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Wyszukujesz frazę "protein analysis" wg kryterium: Temat


Wyświetlanie 1-2 z 2
Tytuł:
Structural analyses of Shigella invasion proteins reveals non-conserved; intrinsically unstructured regions
Autorzy:
Chakrabarti, S.
Ganguli, S.
Powiązania:
https://bibliotekanauki.pl/articles/11240.pdf
Data publikacji:
2013
Wydawca:
Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
Tematy:
structural analysis
Shigella
invasion protein
intrinsically unstructured region
bacterial pathogen
diarrhea
pathogenesis
Opis:
Shigella is one of the most common bacterial pathogens that are isolated from patients with diarrhea. Various attempts are being made worldwide with encouraging observations; still the emergence of multidrug-resistant Shigella strains and a continuous high disease incidence imply that shigellosis is an unsolved global health problem which can probably be solved only by developing a proper vaccine and a vaccine regime for the disease. The need of the hour is to foster the development of an effective vaccine which should not only serve to improve hygiene but also should be able to curb infections by the pathogen. This goal can only be achieved by gaining proper detailed knowledge underlying Shigella pathogenesis. The analyses of the Shigella invasion proteins which have been long been targeted to be potential candidate vaccines remains an open ended problem and forms the core of this present computational study which identifies the fact that long regions in the structure of the proteins are disordered having no distinct structural conformation; multiple alignments however, did not show any conserved stretches in the disordered regions. The results probably explain the ability of these proteins to interact with multiple cellular proteins and perform a diverse array of functions leading to successful pathogenesis.
Źródło:
International Letters of Natural Sciences; 2013, 05
2300-9675
Pojawia się w:
International Letters of Natural Sciences
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Structural analyses of AC4 protein of Sri Lankan cassava mosaic virus
Autorzy:
Gupta, S.
Ganguli, S.
Basu, P.
Datta, A.
Powiązania:
https://bibliotekanauki.pl/articles/11568.pdf
Data publikacji:
2015
Wydawca:
Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
Tematy:
structural analysis
AC4 protein
cassava mosaic virus
RNA silencing
viral infection
viral suppressor
geminivirus
post transcriptional gene silencing
Opis:
RNA silencing is one of the important phenomenon in plant defense mechanism, it actively protect host plants against viral infections. Existing viruses must have developed counter defense strategies to survive this arms race. Such counter defense strategy is the viral silencing suppressor (VSRs) which have been reported to directly interfere with the various steps leading to the interference of viral RNAs. Most identified VSRs are multifunctional, besides being RNA-silencing suppressors, they often perform essential roles by functioning as coat proteins, helper components for viral transmission, replicases and movement proteins, proteases or transcriptional regulators. One such identified VSR is AC4 of Sri Lankan cassava mosaic virus strain. Trivial knowledge about the structure –function relationship of this VSR leads to this work, where we focus on the structure generation by modelling to identify the mode of interactions with the various effector molecules of the silencing pathways. Structural analyses have been performed to screen interacting residues. Results indicate conserved structural features which signify propensity of functional interactions and further shows that this VSR can be a potent tool for the analysis of RNA silencing mechanisms and the relationships between different silencing pathways and VSRs.
Źródło:
International Letters of Natural Sciences; 2015, 06
2300-9675
Pojawia się w:
International Letters of Natural Sciences
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-2 z 2

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