نتایج جستجو برای: outer membrane proteins omp

تعداد نتایج: 884310  

Journal: :Antimicrobial agents and chemotherapy 2005
Maria del Mar Tomás Alejandro Beceiro Astrid Pérez David Velasco Rita Moure Rosa Villanueva Jesús Martínez-Beltrán Germán Bou

We investigated a multiresistant strain of Acinetobacter baumannii isolated in our hospital. Analysis of the N-terminal peptide sequence of the outer membrane proteins (OMPs) purified from the strain allowed us to clone and sequence the nucleotides of the gene encoding the 33- to 36-kDa OMP associated with carbapenem resistance in A. baumannii.

Journal: :eLife 2021

In Proteobacteria, integral outer membrane proteins (OMPs) are crucial for the maintenance of envelope permeability barrier to some antibiotics and detergents. Enterobacteria, stress caused by unfolded OMPs activates sigmaE (? E ) transcriptional response. ? upregulates OMP biogenesis factors, including ?-barrel assembly machinery (BAM) that catalyses folding. Here we report DolP (formerly YraP...

2016
Jim E. Horne Sheena E. Radford

Great strides into understanding protein folding have been made since the seminal work of Anfinsen over 40 years ago, but progress in the study of membrane protein folding has lagged behind that of their water soluble counterparts. Researchers in these fields continue to turn to more advanced techniques such as NMR, mass spectrometry, molecular dynamics (MD) and single molecule methods to inter...

Journal: :Infection and immunity 2002
Ahmet Unver Yasuko Rikihisa Roger W Stich Norio Ohashi Suleyman Felek

Sixteen of 22 omp-1 paralogs encoding 28-kDa-range immunodominant outer membrane proteins of Ehrlichia chaffeensis were transcribed in blood monocytes of dogs throughout a 56-day infection period. Only one paralog was transcribed by E. chaffeensis in three developmental stages of Amblyomma americanum ticks before or after E. chaffeensis transmission to naïve dogs.

Journal: :Circulation 2004
Jes S Lindholt Jette Støvring Lars Østergaard Sigitas Urbonavicius Eskild W Henneberg Bent Honoré Henrik Vorum

BACKGROUND Chlamydia pneumoniae (Cp) has been demonstrated in arteries and abdominal aortic aneurysms (AAAs). However, the validity of the methods used is questioned, and antibiotic treatment trials have thus far shown disappointing results. Nevertheless, antibodies against the Cp outer membrane proteins (OMPs) have been associated with progression of atherosclerosis and AAAs. The aim of this s...

Journal: :Infection and immunity 2005
Charles S Berenson Timothy F Murphy Catherine T Wrona Sanjay Sethi

Interactions of nontypeable Haemophilus influenzae (NTHI) with human macrophages contribute to the pathogenesis of NTHI-induced infection in humans. However, the immunologic mechanisms that initiate and perpetuate NTHI-mediated macrophage responses have not been well explored. Outer membrane protein (OMP) P6 is a conserved lipoprotein expressed by NTHI in vivo that possesses a Pam(3)Cys termina...

Journal: :Cell 2007
Nieng Yan Yigong Shi

In Gram-negative bacteria, envelope stress signals such as unfolded outer membrane proteins (OMP) activate the periplasmic protease DegS. This protease then triggers a cellular pathway to alleviate the stress. Now Sohn et al. (2007) show conclusively that inhibition of DegS is relieved allosterically by binding of the C-terminal sequences in unfolded OMPs to the PDZ domain of DegS.

Journal: :Cell 2007
Jungsan Sohn Robert A. Grant Robert T. Sauer

Regulated intramembrane proteolysis is a method for transducing signals between cellular compartments. When protein folding is compromised in the periplasm of E. coli, the C termini of outer-membrane proteins (OMPs) bind to the PDZ domains of the trimeric DegS protease and activate cleavage of RseA, a transmembrane transcriptional regulator. We show here that DegS is an allosteric enzyme. OMP b...

2012
Zhi-Xin Lyu Qiang Shao Yi Qin Gao Xin Sheng Zhao

The transportation of membrane proteins through the aqueous subcellular space is an important and challenging process. Its molecular mechanism and the associated structural change are poorly understood. Periplasmic chaperones, such as Skp in Escherichia coli, play key roles in the transportation and protection of outer membrane proteins (OMPs) in Gram-negative bacteria. The molecular mechanism ...

Journal: :Frontiers in bioscience : a journal and virtual library 2004
Stanislav D Zakharov William A Cramer

Colicins and phages parasitize outer membrane receptors whose physiological purpose is the transport of metabolites, metals, vitamins, and sugars. From mutagenesis studies, it is known that several colicins require the function of two outer membrane protein (Omp) receptors for cytotoxicity. A formidable list of problems associated with an understanding of a two receptor mechanism for colicin tr...

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