Relevant bibliographies by topics / ATP-binding cassette proteins

Academic literature on the topic 'ATP-binding cassette proteins'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "ATP-binding cassette proteins"

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Greenberger, Lee M., and Yoshihiro Ishikawa. "ATP-binding cassette proteins." Trends in Cardiovascular Medicine 4, no. 4 (July 1994): 193–98. http://dx.doi.org/10.1016/1050-1738(94)90057-4.

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Burke, Michael A., and Hossein Ardehali. "Mitochondrial ATP–binding cassette proteins." Translational Research 150, no. 2 (August 2007): 73–80. http://dx.doi.org/10.1016/j.trsl.2007.03.002.

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Srikant, Sriram. "Evolutionary history of ATP‐binding cassette proteins." FEBS Letters 594, no. 23 (November 21, 2020): 3882–97. http://dx.doi.org/10.1002/1873-3468.13985.

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Michealis, S., and C. Berkower. "Sequence Comparison of Yeast ATP-binding Cassette Proteins." Cold Spring Harbor Symposia on Quantitative Biology 60 (January 1, 1995): 291–307. http://dx.doi.org/10.1101/sqb.1995.060.01.034.

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Lomri, Noureddine, J. Fitz, and Bruce Scharschmidt. "Hepatocellular Transport: Role of ATP-Binding Cassette Proteins." Seminars in Liver Disease 16, no. 02 (1996): 201–10. http://dx.doi.org/10.1055/s-2007-1007232.

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Lorkowski, Stefan, and Paul Cullen. "ABCG subfamily of human ATP-binding cassette proteins." Pure and Applied Chemistry 74, no. 11 (January 1, 2002): 2057–81. http://dx.doi.org/10.1351/pac200274112057.

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ATP-binding cassette (ABC) proteins form one of the largest known protein families and have been found in all known organisms. Most members of the human ABC protein family are membrane-spanning transporters that use energy derived from the hydrolysis of ATP to transport specific substrates across cell membranes. Mutations in certain human ABC transporters of the subfamilies A, B, C, and D have been shown to cause a wide variety of inherited diseases such as the lung condition cystic fibrosis, the nervous degenerative condition adrenoleukodystrophy (of Lorenzo’s Oil fame), hereditary macular degeneration of the eye (Stargardt’s disease), and inherited deficiency of circulating high-density lipoproteins (Tangier disease or familial hypoalphalipoproteinemia). Very recent studies showed that mutations in two members of the subfamily G of human ABC transporters (ABCG5 and ABCG8) cause a condition called sitosterolemia in which plant sterols accumulate in the body and may be responsible for influencing total body sterol homeostasis. In addition, other members of the subfamily G, namely ABCG1 and ABCG4, have also been shown to be involved in cellular lipid trafficking and are thought to play important roles during foam cell formation of human macrophages. By contrast, ABCG2 is a multidrug resistance transporter.In this review, we focus on the current knowledge and physiological background of the members of the subfamily G. We also present new insights on the evolutionary relationship of human and nonhuman ABCG proteins.
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Linton, Kenneth J., and Christopher F. Higgins. "The Escherichia coli ATP-binding cassette (ABC) proteins." Molecular Microbiology 28, no. 1 (May 1, 2002): 5–13. http://dx.doi.org/10.1046/j.1365-2958.1998.00764.x.

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Altenberg, Guillermo A. "The Engine of ABC Proteins." Physiology 18, no. 5 (October 2003): 191–95. http://dx.doi.org/10.1152/nips.01445.2003.

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Proteins that belong to the ATP-binding cassette superfamily span from bacteria to humans and comprise one of the largest protein families. These proteins are characterized by the presence of two nucleotide-binding domains, and recent studies suggest that association and dissociation of these domains is a common basic molecular mechanism of operation that couples ATP binding/hydrolysis to substrate transport across membranes.
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Licht, Anke, and Erwin Schneider. "ATP binding cassette systems: structures, mechanisms, and functions." Open Life Sciences 6, no. 5 (October 1, 2011): 785–801. http://dx.doi.org/10.2478/s11535-011-0054-4.

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AbstractATP-binding cassette (ABC) systems are found in all three domains of life and in some giant viruses and form one of the largest protein superfamilies. Most family members are transport proteins that couple the free energy of ATP hydrolysis to the translocation of solutes across a biological membrane. The energizing module is also used to drive non-transport processes associated, e.g., with DNA repair and protein translation. Many ABC proteins are of considerable medical importance. In humans, dysfunction of at least eighteen out of 49 ABC transporters is associated with disease, such as cystic fibrosis, Tangier disease, adrenoleukodystrophy or Stargardt’s macular degeneration. In prokaryotes, ABC proteins confer resistance to antibiotics, secrete virulence factors and envelope components, or mediate the uptake of a large variety of nutrients. Canonical ABC transporters share a common structural organization comprising two transmembrane domains (TMDs) that form the translocation pore and two nucleotide-binding domains (NBDs) that bind and hydrolyze ATP. In this Mini-Review, we summarize recent structural and biochemical data obtained from both prokaryotic and eukaryotic model systems.
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Demolombe, Sophie, and Denis Escande. "ATP-binding cassette proteins as targets for drug discovery." Trends in Pharmacological Sciences 17, no. 8 (August 1996): 273–75. http://dx.doi.org/10.1016/0165-6147(96)10037-7.

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Dissertations / Theses on the topic "ATP-binding cassette proteins"

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Fischer, Jeffrey James, and University of Lethbridge Faculty of Arts and Science. "Initial characterization of the ribosome-associated ATP binding cassette (ABC) protein YHIH from E. Coli." Thesis, Lethbridge, Alta. : University of Lethbridge, Faculty of Arts and Science, 2007, 2007. http://hdl.handle.net/10133/658.

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Protein synthesis is a highly conserved process across all domains of life, both structurally and functionally. This cyclic process is catalyzed by numerous soluble protein factors that interact with the ribosome to facilitate efficient protein synthesis. Many canonical translation factors bind and hydrolyze GTP to induce conformational changes that facilitate translation. For example, GTP hydrolysis by EF-Tu is required for the release of aminoacyl-tRNA into the ribosomal A site; GTP hydrolysis by EF-G facilitates the movement of tRNA and mRNA from the A site to the P site of the ribosome. However, protein synthesis seems to also have a requirement for ATP; the essential yeast protein eEF-3 facilitates release of deacyl-tRNA from the ribosomal E site. In Escherichia coli, the protein product of the open reading frame yhih has been suggested to have a similar function. However, the role of this unique prokaryotic protein is not understood. Preliminary characterization of this protein suggests a nucleotide-dependent conformational change occurs in a truncated form of the protein, ΔP541 Yhih. Interestingly, this phenomenon is not observed in ΔL432 Yhih. Both ΔP541 Yhih, and to a lesser extent ΔL432 Yhih, exhibit a ribosome-dependent ATPase activity, suggesting the primary region for binding with the ribosome lies between Leu432 and Pro541.
x, 101 leaves : ill. ; 29 cm.
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Harrington, Leon E. O. "Engineering pores for stochastic sensing and single molecule studies." Thesis, University of Oxford, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.711643.

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Johnson, Soraya Sarah. "Control of the protein and lipid content of the plasma membrane by ATP-binding cassette transporter proteins in S. Cerevisiae." Diss., University of Iowa, 2010. https://ir.uiowa.edu/etd/825.

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Pdr5 and Yor1 are two ATP-binding cassette transporters regulated by the pleiotropic drug resistance (PDR) network in the yeast Saccharomyces cerevisiae. Recent work from another group demonstrated that a pdr5Δ yor1 strain confers remarkable resistance to a sphingolipid intermediate, phytosphingosine (PHS), which was surprising as loss of these transporters normally leads to elevated drug sensitivity. PHS is toxic to the cell at high levels due to mislocalization of nutrient permeases, such as the high affinity tryptophan transporter, Tat2. Although the above study suggested that this resistance was due to increased expression of Rsb1, a known mediator of PHS tolerance, this was not reproducible in our hands and we sought to identify other determinants for this phenotype. The work presented here demonstrates that the pdr5Δ yor1 strain exhibits delayed turnover of Tat2 and an increase in tryptophan uptake, which we postulate is due to changes membrane asymmetry resulting in decreased endocytosis. Conversely, cells lacking Rsb1 showed a decrease in tryptophan import and increased Tat2 turnover, independent of endogenous PHS levels. Rsb1 has a predicted 7 transmembrane (7TM) topology, which argues against the idea that Rsb1 functions directly in PHS transport, as there are currently no known transporters with this topology. These data suggest that Rsb1 and Pdr5/Yor1 function in regulation of endocytosis of Tat2, and possibly other membrane proteins. Ethyl methanesulfonate mutagenesis of the pdr5Δ yor1 strain and a candidate gene approach were alternative methods used to identify mediators of PHS tolerance in this strain. Inconsistent results from PHS selection led to the discovery that the pdr5Δ yor1 strain was also robustly resistant to the sphingolipid biosynthesis inhibitor, Aureobasidin A (AbA), which was subsequently used for analysis. These approaches revealed several genes, including Gda1, Mss4, and Ypk1 that are important for AbA tolerance in the pdr5Δ yor1 strain. Many of these determinants play a role in cell wall integrity, suggesting that loss of Pdr5 and Yor1 may lead to activated cell wall integrity pathways resulting in altered cell wall structure.
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Kennedy, Kathleen Anne. "Assembly of the maltose transport complex of Escherichia coli and the dimerization, localization, and functional domain structure of its ATP-binding subunit, MalK /." Thesis, Connect to this title online; UW restricted, 1999. http://hdl.handle.net/1773/11504.

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Englund, Gunilla. "Interindividual Variability of Drug Transport Proteins : Focus on Intestinal Pgp (ABCB1) and BCRP (ABCG2)." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis: Univ.-bibl. [distributör], 2005. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-6127.

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Brechbuhl, Heather Michelle. "ATP-cassette binding transporters : modulators of glutathione levels in normal cellular physiology and as a means for therapeutic applications /." Connect to abstract via ProQuest. Full text is not available online, 2008.

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Nelson, Bryn D. "Examining the role of MalG in the assembly and function of the maltose transport complex in Escherichia coli : implications for the study of integral membrane proteins /." Thesis, Connect to this title online; UW restricted, 1998. http://hdl.handle.net/1773/11508.

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Ibbotson, Kathryn, Joshua Yell, and Patrick T. Ronaldson. "Nrf2 signaling increases expression of ATP-binding cassette subfamily C mRNA transcripts at the blood–brain barrier following hypoxia-reoxygenation stress." BIOMED CENTRAL LTD, 2017. http://hdl.handle.net/10150/623277.

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Background: Strategies to maintain BBB integrity in diseases with a hypoxia/reoxygenation (H/R) component involve preventing glutathione (GSH) loss from endothelial cells. GSH efflux transporters include multidrug resistance proteins (Mrps). Therefore, characterization of Mrp regulation at the BBB during H/R is required to advance these transporters as therapeutic targets. Our goal was to investigate, in vivo, regulation of Abcc1, Abcc2, and Abcc4 mRNA expression (i.e., genes encoding Mrp isoforms that transport GSH) by nuclear factor E2-related factor (Nrf2) using a well-established H/R model. Methods: Female Sprague-Dawley rats (200-250 g) were subjected to normoxia (Nx, 21% O-2, 60 min), hypoxia (Hx, 6% O-2, 60 min) or H/R (6% O-2, 60 min followed by 21% O-2, 10 min, 30 min, or 1 h) or were treated with the Nrf2 activator sulforaphane (25 mg/kg, i.p.) for 3 h. Abcc mRNA expression in brain microvessels was determined using quantitative real-time PCR. Nrf2 signaling activation was examined using an electrophoretic mobility shift assay (EMSA) and chromatin immunoprecipitation (ChIP) respectively. Data were expressed as mean +/- SD and analyzed via ANOVA followed by the post hoc Bonferroni t test. Results: We observed increased microvascular expression of Abcc1, Abcc2, and Abcc4 mRNA following H/R treatment with reoxygenation times of 10 min, 30 min, and 1 h and in animals treated with sulforaphane. Using a biotinylated Nrf2 probe, we observed an upward band shift in brain microvessels isolated from H/R animals or animals administered sulforaphane. ChIP studies showed increased Nrf2 binding to antioxidant response elements on Abcc1, Abcc2, and Abcc4 promoters following H/R or sulforaphane treatment, suggesting a role for Nrf2 signaling in Abcc gene regulation. Conclusions: Our data show increased Abcc1, Abcc2, and Abcc4 mRNA expression at the BBB in response to H/R stress and that Abcc gene expression is regulated by Nrf2 signaling. Since these Mrp isoforms transport GSH, these results may point to endogenous transporters that can be targeted for BBB protection during H/R stress. Experiments are ongoing to examine functional implications of Nrf2-mediated increases in Abcc transcript expression. Such studies will determine utility of targeting Mrp isoforms for BBB protection in diseases with an H/R component.
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Petri, Niclas. "Involvement of Membrane Transport Proteins in Intestinal Absorption and Hepatic Disposition of Drugs Using Fexofenadine as a Model Drug." Doctoral thesis, Uppsala University, Department of Pharmacy, 2005. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-5808.

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The aims of this thesis were to study the in vivo relevance of membrane transporters for intestinal absorption and the hepatic disposition of drugs in humans and preclinical models. Fexofenadine is a substrate for ABCB1 (P-glycoprotein) and members of the organic anion transporting polypeptide (OATP/SLCO) family. It is marginally metabolised in humans.

The influence of known inhibitors of ABCB1 and OATPs on the membrane transport and pharmacokinetics of fexofenadine was investigated in Caco-2 and porcine models and in humans. The permeability of fexofenadine remained low, even when significantly altered by the addition of an inhibitor. Using the Loc-I-Gut® technique in vivo in humans, it was possible to see that the jejunal effective permeability of fexofenadine was unchanged when given with verapamil. However, the systemic exposure and apparent absorption rate of fexofenadine increased. This suggests that the first-pass liver extraction of fexofenadine was reduced by verapamil, probably through the inhibition of sinusoidal OATP-mediated and/or canalicular ABCB1-mediated secretion. The unchanged permeability can be explained by simultaneous inhibition of jejunal apical OATP-uptake and ABCB1-efflux, which would leave fexofenadine to be transported by passive trancellular diffusion. A Loc-I-Gut® perfusion in the porcine model enabling blood sampling in the portal and hepatic veins and bile collection revealed increased jejunal permeability, but no subsequent verapamil-induced elevation in the systemic exposure of fexofenadine. This indicates a species-related difference in the localisation of and/or the substrate specificity of fexofenadine for the transporters involved. The absence of an effect on the first-pass liver extraction in the porcine model might be caused by the observed lower liver exposure of verapamil.

Finally, a novel intubation technique enabling dosing of fexofenadine in the jejunum, ileum and the colon showed that fexofenadine was absorbed less along the length the intestine in agreement with the properties of a low permeability drug.

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Turner, Joel G. "Drug resistance to topoisomerase directed chemotherapy in human multiple myeloma." [Tampa, Fla] : University of South Florida, 2008. http://purl.fcla.edu/usf/dc/et/SFE0002446.

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Books on the topic "ATP-binding cassette proteins"

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B, Holland I., ed. ABC proteins: From bacteria to man. Amsterdam: Academic Press, 2003.

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Ahcène, Boumendjel, Boutonnat Jean, and Robert Jacques M. D, eds. ABC transporters and multidrug resistance. Hoboken, N.J: John Wiley & Sons, 2009.

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(Editor), I. Barry Holland, Susan P. C. Cole (Editor), Karl Kuchler (Editor), and Christopher F. Higgins (Editor), eds. ABC Proteins: From Bacteria to Man. Academic Press, 2002.

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ABC Proteins: From Bacteria to Man. Academic Press, 2002.

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Robert, Jacques, Ahcène Boumendjel, Jean Boutonnat, and Ahcène Boumendjel. ABC Transporters and Multidrug Resistance. Wiley & Sons, Incorporated, John, 2009.

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Boumendjel, Ahcne, Ahc Boumendjel, Jacques Robert, and Jean Boutonnat. ABC Transporters and Multidrug Resistance. Wiley & Sons, Incorporated, John, 2009.

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Book chapters on the topic "ATP-binding cassette proteins"

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Leighton, Jonathan. "Identification and Characterization of Novel ATP-Binding Cassette Proteins in Saccharomyces Cerevisiae." In Biological Membranes: Structure, Biogenesis and Dynamics, 263–68. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78846-8_26.

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Bozdech, Zbynek, and Erwin Schurr. "Protein Transport in the Host Cell Cytoplasm and ATP-Binding Cassette Proteins in Plasmodium Falciparum-Infected Erythrocytes." In Novartis Foundation Symposium 226 - Transport and Trafficking in the Malaria-Infected Erythrocyte, 231–51. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470515730.ch16.

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"ATP Binding Cassette Proteins." In Encyclopedia of Molecular Pharmacology, 261. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-57401-7_300068.

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Berkower, Carol, and Susan Michaelis. "ATP binding cassette proteins in yeast." In Membrane Protein Transport, 231–77. Elsevier, 1996. http://dx.doi.org/10.1016/s1874-592x(96)80010-2.

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Yazaki, Kazufumi, Nobukazu Shitan, Akifumi Sugiyama, and Kojiro Takanashi. "Chapter 6 Cell and Molecular Biology of ATP‐Binding Cassette Proteins in Plants." In International Review of Cell and Molecular Biology, 263–99. Elsevier, 2009. http://dx.doi.org/10.1016/s1937-6448(09)76006-x.

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DASSA, ELIE. "PHYLOGENETIC AND FUNCTIONAL CLASSIFICATION OF ABC (ATP-BINDING CASSETTE) SYSTEMS**ABSCISSE, a database of ABC systems, which includes functional, sequence and structural information, is available on the internet at the following address: www.pasteur.fr/recherche/unites/pmtg/abc/index.html." In ABC Proteins, 3–35. Elsevier, 2003. http://dx.doi.org/10.1016/b978-012352551-2/50002-0.

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Egner, Ralf, Yannick Mahé, Rudy Pandjaitan, Veronika Huter, Andrea Lamprecht, and Karl Kuchler. "ATP binding cassette transporters in yeast." In Membrane Protein Transport, 57–96. Elsevier, 1995. http://dx.doi.org/10.1016/s1874-592x(06)80004-1.

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Korolev, Sergey. "ATP-Binding Cassette Properties of Recombination Mediator Protein RecF." In DNA Repair. InTech, 2011. http://dx.doi.org/10.5772/21178.

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Wierzbicki, Anthony S. "Disorders of peroxisomal metabolism in adults." In Oxford Textbook of Medicine, edited by Timothy M. Cox, 2157–73. Oxford University Press, 2020. http://dx.doi.org/10.1093/med/9780198746690.003.0236.

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The peroxisome is a specialized organelle which employs molecular oxygen in the oxidation of complex organic molecules including lipids. Enzymatic pathways for the metabolism of fatty acids, including very long-chain fatty acids (VLCFAs), enable this organelle to carry out β‎-oxidation in partnership with mitochondria. A peroxisomal pathway for isoprenoid lipids derived from chlorophyll, such as phytanic acid, utilizes α‎-oxidation, but a default mechanism involving ω‎-oxidation may also metabolize phytanic acid and its derivatives. The biochemical manifestations, molecular pathology, and diverse clinical features of many peroxisomal disorders have now been clarified, offering the promise of prompt diagnosis, better management, and useful means to provide appropriate genetic counselling for affected families. At the same time, specific treatments including rigorous dietary interventions and plasmapheresis to remove undegraded toxic metabolites offer credible hope of improvement and prevention of disease in affected individuals. X-linked adrenoleukodystrophy (X-ALD)—due to mutations in the gene for an ATP-binding cassette (ABC) protein of unknown function and characterized by accumulation of unbranched saturated VLCFAs, particularly hexacosanoate (C26), in the cholesterol esters of brain white matter, adrenal cortex, and certain sphingolipids of the brain. The disease has multiple phenotypes. Most cases develop increasing handicap; management is palliative and supportive in most instances. Adult Refsum’s disease—due in most cases to mutations in the gene for phytanoyl-CoA hydroxylase (PHYH) such that patients are unable to detoxify phytanic acid by α‎-oxidation and have greatly elevated levels of this in their plasma. Usually presents in late childhood with progressive deterioration of night vision, the occurrence of progressive retinitis pigmentosa, and anosmia. Treatment is by restriction of dietary phytanic acid, with or without its elimination by plasmapheresis or apheresis.
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"PGP, P-GP, Multidrug Resistance Protein 1, MDR1, ATP-Binding Cassette Transporter Subfamily B Member 1, ABCB1, Permeability Glycoprotein, Cluster of Differentiation 243." In The ADME Encyclopedia, 786. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-84860-6_300308.

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Conference papers on the topic "ATP-binding cassette proteins"

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Hsiao, Sung-Han, Shahrooz Vahedi, Suresh V. Ambudkar, and Chung-Pu Wu. "Abstract 4895: Human ATP-binding cassette proteins ABCB1 and ABCG2 confer resistance to histone deacetylase 6 inhibitor ricolinostat (ACY-1215) in cancer cell lines." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-4895.

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Teo, Ka Yaw, and Bumsoo Han. "Freezing-Assisted Intracellular Drug Delivery to Multi-Drug Resistant Cancer Cells." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-192373.

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The efficacy of chemotherapy is significantly impaired by multi-drug resistance (MDR) of cancer cells. The mechanism of MDR is associated with the overexpression of certain ATP-binding cassette protein transporters in plasma membranes. These transporters actively keep intracellular drug concentration below the cell-killing threshold by extruding cytotoxic drugs. Various strategies to overcome MDR have been proposed and have shown promising results at the laboratory level. However, pharmacokinetic alteration of co-administered anticancer agents reduces their clinical effectiveness. This leads to increased toxicity and undesirable side effects at effective concentrations [1]. Hence, a clinically feasible strategy to overcome the phenomenon of MDR is highly desired.
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Natarajan, Karthika, Mehmet Burcu, and Maria R. Baer. "Abstract 706: The serine/threonine kinase Pim-1 promotes drug resistance mediated by the ATP-binding cassette multidrug resistance protein breast cancer resistance protein (BCRP, ABCG2) by stabilizing higher-order BCRP multimers." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-706.

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