Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Sara Cohen-Krausz"'
Publikováno v:
Journal of Molecular Biology. 410:194-213
Spiroplasmas belong to the class Mollicutes, representing the minimal, free-living, and self-replicating forms of life. Spiroplasmas are helical wall-less bacteria and the only ones known to swim by means of a linear motor (rather than the near-unive
Autor:
Helen E. White, Elena V. Orlova, Shirley A. Müller, Thomas R. Jahn, Sheena E. Radford, Sara Cohen-Krausz, Julie L. Hodgkinson, Walraj S. Gosal, Helen R. Saibil
Publikováno v:
Journal of Molecular Biology
Amyloid fibrils are ordered polymers in which constituent polypeptides adopt a non-native fold. Despite their importance in degenerative human diseases, the overall structure of amyloid fibrils remains unknown. High-resolution studies of model peptid
Autor:
Sara Cohen-Krausz, Shlomo Trachtenberg
Publikováno v:
Journal of Molecular Biology. 375:1113-1124
Archaea, constituting a third domain of life between Eubacteria and Eukarya, characteristically inhabit extreme environments. They swim by rotating flagellar filaments that are phenomenologically and functionally similar to those of eubacteria. Howev
Publikováno v:
Journal of Molecular Biology. 368:319-327
Splicing of pre-mRNA takes place on a massive macromolecular machine in the nucleus of eukaryotic cells, the supraspliceosome. This particle is a multicomponent biological complex of RNA and proteins. It is composed of four sub-structures termed nati
Autor:
Sara Cohen-Krausz, Helen R. Saibil, MH Tattum, K Thumanu, Anthony R. Clarke, John Collinge, Azadeh Khalili-Shirazi, Elena V. Orlova, Graham S. Jackson, Christopher W. Wharton
Publikováno v:
Journal of Molecular Biology. 357:975-985
In prion diseases, the mammalian prion protein PrP is converted from a monomeric, mainly alpha-helical state into beta-rich amyloid fibrils. To examine the structure of the misfolded state, amyloid fibrils were grown from a beta form of recombinant m
Autor:
Sara Cohen-Krausz, Shlomo Trachtenberg
Publikováno v:
Journal of Molecular Biology. 331:1093-1108
Of the two known “complex” flagellar filaments, those of Pseudomonas are far more flexible than those of Rhizobium. Their diameter is larger and their outer three-start ridges and grooves are more prominent. Although the symmetry of both complex
Autor:
Sara Cohen-Krausz, Shlomo Trachtenberg
Publikováno v:
Molecular Microbiology. 48:1305-1316
Summary Bacterial flagella, the organelles of motility, are commonly divided into two classes: ‘plain’ and ‘complex’. The complex filaments are pairwise, helically perturbed forms of the plain filaments and have been reported to occur only in
Autor:
Sara Cohen-Krausz, Shlomo Trachtenberg
Publikováno v:
Journal of Molecular Biology. 321:383-395
Although the phenomenology and mechanics of swimming are very similar in eubacteria and archaeabacteria (e.g. reversible rotation, helical polymorphism of the filament and formation of bundles), the dynamic flagellar filaments seem completely unrelat
Autor:
Sara Cohen-Krausz, Helen R. Saibil
Publikováno v:
Protein Misfolding, Aggregation, and Conformational Diseases ISBN: 9780387259185
Amyloid fibrils are insoluble aggregates that result from the self-assembly of partially unfolded proteins. Regardless of the native structure of the precursor proteins, the predominant secondary structure in the fibrillar form is β-sheet. Proteins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::da246bbad2e1197db935ba735960e1c0
https://doi.org/10.1007/0-387-25919-8_15
https://doi.org/10.1007/0-387-25919-8_15
Autor:
Sara Cohen-Krausz, Shlomo Trachtenberg
Publikováno v:
Journal of molecular microbiology and biotechnology. 11(3-5)
Common prokaryotic motility modes are swimming by means of rotating internal or external flagellar filaments or gliding by means of retracting pili. The archaeabacterial flagellar filament differs significantly from the eubacterial flagellum: (1) Its