of the recombinant thiamin diphosphate-dependent E1 component from the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc) has been determined at a resolution of 1.85 A. The E. coli PDHc E1 component E1p is a homo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::beede157b7cd33b3ae92a30b7f6fb034
https://pubmed.ncbi.nlm.nih.gov/11955070
https://pubmed.ncbi.nlm.nih.gov/11955070