نتایج جستجو برای: coat proteins

تعداد نتایج: 571601  

Journal: :Journal of proteome research 2013
Wishwas Abhyankar Abeer H Hossain André Djajasaputra Patima Permpoonpattana Alexander Ter Beek Henk L Dekker Simon M Cutting Stanley Brul Leo J de Koning Chris G de Koster

Bacillus cereus, responsible for food poisoning, and Clostridium difficile, the causative agent of Clostridium difficile-associated diarrhea (CDAD), are both spore-forming pathogens involved in food spoilage, food intoxication, and other infections in humans and animals. The proteinaceous coat and the exosporium layers from spores are important for their resistance and pathogenicity characteris...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2008
Lionel Foret Pierre Sens

The secretion of vesicles for intracellular transport often relies on the aggregation of specialized membrane-bound proteins into a coat able to curve cell membranes. The nucleation and growth of a protein coat is a kinetic process that competes with the energy-consuming turnover of coat components between the membrane and the cytosol. We propose a generic kinetic description of coat assembly a...

Journal: :The Journal of Cell Biology 1996
F Simpson N A Bright M A West L S Newman R B Darnell M S Robinson

Coat proteins are required for the budding of the transport vesicles that mediate membrane traffic pathways, but for many pathways such proteins pathways, but for many pathways such proteins have not yet been identified. We have raised antibodies against p47, a homologue of the medium chains of the adaptor complexes of clathrin-coated vesicles (Pevsner, J., W. Volknandt, B.R. Wong, and R.H. Sch...

Journal: :The Journal of Cell Biology 1994
Z Elazar L Orci J Ostermann M Amherdt G Tanigawa J E Rothman

The coat proteins required for budding COP-coated vesicles from Golgi membranes, coatomer and ADP-ribosylation factor (ARF) protein, are shown to be required to reconstitute the orderly process of transport between Golgi cisternae in which fusion of transport vesicles begins only after budding ends. When either coat protein is omitted, fusion is uncoupled from budding-donor and acceptor compart...

2012
Ilona Rissanen Alice Pawlowski Karl Harlos Jonathan M. Grimes David I. Stuart Jaana K. H. Bamford

Members of the diverse double-β-barrel lineage of viruses are identified by the conserved structure of their major coat protein. New members of this lineage have been discovered based on structural analysis and we are interested in identifying relatives that utilize unusual versions of the double-β-barrel fold. One candidate for such studies is P23-77, an icosahedral dsDNA bacteriophage that in...

Journal: :The Journal of biological chemistry 2012
G Pauline Padilla-Meier Eddie B Gilcrease Peter R Weigele Juliana R Cortines Molly Siegel Justin C Leavitt Carolyn M Teschke Sherwood R Casjens

Many viruses encode scaffolding and coat proteins that co-assemble to form procapsids, which are transient precursor structures leading to progeny virions. In bacteriophage P22, the association of scaffolding and coat proteins is mediated mainly by ionic interactions. The coat protein-binding domain of scaffolding protein is a helix turn helix structure near the C terminus with a high number of...

Journal: :Molecular microbiology 2007
Kristin N Parent Margaret M Suhanovsky Carolyn M Teschke

Eighteen single amino acid substitutions in phage P22 coat protein cause temperature-sensitive folding defects (tsf). Three intragenic global suppressor (su) substitutions (D163G, T166I and F170L), localized to a flexible loop, rescue the folding of several tsf coat proteins. Here we investigate the su substitutions in the absence of the original tsf substitutions. None of the su variant coat p...

Journal: :Seminars in cell & developmental biology 2011
Cortney G Angers Alexey J Merz

Vesicle trafficking is a highly regulated process that transports proteins and other cargoes through eukaryotic cells while maintaining cellular organization and compartmental identity. In order for cargo to reach the correct destination, each step of trafficking must impart specificity. During vesicle formation, this is achieved by coat proteins, which selectively incorporate cargo into the na...

Journal: :Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan 2012
Daisuke Imamura

The Gram-positive bacterium Bacillus subtilis forms spores when conditions are unsuitable for growth. The spores are encased in a multilayered shell that includes a cortex and a spore coat, and remain viable for long periods in the harsh environment. In the present article, recent progress in our understanding of the outer structure of B. subtilis spores is reviewed in the Japanese language. Al...

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