scholarly journals Dielectric saturation of water in a membrane protein channel

2009 ◽  
Vol 11 (2) ◽  
pp. 358-365 ◽  
Author(s):  
Marcel Aguilella-Arzo ◽  
Andreu Andrio ◽  
Vicente M. Aguilella ◽  
Antonio Alcaraz
Keyword(s):  
Membrane Protein ◽  
Protein Channel ◽  
Dielectric Saturation

scholarly journals Opening of the Outer Membrane Protein Channel in Tripartite Efflux Pumps Is Induced by Interaction with the Membrane Fusion Partner

2010 ◽  
Vol 286 (7) ◽  
pp. 5484-5493 ◽  
Author(s):  
Thamarai K. Janganan ◽  
Li Zhang ◽  
Vassiliy N. Bavro ◽  
Dijana Matak-Vinkovic ◽  
Nelson P. Barrera ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Membrane Fusion ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Efflux Pumps ◽  
Fusion Partner ◽  
Protein Channel

scholarly journals On the different sources of cooperativity in pH titrating sites of a membrane protein channel

2016 ◽  
Vol 39 (3) ◽  
Author(s):  
Antonio Alcaraz ◽  
María Queralt-Martín
Keyword(s):  
Membrane Protein ◽  
Protein Channel ◽  
Different Sources

scholarly journals A Single-Molecule Interaction Spectrum for Non-Covalent Interaction Inside Membrane Protein Channel

2019 ◽  
Vol 116 (3) ◽  
pp. 468a
Author(s):  
Meng-Yin Li ◽  
Yi-Lun Ying ◽  
Wei Tong ◽  
Yong-Jing Wan ◽  
Yi-Tao Long
Keyword(s):  
Membrane Protein ◽  
Single Molecule ◽  
Covalent Interaction ◽  
Protein Channel ◽  
Molecule Interaction

Modelling of calcium ion (Ca+2) conductance in nerve membrane protein channel as memristive circuit element

2011 ◽  
Vol 47 (25) ◽  
pp. 1361-1363 ◽  
Author(s):  
S. Alam ◽  
S.M. Rezaul Hasan
Keyword(s):  
Membrane Protein ◽  
Calcium Ion ◽  
Nerve Membrane ◽  
Circuit Element ◽  
Protein Channel ◽  
Memristive Circuit

scholarly journals The TolC-Like Protein of Neisseria meningitidis Is Required for Extracellular Production of the Repeats-in-Toxin Toxin FrpC but Not for Resistance to Antimicrobials Recognized by the Mtr Efflux Pump System

2007 ◽  
Vol 75 (12) ◽  
pp. 6008-6012 ◽  
Author(s):  
Nazia Kamal ◽  
Corinne Rouquette-Loughlin ◽  
William M. Shafer
Keyword(s):  
Membrane Protein ◽  
Neisseria Meningitidis ◽  
Outer Membrane Protein ◽  
Efflux Pump ◽  
Open Reading Frames ◽  
Extracellular Production ◽  
Pump System ◽  
Tolc Protein ◽  
Protein Channel ◽  
Reading Frames

ABSTRACT A 2.9-kilobase pair locus in Neisseria meningitidis was identified as containing transcriptionally linked open reading frames encoding TolC- and HlyD-like proteins. Although the meningococcal TolC protein was required for extracellular production of the repeats-in-toxin (RTX) FrpC toxin, it could not functionally replace the MtrE protein as the outer membrane protein channel for drug export by the MtrC-MtrD-MtrE efflux pump.

scholarly journals Water diffusion through a membrane protein channel: A first passage time approach

2007 ◽  
Vol 127 (8) ◽  
pp. 085101 ◽  
Author(s):  
Vincent J. van Hijkoop ◽  
Anton J. Dammers ◽  
Kourosh Malek ◽  
Marc-Olivier Coppens
Keyword(s):  
Membrane Protein ◽  
First Passage Time ◽  
Passage Time ◽  
Water Diffusion ◽  
First Passage ◽  
Protein Channel

scholarly journals Proton Transport in a Membrane Protein Channel: Two-Dimensional Infrared Spectrum Modeling

2012 ◽  
Vol 116 (22) ◽  
pp. 6336-6345 ◽  
Author(s):  
Chungwen Liang ◽  
Jasper Knoester ◽  
Thomas L. C. Jansen
Keyword(s):  
Membrane Protein ◽  
Infrared Spectrum ◽  
Proton Transport ◽  
Two Dimensional ◽  
Protein Channel ◽  
Spectrum Modeling

scholarly journals Lacking of efflux mechanism in clinical isolate of Pseudomonas aerupinosa highly resistant to β-Lactams And imimnem

2003 ◽  
Vol 71 (2) ◽  
pp. 89-100
Author(s):  
Ashraf. Kadry
Keyword(s):  
Cystic Fibrosis ◽  
Pseudomonas Aeruginosa ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Clinical Isolate ◽  
Broad Spectrum ◽  
Resistance Mechanism ◽  
M Protein ◽  
Efflux Mechanism ◽  
Protein Channel

In this investigation, the isolate of Pseudomonas aeruginosa from cystic fibrosis was highly resistant to β-lactarns and β-lactamase inhibitors. The resistant determinants of clinical isolate to imipenem, ceftazidime, ceftriaxone and cefepime were conjugally non-transfer. The slow or non-enzymatically mediated breakdown of imipenem and other broad spectrum p-lactams suggest the resistance of P.aeruginosa isolate to these drugs might be attributed to either permeability or efflux. Impaired penetration of imipenem and other p-lactams through the membrane was detected by a diminished expression of outer membrane (OM) proteins of approximate weight of 46 and 39 Kdal, matched to Opr D and OprF, respectively. Efflux resistance mechanism for meropenem and p-lactams has been ruled out since the isolate failed to express outer membrane protein of about 50 Kdal, which is matched to Opr M protein channel. Thus, reduced permeability in the clinical isolate may be the main mechanism conferring resistance against p-lactarns including imipenem.

scholarly journals Dielectric Saturation of Water in a Protein Channel

2009 ◽  
Vol 96 (3) ◽  
pp. 603a
Author(s):  
Vicente M. Aguilella ◽  
Antonio Alcaraz ◽  
Andreu Andrio ◽  
Marcel Aguilella-Arzo
Keyword(s):  
Protein Channel ◽  
Dielectric Saturation
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