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Littérature scientifique sur le sujet « LptC protein »

Auteur : Grafiati

Publié le 9 mars 2023

Mis à jour le 31 juillet 2025

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Articles de revues sur le sujet "LptC protein"

Sperandeo, Paola, Fion K. Lau, Andrea Carpentieri, et al. "Functional Analysis of the Protein Machinery Required for Transport of Lipopolysaccharide to the Outer Membrane of Escherichia coli." Journal of Bacteriology 190, no. 13 (2008): 4460–69. http://dx.doi.org/10.1128/jb.00270-08.

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ABSTRACT Lipopolysaccharide (LPS) is an essential component of the outer membrane (OM) in most gram-negative bacteria, and its structure and biosynthetic pathway are well known. Nevertheless, the mechanisms of transport and assembly of this molecule at the cell surface are poorly understood. The inner membrane (IM) transport protein MsbA is responsible for flipping LPS across the IM. Additional components of the LPS transport machinery downstream of MsbA have been identified, including the OM protein complex LptD/LptE (formerly Imp/RlpB), the periplasmic LptA protein, the IM-associated cytopla

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Martorana, Alessandra M., Mattia Benedet, Elisa A. Maccagni, et al. "Functional Interaction between the Cytoplasmic ABC Protein LptB and the Inner Membrane LptC Protein, Components of the Lipopolysaccharide Transport Machinery in Escherichia coli." Journal of Bacteriology 198, no. 16 (2016): 2192–203. http://dx.doi.org/10.1128/jb.00329-16.

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ABSTRACTThe assembly of lipopolysaccharide (LPS) in the outer leaflet of the outer membrane (OM) requires the transenvelope Lpt (lipopolysaccharide transport) complex, made inEscherichia coliof seven essential proteins located in the inner membrane (IM) (LptBCFG), periplasm (LptA), and OM (LptDE). At the IM, LptBFG constitute an unusual ATP binding cassette (ABC) transporter, composed by the transmembrane LptFG proteins and the cytoplasmic LptB ATPase, which is thought to extract LPS from the IM and to provide the energy for its export across the periplasm to the cell surface. LptC is a small

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Ren, Yixin, Wenting Dong, Yan Li, et al. "The Prediction of LptA and LptC Protein–Protein Interactions and Virtual Screening for Potential Inhibitors." Molecules 29, no. 8 (2024): 1827. http://dx.doi.org/10.3390/molecules29081827.

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Antibiotic resistance in Gram-negative bacteria remains one of the most pressing challenges to global public health. Blocking the transportation of lipopolysaccharides (LPS), a crucial component of the outer membrane of Gram-negative bacteria, is considered a promising strategy for drug discovery. In the transportation process of LPS, two components of the LPS transport (Lpt) complex, LptA and LptC, are responsible for shuttling LPS across the periplasm to the outer membrane, highlighting their potential as targets for antibacterial drug development. In the current study, a protein–protein int

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Lin, Yu-Ling, Li-Yi Chen, Chia-Hung Chen, et al. "A Soybean Oil-Based Liposome-Polymer Transfection Complex as a Codelivery System for DNA and Subunit Vaccines." Journal of Nanomaterials 2012 (2012): 1–12. http://dx.doi.org/10.1155/2012/427306.

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Inexpensive liposome-polymer transfection complexes (LPTCs) were developed and used as for DNA or protein delivery. The particle sizes of the LPTCs were in the range of 212.2 to 312.1 nm, and the zetapotential was +38.7 mV. LPTCs condensed DNA and protected DNA from DNase I digestion and efficiently delivered LPTC/DNA complexes in Balb/3T3 cells. LPTCs also enhanced the cellular uptake of antigen in mouse macrophage cells and stimulated TNF-αrelease in naïve mice splenocytes, both indicating the potential of LPTCs as adjuvants for vaccines.In vivostudies were performed usingH. pylorirelative h

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Dai, Xiaowei, Min Yuan, Yu Lu, et al. "Identification of a Small Molecule That Inhibits the Interaction of LPS Transporters LptA and LptC." Antibiotics 11, no. 10 (2022): 1385. http://dx.doi.org/10.3390/antibiotics11101385.

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The need for novel antibiotics has become imperative with the increasing prevalence of antibiotic resistance in Gram-negative bacteria in clinics. Acting as a permeability barrier, lipopolysaccharide (LPS) protects Gram-negative bacteria against drugs. LPS is synthesized in cells and transported to the outer membrane (OM) via seven lipopolysaccharide transport (Lpt) proteins (LptA–LptG). Of these seven Lpt proteins, LptC interacts with LptA to transfer LPS from the inner membrane (IM) to the OM, and assembly is aided by LptD/LptE. This interaction among the Lpt proteins is important for the bi

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Hicks, Greg, and Zongchao Jia. "Structural Basis for the Lipopolysaccharide Export Activity of the Bacterial Lipopolysaccharide Transport System." International Journal of Molecular Sciences 19, no. 9 (2018): 2680. http://dx.doi.org/10.3390/ijms19092680.

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Gram-negative bacteria have a dense outer membrane (OM) coating of lipopolysaccharides, which is essential to their survival. This coating is assembled by the LPS (lipopolysaccharide) transport (Lpt) system, a coordinated seven-subunit protein complex that spans the cellular envelope. LPS transport is driven by an ATPase-dependent mechanism dubbed the “PEZ” model, whereby a continuous stream of LPS molecules is pushed from subunit to subunit. This review explores recent structural and functional findings that have elucidated the subunit-scale mechanisms of LPS transport, including the novel AB

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Xiang, Quanju, Haiyan Wang, Zhongshan Wang, Yizheng Zhang, and Changjiang Dong. "Characterization of lipopolysaccharide transport protein complex." Open Life Sciences 9, no. 2 (2014): 131–38. http://dx.doi.org/10.2478/s11535-013-0250-5.

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AbstractLipopolysaccharide (LPS) is an essential component of the outer membranes (OM) of most Gram-negative bacteria, which plays a crucial role in protection of the bacteria from toxic compounds and harsh conditions. The LPS is biosynthesized at the cytoplasmic side of inner membrane (IM), and then transported across the aqueous periplasmic compartment and assembled correctly at the outer membrane. This process is accomplished by seven LPS transport proteins (LptA-G), but the transport mechanism remains poorly understood. Here, we present findings by pull down assays in which the periplasmic

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Vetterli, Stefan U., Katja Zerbe, Maik Müller, et al. "Thanatin targets the intermembrane protein complex required for lipopolysaccharide transport inEscherichia coli." Science Advances 4, no. 11 (2018): eaau2634. http://dx.doi.org/10.1126/sciadv.aau2634.

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With the increasing resistance of many Gram-negative bacteria to existing classes of antibiotics, identifying new paradigms in antimicrobial discovery is an important research priority. Of special interest are the proteins required for the biogenesis of the asymmetric Gram-negative bacterial outer membrane (OM). Seven Lpt proteins (LptA to LptG) associate in most Gram-negative bacteria to form a macromolecular complex spanning the entire envelope, which transports lipopolysaccharide (LPS) molecules from their site of assembly at the inner membrane to the cell surface, powered by adenosine 5′-t

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Schultz, Kathryn M., and Candice S. Klug. "Characterization of and lipopolysaccharide binding to the E. coli LptC protein dimer." Protein Science 27, no. 2 (2017): 381–89. http://dx.doi.org/10.1002/pro.3322.

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Cina, Nicholas P., and Candice S. Klug. "Characterizing the interactions between the LPS transport protein LptC and the ABC transporter LptB2FG." Biophysical Journal 122, no. 3 (2023): 56a. http://dx.doi.org/10.1016/j.bpj.2022.11.511.

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Thèses sur le sujet "LptC protein"

SESTITO, STEFANIA ENZA. "LPS-binding proteins: interaction studies with natural and synthetic ligands." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2015. http://hdl.handle.net/10281/67756.

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L’obiettivo di questa tesi è elucidare alcuni aspetti dell’interazione tra proteine che legano il lipopolisaccaride (LPS) batterico e il loro ligando naturale o ligandi di sintesi. LptC (Lipopolysaccharide transport C) è una proteina batterica che appartiene al sistema di trasporto Lpt, un sistema di 7 proteine essenziali che trasportano l’LPS sulla membrana esterna dei batteri Gram negativi dopo la sua biosintesi. Sebbene molti elementi della biosintesi dell’LPS siano stati elucidati, il preciso meccanismo di trasporto è ancora poco chiaro. Poiché LptC può essere considerata come proteina m

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Pandey, Sundar. "Novel Role of Pseudomonas Aeruginosa LptD Operon." FIU Digital Commons, 2018. https://digitalcommons.fiu.edu/etd/3734.

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Pseudomonas aeruginosais an opportunistic pathogen that infects cystic fibrosis (CF) patients contributing to their high morbidity and mortality. P. aeruginosaundergoes a phenotypic conversion in the CF lung, from nonmucoid to mucoid, by constitutively producing a polysaccharide called alginate. These mucoid strains often revert to nonmucoid in vitrodue to second-site suppressor mutations. We hypothesized that mapping these mutations would lead to the identification of novel genes involved in alginate production. In a previous study, a mucoid strain, PDO300 (PAOmucA22), was used to isolate sup

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CIARAMELLI, CARLOTTA. "Synthesis and characterization of new small-molecule ligands of LPS binding proteins." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2015. http://hdl.handle.net/10281/77016.

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Lo scopo del presente lavoro è la progettazione, la sintesi e la caratterizzazione di nuove small molecules, attive come ligandi di LPS (lipopolisaccaridi)-binding proteins. Gli LPS, o endotossine batteriche, sono macromolecole anfifiliche ubiquitarie sulla membrana esterna dei batteri Gram-negativi. Le proteine che legano gli LPS studiate nel corso di questo progetto di tesi di dottorato appartengono a due categorie: le proteine batteriche di trasporto Lpt e il sistema recettoriale TLR4, che comprende anche i co-recettori LBP, CD14, MD2. Le proteine Lpt, e in particolare la proteina LptC, so

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Lundstedt, Emily. "Lipopolysaccharide structure and LptFG modulate the activity of the LptB₂ ATPase." The Ohio State University, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1594998769457759.

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Lin, Wan-Ting, and 林琬亭. "Pre-emptive analgesia reduced GalR2 and pain-related proteins expression on LPC induced animal neuropathic pain model." Thesis, 2014. http://ndltd.ncl.edu.tw/handle/20143053377211524504.

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碩士<br>國立臺灣大學<br>解剖學暨細胞生物學研究所<br>102<br>Previous studies have shown that Galanin modulated peripheral pain sensation via galanin receptor type 2 (GalR2). Following nerve injury, inflammation, spontaneous discharge and upregulation of pain related factors would involve in neuropathic pain development. To our knowledge, the correlation between median nerve demyelination and GalR2 and its substrate expression levels has not been documented; and yet the effect of GalR2 on medain neuropathic pain is not valid. Thus, using LPC treated median nerve injury model, we investigate the role of GalR2 and it

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Livres sur le sujet "LptC protein"

The 2.05 Å crystal structure of LptB, an essential protein in gram-negative bacterial outer membrane biogenesis. 2011.

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Chapitres de livres sur le sujet "LptC protein"

Bollati, Michela, and Louise J. Gourlay. "Protein Crystallization of Two Recombinant Lpt Proteins." In Lipopolysaccharide Transport. Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2581-1_15.

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Actes de conférences sur le sujet "LptC protein"

Boachie, Ruth, Ogadimma Okagu, Raliat Abioye, et al. "Formation of Lentil Protein-tannic Acid Complexes Limits in Vitro Peptic Hydrolysis and Alters Peptidomic Profiles of the Protein." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/txix9391.

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Food protein interaction with other biopolymers, such as tannic acids, within a food matrix can alter their structure and functionality. In this study, the nature of lentil protein-tannic acid (LPTA) interaction and its effect on in vitro peptic hydrolysis were investigated. In LPTA mixtures containing 1% w/v LP and 0.001% - 0.5% TA, a twenty-fold increase in particle size was observed in LPTA 0.5% compared to LPI, indicating aggregation. Static quenching of tryptophan residues within the protein hydrophobic folds were observed. Increasing TA content caused an overall increase in α-helix fract

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Muth, Bastian, and Reinhard Niehuis. "Axial Loss Development in Low Pressure Turbine Cascades." In ASME Turbo Expo 2012: Turbine Technical Conference and Exposition. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/gt2012-69726.

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The objective of this work presented in this paper is to study the performance of low pressure turbines in detail by extensive numerical simulations. The numerical flow simulations were conducted using the general purpose code ANSYS CFX. Particular attention is focused on the loss development in axial direction within the flow passage of the cascade. It is shown that modern CFD tools are able to break down the integral loss of the turbine profile into its components depending on attached and separated flow areas. In addition the numerical results allow to show the composition of the loss depen

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