نتایج جستجو برای: oprd porin protein

تعداد نتایج: 1235787  

2009
Jie Liang Jingbo Wang Guanhong Luo Yanglin Pan Xin Wang Changcun Guo Dexin Zhang Fang Yin Xiaoyin Zhang Jie Liu Jianhong Wang Xuegang Guo Kaichun Wu Daiming Fan

Approximately 10-15% of the human prion disease is inherited and one of the important genetic mutations occurs in the octapeptide repeat region of prion protein gene. One of the variants, one octapeptide repeat deletion (1-OPRD), existed in several gastric cancer cell lines and its mutation frequency was higher in gastric cancer cases. However, the biological functions of it remain unknown. Wil...

Journal: :Journal of bacteriology 1983
J Sutcliffe R Blumenthal A Walter J Foulds

Protein K is an outer membrane protein found in pathogenic encapsulated strains of Escherichia coli. We present evidence here that protein K is structurally and functionally related to the E. coli K-12 porin proteins (OmpF, OmpC, and PhoE). Protein K was found to cross-react with antibody to OmpF protein and to share 8 out of 17 peptides in common with the OmpF protein. Strains that are OmpC po...

ژورنال: :مجله دانشگاه علوم پزشکی فسا 0
بدرالسادات متقی badrosadat motaghi department of microbiology, college of microbiology, shiraz science and research branch, islamic azad university, shiraz, iran.گروه میکروب شناسی، دانشکده میکروب شناسی، واحد علوم و تحقیقات شیراز، دانشگاه آزاد اسلامی، شیراز، ایران. سهراب نجفی پور sohrab najafipour department of microbiology, fasa medical school, fasa university of medical sciences, fasa. iran.گروه میکروبیولوژی، دانشکده پزشکی، دانشگاه علوم پزشکی فسا، فسا، ایران.

زمینه و هدف: سودوموناس آئروژینوزا شایع ترین عامل عفونت های بیمارستانی در بیماران بستری می باشد. پروتئین oprd یک پورین اختصاصی است که ورود آنتی بیوتیک های کارباپنم به درون باکتری را تنظیم می کند. فقدان پروتئین oprd سبب مقاومت سودوموناس آئروژینوزا به کارباپنم ها می گردد. در این مطالعه، حضور ژن outer membrane protein d(oprd) در باکتری های سودوموناس آئروژینوزا جدا شده از بیماران بستری در بیمارستان ...

Journal: :The Journal of Cell Biology 2001
Thomas Krimmer Doron Rapaport Michael T. Ryan Chris Meisinger C. Kenneth Kassenbrock Elizabeth Blachly-Dyson Michael Forte Michael G. Douglas Walter Neupert Frank E. Nargang Nikolaus Pfanner

Porin, also termed the voltage-dependent anion channel, is the most abundant protein of the mitochondrial outer membrane. The process of import and assembly of the protein is known to be dependent on the surface receptor Tom20, but the requirement for other mitochondrial proteins remains controversial. We have used mitochondria from Neurospora crassa and Saccharomyces cerevisiae to analyze the ...

Journal: :The Journal of biological chemistry 1985
R Pfaller H Freitag M A Harmey R Benz W Neupert

Mitochondrial porin, the outer membrane pore-forming protein, was isolated in the presence of detergents and converted into a water-soluble form. This water-soluble porin existed under nondenaturing conditions as a mixture of dimers and oligomers. The proportion of dimers increased with decreasing porin concentration during conversion. Water-soluble porin inserted spontaneously into artificial ...

Journal: :Antimicrobial agents and chemotherapy 2014
Dinesh M Fernando Wayne Xu Peter C Loewen George G Zhanel Ayush Kumar

In order to determine if triclosan can select for mutants of Acinetobacter baumannii ATCC 17978 that display reduced susceptibilities to antibiotics, we isolated a triclosan-resistant mutant, A. baumannii AB042, by serial passaging of A. baumannii ATCC 17978 in growth medium supplemented with triclosan. The antimicrobial susceptibility of AB042 was analyzed by the 2-fold serial dilution method....

Journal: :The Journal of biological chemistry 2001
U Schlattner M Dolder T Wallimann M Tokarska-Schlattner

Mitochondrial creatine kinase (MtCK) co-localizes with mitochondrial porin (voltage-dependent anion channel) and adenine nucleotide translocator in mitochondrial contact sites. A specific, direct protein-protein interaction between MtCK and mitochondrial porin was demonstrated using surface plasmon resonance spectroscopy. This interaction was independent of the immobilized binding partner (pori...

Journal: :Journal of bacteriology 1999
T Köhler S F Epp L K Curty J C Pechère

We investigated the regulation of the MexEF-OprN multidrug efflux system of Pseudomonas aeruginosa, which is overexpressed in nfxC-type mutants and confers resistance to quinolones, chloramphenicol and trimethoprim. Sequencing of the DNA region upstream of the mexEF-oprN operon revealed the presence of an open reading frame (ORF) of 304 amino acids encoding a LysR-type transcriptional activator...

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