نتایج جستجو برای: moqatta’e in twenty nine sura

تعداد نتایج: 16989160  

پایان نامه :وزارت علوم، تحقیقات و فناوری - دانشگاه تربیت معلم تهران 1381

‏‎the purpose of the present study was to investigate the latent pattern underlying reading ability . some 272 male and female participants. english majors at the ba level , participated in the study. two valid tests were used in this study, the reading test developed exclusively for the purpose of this project and academic reading section of ielts. to investigate the possible latent underlying...

2013
Dante P. Ricci Jaclyn Schwalm Michelle Gonzales-Cope Thomas J. Silhavy

UNLABELLED SurA is a component of the periplasmic chaperone network that plays a central role in biogenesis of integral outer membrane β-barrel proteins (OMPs) in Escherichia coli. Although SurA contains two well-conserved proline isomerase (PPIase) domains, the contribution of these domains to SurA function is unclear. In the present work, we show that defects in OMP assembly caused by mutatio...

Journal: :Journal of bacteriology 2001
A E Rizzitello J R Harper T J Silhavy

The periplasm of Escherichia coli contains many proteins proposed to have redundant functions in protein folding. Using depletion analysis, we directly demonstrated that null mutations in skp and surA, as well as in degP and surA, result in synthetic phenotypes, suggesting that Skp, SurA, and DegP are functionally redundant. The Deltaskp surA::kan combination has a bacteriostatic effect and lea...

Journal: :Journal of bacteriology 2013
Meng Zhong Brent Ferrell Wei Lu Qian Chai Yinan Wei

SurA is the primary periplasmic molecular chaperone that facilitates the folding and assembling of outer membrane proteins (OMPs) in Gram-negative bacteria. Deletion of the surA gene in Escherichia coli leads to a decrease in outer membrane density and an increase in bacterial drug susceptibility. Here, we conducted mutational studies on SurA to identify residues that are critical for function....

Journal: :Journal of bacteriology 2016
Garner R Soltes Jaclyn Schwalm Dante P Ricci Thomas J Silhavy

UNLABELLED The periplasmic chaperone SurA is critical for the biogenesis of outer membrane proteins (OMPs) and, thus, the maintenance of membrane integrity in Escherichia coli. The activity of this modular chaperone has been attributed to a core chaperone module, with only minor importance assigned to the two SurA peptidyl-prolyl isomerase (PPIase) domains. In this work, we used synthetic pheno...

Journal: :Infection and immunity 2006
Sheryl S Justice Scott R Lauer Scott J Hultgren David A Hunstad

Escherichia coli is the most common cause of community-acquired urinary tract infection (UTI). During murine cystitis, uropathogenic E. coli (UPEC) utilizes type 1 pili to bind and invade superficial bladder epithelial cells. UPEC then replicates within to form intracellular bacterial communities (IBCs), a process whose genetic determinants are as yet undefined. In this study, we investigated t...

Journal: :Protein engineering, design & selection : PEDS 2014
Qian Chai Brent Ferrell Meng Zhong Xinyi Zhang Cui Ye Yinan Wei

SurA is a major periplasmic molecular chaperone in Escherichia coli and has been shown to assist the biogenesis of several outer membrane proteins. The C-terminal fragment of SurA folds into a short β-strand, which forms a small three-stranded anti-parallel β-sheet module with the N-terminal β-hairpin. We found that the length of the C-terminal fragment, rather than its exact amino acid composi...

Journal: :American Journal of Ophthalmology 1919

Journal: :PLoS ONE 2008
Kristin M. Watts David A. Hunstad

BACKGROUND SurA is a periplasmic peptidyl-prolyl isomerase (PPIase) and chaperone of Escherichia coli and other Gram-negative bacteria. In contrast to other PPIases, SurA appears to have a distinct role in chaperoning newly synthesized porins destined for insertion into the outer membrane. Previous studies have indicated that the chaperone activity of SurA rests in its "core module" (the N- plu...

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