Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Itai Wekselman"'
Autor:
Tamar Auerbach-Nevo, David Baram, Anat Bashan, Matthew Belousoff, Elinor Breiner, Chen Davidovich, Giuseppe Cimicata, Zohar Eyal, Yehuda Halfon, Miri Krupkin, Donna Matzov, Markus Metz, Mruwat Rufayda, Moshe Peretz, Ophir Pick, Erez Pyetan, Haim Rozenberg, Moran Shalev-Benami, Itai Wekselman, Raz Zarivach, Ella Zimmerman, Nofar Assis, Joel Bloch, Hadar Israeli, Rinat Kalaora, Lisha Lim, Ofir Sade-Falk, Tal Shapira, Leena Taha-Salaime, Hua Tang, Ada Yonath
Publikováno v:
Antibiotics, Vol 5, Iss 3, p 24 (2016)
Most ribosomal antibiotics obstruct distinct ribosomal functions. In selected cases, in addition to paralyzing vital ribosomal tasks, some ribosomal antibiotics are involved in cellular regulation. Owing to the global rapid increase in the appearance
Externí odkaz:
https://doaj.org/article/38f282b678d544b195b47abf37f54af3
Autor:
Miri Krupkin, Z. Eyal, Haim Rozenberg, Ella Zimmerman, Anat Bashan, Donna Matzov, Ada Yonath, Itai Wekselman, Yael Diskin Posner
Publikováno v:
'Proceedings of the National Academy of Sciences of the USA ', vol: 113, pages: E6796-E6805 (2016)
Two structurally unique ribosomal antibiotics belonging to the orthosomycin family, avilamycin and evernimicin, possess activity against Enterococci, Staphylococci, and Streptococci, and other Gram-positive bacteria. Here, we describe the high-resolu
Autor:
Anat Bashan, Ella Zimmerman, Donna Matzov, Z. Eyal, Susanne Paukner, Miri Krupkin, Itai Wekselman, Haim Rozenberg, Ada Yonath
Publikováno v:
'Proceedings of the National Academy of Sciences of the USA ', vol: 112, pages: E5805-E5814 (2015)
Significance Clinical use of the currently available antibiotics is severely compromised by the increasing resistance to them, acquired by the natural bacterial capability to manipulate their genomes. Many existing antibiotics target the fundamental
Autor:
Mruwat Rufayda, Itai Wekselman, Moshe Peretz, Giuseppe Cimicata, Tal Shapira, Erez Pyetan, Donna Matzov, Ofir Sade-Falk, Y. Halfon, Chen Davidovich, Tamar Auerbach-Nevo, Matthew J. Belousoff, Elinor Breiner, Hua Tang, Haim Rozenberg, Ella Zimmerman, Anat Bashan, Rinat Kalaora, Lisha Lim, Moran Shalev-Benami, Miri Krupkin, Ophir Pick, Joël S. Bloch, David Baram, Raz Zarivach, Ada Yonath, Leena Taha-Salaime, Hadar Israeli, Nofar Assis, Markus Metz, Z. Eyal
Publikováno v:
Antibiotics, Vol 5, Iss 3, p 24 (2016)
Antibiotics
Antibiotics
Most ribosomal antibiotics obstruct distinct ribosomal functions. In selected cases, in addition to paralyzing vital ribosomal tasks, some ribosomal antibiotics are involved in cellular regulation. Owing to the global rapid increase in the appearance
Autor:
Chen Davidovich, Matthew J. Belousoff, Haim Rozenberg, Janice M. Zengel, Itai Wekselman, Gilgi Friedlander, Miri Krupkin, Ella Zimmerman, Anat Bashan, Hanne Ingmer, Lasse Lindahl, Jette Kjeldgaard, Ada Yonath, Donna Matzov
Publikováno v:
Structure (London, England : 1993). 25(8)
Summary Erythromycin is a clinically useful antibiotic that binds to an rRNA pocket in the ribosomal exit tunnel. Commonly, resistance to erythromycin is acquired by alterations of rRNA nucleotides that interact with the drug. Mutations in the β hai
Autor:
Ada Yonath, Chen Davidovich, Anat Bashan, Ella Zimmerman, Matthew J. Belousoff, Tal Shapira, Miri Krupkin, Itai Wekselman
Publikováno v:
Israel Journal of Chemistry. 50:29-35
The ribosome is a ribozyme whose active site, the peptidyl transferase center (PTC), is situated within a highly conserved universal symmetrical region that connects all ri- bosomal functional centers involved in amino acid polymeri- zation. The link
Autor:
Ella Zimmerman, Leena Taha, Ofir Sade-Falk, Lin Rozenszajn, Manfred S. Weiss, Ada Yonath, Tal Shapira, Anat Bashan, Yaron Caspi, Matthew J. Belousoff, Chen Davidovich, Itai Wekselman
Publikováno v:
Biochemical Society transactions. 38(2)
Structural analysis, supported by biochemical, mutagenesis and computational evidence, indicates that the peptidyltransferase centre of the contemporary ribosome is a universal symmetrical pocket composed solely of rRNA. This pocket seems to be a rel
Autor:
Haruyasu Kinashi, Alexander S. Mankin, Inbal Mermershtain, Ella Zimmerman, Kenji Arakawa, Liqun Xiong, Tamar Auerbach, Anat Bashan, Itai Wekselman, Matthew J. Belousoff, Dorota Klepacki, Chen Davidovich, Ada Yonath
Crystallographic analysis revealed that the 17-member polyketide antibiotic lankacidin produced by Streptomyces rochei binds at the peptidyl transferase center of the eubacterial large ribosomal subunit. Biochemical and functional studies verified th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e314d46431d3a624e0d9ec4e95c4ed4
https://europepmc.org/articles/PMC2804743/
https://europepmc.org/articles/PMC2804743/
Autor:
Haim Rozenberg, Ilana Agmon, Ella Zimmerman, Rita Berisio, Itai Wekselman, Anat Bashan, Ada Yonath, Chen Davidovich
Publikováno v:
Journal of peptide science
15 (2009): 122–130.
info:cnr-pdr/source/autori:Wekselman, Itai; Davidovich, Chen; Agmon, Ilana; Zimmerman, Ella; Rozenberg, Haim; Bashan, Anat; Berisio, Rita; Yonath, Ada/titolo:Ribosome's mode of function: myths, facts and recent results/doi:/rivista:Journal of peptide science (Print)/anno:2009/pagina_da:122/pagina_a:130/intervallo_pagine:122–130/volume:15
15 (2009): 122–130.
info:cnr-pdr/source/autori:Wekselman, Itai; Davidovich, Chen; Agmon, Ilana; Zimmerman, Ella; Rozenberg, Haim; Bashan, Anat; Berisio, Rita; Yonath, Ada/titolo:Ribosome's mode of function: myths, facts and recent results/doi:/rivista:Journal of peptide science (Print)/anno:2009/pagina_da:122/pagina_a:130/intervallo_pagine:122–130/volume:15
Ribosomes translate the genetic code into proteins in all living cells with extremely high efficiency, owing to their inherent flexibility and to their spectacular architecture. During the last 6 decades, extensive effort has been made to elucidate t
Autor:
Chen Davidovich, Anat Bashan, Itai Wekselman, Tal Shapira, Ella Zimmerman, Ada Yonath, Matthew J. Belousoff, Miri Krupkin
Publikováno v:
Israel Journal of Chemistry. 50:1-1