Статті в журналах: "ATP-binding cassette proteins"

1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Cooper, Rebecca S., and Guillermo A. Altenberg. "Association/Dissociation of the Nucleotide-binding Domains of the ATP-binding Cassette Protein MsbA Measured during Continuous Hydrolysis." Journal of Biological Chemistry 288, no. 29 (May 30, 2013): 20785–96. http://dx.doi.org/10.1074/jbc.m113.477976.

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In ATP-binding cassette proteins, the two nucleotide-binding domains (NBDs) work as dimers to bind and hydrolyze ATP, but the molecular mechanism of nucleotide hydrolysis is controversial. It is still unresolved whether hydrolysis leads to dissociation of the ATP-induced dimers or partial opening of the dimers such that the NBDs remain in contact during the hydrolysis cycle. We studied the bacterial lipid flippase MsbA by luminescence resonance energy transfer (LRET). The LRET signal between optical probes reacted with single-cysteine mutants was employed to follow NBD association/dissociation in real time. The intermonomer distances calculated from LRET data indicate that the NBDs separate completely following ATP hydrolysis, even in the presence of mm MgATP, and that the dissociation occurs following each hydrolysis cycle. The results support association/dissociation, as opposed to constant contact models, for the mode of operation of ATP-binding cassette proteins.

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12

Su, Weixin, Veerendra Kumar, Yichen Ding, Rya Ero, Aida Serra, Benjamin Sian Teck Lee, Andrew See Weng Wong, et al. "Ribosome protection by antibiotic resistance ATP-binding cassette protein." Proceedings of the National Academy of Sciences 115, no. 20 (April 30, 2018): 5157–62. http://dx.doi.org/10.1073/pnas.1803313115.

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The ribosome is one of the richest targets for antibiotics. Unfortunately, antibiotic resistance is an urgent issue in clinical practice. Several ATP-binding cassette family proteins confer resistance to ribosome-targeting antibiotics through a yet unknown mechanism. Among them, MsrE has been implicated in macrolide resistance. Here, we report the cryo-EM structure of ATP form MsrE bound to the ribosome. Unlike previously characterized ribosomal protection proteins, MsrE is shown to bind to ribosomal exit site. Our structure reveals that the domain linker forms a unique needle-like arrangement with two crossed helices connected by an extended loop projecting into the peptidyl-transferase center and the nascent peptide exit tunnel, where numerous antibiotics bind. In combination with biochemical assays, our structure provides insight into how MsrE binding leads to conformational changes, which results in the release of the drug. This mechanism appears to be universal for the ABC-F type ribosome protection proteins.

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13

Dean, Michael, Andrey Rzhetsky, and Rando Allikmets. "The Human ATP-Binding Cassette (ABC) Transporter Superfamily." Genome Research 11, no. 7 (January 18, 2001): 1156–66. http://dx.doi.org/10.1101/gr.184901.

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The ATP-binding cassette (ABC) transporter superfamily contains membrane proteins that translocate a variety of substrates across extra- and intra-cellular membranes. Genetic variation in these genes is the cause of or contributor to a wide variety of human disorders with Mendelian and complex inheritance, including cystic fibrosis, neurological disease, retinal degeneration, cholesterol and bile transport defects, anemia, and drug response. Conservation of the ATP-binding domains of these genes has allowed the identification of new members of the superfamily based on nucleotide and protein sequence homology. Phylogenetic analysis is used to divide all 48 known ABC transporters into seven distinct subfamilies of proteins. For each gene, the precise map location on human chromosomes, expression data, and localization within the superfamily has been determined. These data allow predictions to be made as to potential functions or disease phenotypes associated with each protein. In this paper, we review the current state of knowledge on all human ABC genes in inherited disease and drug resistance. In addition, the availability of the completeDrosophila genome sequence allows the comparison of the known human ABC genes with those in the fly genome. The combined data enable an evolutionary analysis of the superfamily. Complete characterization of all ABC from the human genome and from model organisms will lead to important insights into the physiology and the molecular basis of many human disorders.

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14

Davidson, Amy L., Elie Dassa, Cedric Orelle, and Jue Chen. "Structure, Function, and Evolution of Bacterial ATP-Binding Cassette Systems." Microbiology and Molecular Biology Reviews 72, no. 2 (June 2008): 317–64. http://dx.doi.org/10.1128/mmbr.00031-07.

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SUMMARY ATP-binding cassette (ABC) systems are universally distributed among living organisms and function in many different aspects of bacterial physiology. ABC transporters are best known for their role in the import of essential nutrients and the export of toxic molecules, but they can also mediate the transport of many other physiological substrates. In a classical transport reaction, two highly conserved ATP-binding domains or subunits couple the binding/hydrolysis of ATP to the translocation of particular substrates across the membrane, through interactions with membrane-spanning domains of the transporter. Variations on this basic theme involve soluble ABC ATP-binding proteins that couple ATP hydrolysis to nontransport processes, such as DNA repair and gene expression regulation. Insights into the structure, function, and mechanism of action of bacterial ABC proteins are reported, based on phylogenetic comparisons as well as classic biochemical and genetic approaches. The availability of an increasing number of high-resolution structures has provided a valuable framework for interpretation of recent studies, and realistic models have been proposed to explain how these fascinating molecular machines use complex dynamic processes to fulfill their numerous biological functions. These advances are also important for elucidating the mechanism of action of eukaryotic ABC proteins, because functional defects in many of them are responsible for severe human inherited diseases.

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15

Müller, Michael. "FUNCTION AND REGULATION OF HEPATIC ATP-BINDING CASSETTE TRANSPORTER PROTEINS." Drug Metabolism and Pharmacokinetics 13, supplement (1998): 64–67. http://dx.doi.org/10.2133/dmpk.13.supplement_64.

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16

MATSUO, Michinori. "ATP-Binding Cassette Proteins Involved in Glucose and Lipid Homeostasis." Bioscience, Biotechnology, and Biochemistry 74, no. 5 (May 23, 2010): 899–907. http://dx.doi.org/10.1271/bbb.90921.

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17

Xavier, Bala M., William J. Jennings, Aiman A. Zein, Junmei Wang, and Jyh-Yeuan Lee. "Structural snapshot of the cholesterol-transport ATP-binding cassette proteins." Biochemistry and Cell Biology 97, no. 3 (June 2019): 224–33. http://dx.doi.org/10.1139/bcb-2018-0151.

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18

Zoghbi, Maria E., and Guillermo A. Altenberg. "Luminescence resonance energy transfer spectroscopy of ATP-binding cassette proteins." Biochimica et Biophysica Acta (BBA) - Biomembranes 1860, no. 4 (April 2018): 854–67. http://dx.doi.org/10.1016/j.bbamem.2017.08.005.

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19

Hopfner, Karl‐Peter. "Invited review: Architectures and mechanisms of ATP binding cassette proteins." Biopolymers 105, no. 8 (May 20, 2016): 492–504. http://dx.doi.org/10.1002/bip.22843.

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20

Gulati, Sonali, Mohammed Jamshad, Timothy J. Knowles, Kerrie A. Morrison, Rebecca Downing, Natasha Cant, Richard Collins, et al. "Detergent-free purification of ABC (ATP-binding-cassette) transporters." Biochemical Journal 461, no. 2 (June 26, 2014): 269–78. http://dx.doi.org/10.1042/bj20131477.

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A styrene maleic acid copolymer can be effectively used to extract and purify large eukaryotic transmembrane proteins in the absence of detergents, forming small bilayer discs encapsulating the protein, which have great potential for future structure and function studies.

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21

Boyum, Rodney, and Guido Guidotti. "Effect of ATP Binding Cassette/Multidrug Resistance Proteins on ATP Efflux ofSaccharomyces cerevisiae." Biochemical and Biophysical Research Communications 230, no. 1 (January 1997): 22–26. http://dx.doi.org/10.1006/bbrc.1996.5913.

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22

Al-Awaida, Wajdy J., Hamzeh J. Al-Ameer, Ahmad Sharab, Ghizal Fatima, and Najah R. Hadi. "THE ATP-BINDING CASSETTE TRANSPORTER A1 GENE POLYMORPHISMS AND TYPE 2 DIABETES MELLITUS." Era's Journal of Medical Research 9, no. 1 (June 2022): 45–51. http://dx.doi.org/10.24041/ejmr2022.07.

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Insulin resistance (IR), secretion of insulin, and abnormalities of lipid metabolism are all markers of type 2 diabetes (T2DM), which is a progressive and complex metabolic disorder. Major risk factors for the development of T2DM were identified as genetic, environmental, and lifestyle factors. Several studies found that many genes contribute to T2DM susceptibility after glucose tolerance. Adenosine Binding Cassette Transporter Proteins 1 is a member of the ABC gene superfamily that is involved in cholesterol transport and HDL cholesterol (HDL-C) biosynthesis. Abnormal cholesterol metabolism, particularly high-density lipoprotein, has been related to genetic variations in the ABCA1 gene (HDL-C). Previous research suggested that ABCA1 gene polymorphisms may a hereditary risk factor for type 2 diabetes, along with lower HDLlevels in various populations.

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23

Locher, Kaspar P. "Structure and mechanism of ATP-binding cassette transporters." Philosophical Transactions of the Royal Society B: Biological Sciences 364, no. 1514 (October 28, 2008): 239–45. http://dx.doi.org/10.1098/rstb.2008.0125.

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ATP-binding cassette (ABC) transporters constitute a large superfamily of integral membrane proteins that includes both importers and exporters. In recent years, several structures of complete ABC transporters have been determined by X-ray crystallography. These structures suggest a mechanism by which binding and hydrolysis of ATP by the cytoplasmic, nucleotide-binding domains control the conformation of the transmembrane domains and therefore which side of the membrane the translocation pathway is exposed to. A basic, conserved two-state mechanism can explain active transport of both ABC importers and ABC exporters, but various questions remain unresolved. In this article, I will review some of the crystal structures and the mechanistic insight gained from them. Future challenges for a better understanding of the mechanism of ABC transporters will be outlined.

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24

López-Fernández, Luis A. "ATP-Binding Cassette Transporters in the Clinical Implementation of Pharmacogenetics." Journal of Personalized Medicine 8, no. 4 (December 5, 2018): 40. http://dx.doi.org/10.3390/jpm8040040.

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ATP-binding cassette (ABC) transporters are involved in a large number of processes and contribute to various human genetic diseases. Among other functions, ABC proteins are involved in the transport of multiple drugs through cells. Most of the genes coding for these transporters are highly polymorphic and DNA variants in these genes can affect the normal functioning of these proteins, affecting the way drugs are transported, increasing or decreasing drug levels. These changes in the intracellular and extracellular drug levels may be associated with altered drug effectiveness or severe drug-induced adverse events. This review presents a state-of-art of the most pharmacogenetics clinically relevant ABC transporters closed to the clinical implementation.

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25

Molinski, Steven V., Zoltán Bozóky, Surtaj H. Iram, and Saumel Ahmadi. "Biophysical Approaches Facilitate Computational Drug Discovery for ATP-Binding Cassette Proteins." International Journal of Medicinal Chemistry 2017 (March 19, 2017): 1–9. http://dx.doi.org/10.1155/2017/1529402.

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Although membrane proteins represent most therapeutically relevant drug targets, the availability of atomic resolution structures for this class of proteins has been limited. Structural characterization has been hampered by the biophysical nature of these polytopic transporters, receptors, and channels, and recent innovations to in vitro techniques aim to mitigate these challenges. One such class of membrane proteins, the ATP-binding cassette (ABC) superfamily, are broadly expressed throughout the human body, required for normal physiology and disease-causing when mutated, yet lacks sufficient structural representation in the Protein Data Bank. However, recent improvements to biophysical techniques (e.g., cryo-electron microscopy) have allowed for previously “hard-to-study” ABC proteins to be characterized at high resolution, providing insight into molecular mechanisms-of-action as well as revealing novel druggable sites for therapy design. These new advances provide ample opportunity for computational methods (e.g., virtual screening, molecular dynamics simulations, and structure-based drug design) to catalyze the discovery of novel small molecule therapeutics that can be easily translated from computer to bench and subsequently to the patient’s bedside. In this review, we explore the utility of recent advances in biophysical methods coupled with well-established in silico techniques towards drug development for diseases caused by dysfunctional ABC proteins.

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26

Ballerini, Patrizia, Patrizia Di Iorio, Renata Ciccarelli, Eleonora Nargi, Iolanda DʼAlimonte, Ugo Traversa, Michel P. Rathbone, and Francesco Caciagli. "Glial cells express multiple ATP binding cassette proteins which are involved in ATP release." NeuroReport 13, no. 14 (October 2002): 1789–92. http://dx.doi.org/10.1097/00001756-200210070-00019.

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27

Sauvage, Virginie, Dominique Aubert, Sandie Escotte-Binet, and Isabelle Villena. "The role of ATP-binding cassette (ABC) proteins in protozoan parasites." Molecular and Biochemical Parasitology 167, no. 2 (October 2009): 81–94. http://dx.doi.org/10.1016/j.molbiopara.2009.05.005.

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28

Bosch, Irene B., Zhen-Xi Wang, Liang-Feng Tao, and Charles B. Shoemaker. "Two Schistosoma mansoni cDNAs encoding ATP-binding cassette (ABC) family proteins." Molecular and Biochemical Parasitology 65, no. 2 (June 1994): 351–56. http://dx.doi.org/10.1016/0166-6851(94)90085-x.

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29

Kerr, I. D., E. D. Reynolds, and J. H. Cove. "ABC proteins and antibiotic drug resistance: is it all about transport?" Biochemical Society Transactions 33, no. 5 (October 26, 2005): 1000–1002. http://dx.doi.org/10.1042/bst0331000.

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The precise mechanism of antibiotic-resistance-conferring ABC (ATP-binding-cassette) proteins (termed NBD2) remains open to debate. Currently, two hypotheses are recognized. In one, the NBD2 proteins are envisaged to act at the ribosome to impair antibiotic access to the target site on the 23 S rRNA. In the other, NBD2 proteins are believed to act as the components of ATP driven efflux pumps by associating with membrane spanning proteins capable of binding and transporting antibiotics. Pertinent data in support of these two hypotheses are discussed in this paper.

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30

Van Der Does, Chris, and Robert Tampé. "How do ABC transporters drive transport?" Biological Chemistry 385, no. 10 (October 1, 2004): 927–33. http://dx.doi.org/10.1515/bc.2004.121.

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Abstract Members of the ATP-binding cassette (ABC) superfamily are integral membrane proteins that hydrolyze ATP to drive transport. In the last two decades these proteins have been extensively characterized on a genetic and biochemical level, and in recent years high-resolution crystal structures of several nucleotide-binding domains and full-length transporters have extended our knowledge. Here we discuss the possible mechanisms of transport that have been derived from these crystal structures and the extensive available biochemical data.

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31

Li, Xiangyu, Xiaolian Li, Xingcai Yang, Chengxiang Lan, Ying Huang, and Bin Jia. "Identification and characterization of ATP-Binding Cassette Transporters in Chlamydomonas reinhardtii." Marine Drugs 20, no. 10 (September 25, 2022): 603. http://dx.doi.org/10.3390/md20100603.

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Microalgae are promising microorganisms used to produce value-added products or to develop sustainable approaches for environmental remediation. The ATP-binding cassette proteins (ABCs) of Chlamydomonas reinhardtii have been characterized as indispensable transporters for CO2 concentrating mechanism, lipid biosynthesis, and heavy metal sequestration. However, few microalgal ABC proteins have been studied compared with higher plants or non-photosynthetic microorganisms. This study performed a genome-wide, evolutionary, and transcriptomic survey of C. reinhardtii ABC proteins (CrABCs). A total of 75 CrABCs were identified and classed into eight ABC subfamilies, from ABCA to ABCI. We found that no whole or partial genome duplication events occurred in C. reinhardtii after the ancient endosymbiosis events, but gene duplications occurred in a small range of chromosomal regions, which forced ABC family expansion. Abundant light, abscisic acid, and jasmonic acid response cis-elements were mapped in the CrABC promoters, coinciding with the evolutionary history of hormone signaling in Chlorophyta. The expression survey under light/dark rhythms revealed a close bond of CrABCs with cell division and development. A broad study of CrABCs supported their expected roles in heavy metal detoxiﬁcation, lipid metabolism, and environmental adaptation. Moreover, the evolutionary and expression survey predicted the functions of unknown CrABCs, which are elaborated in the text. Two half-size CrABCGs—CrABCG3 and CrABCG26—were described as plasma-membrane transporters that might participate in lipidic compound secretion. This study provides fundamental and exhaustive information about CrABCs, which are indispensable for the functional elucidation of ABC proteins in microalgae.

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32

Van Bibber, Michael, Clive Bradbeer, Nica Clark, and John R. Roth. "A New Class of Cobalamin Transport Mutants (btuF) Provides Genetic Evidence for a Periplasmic Binding Protein in Salmonella typhimurium." Journal of Bacteriology 181, no. 17 (September 1, 1999): 5539–41. http://dx.doi.org/10.1128/jb.181.17.5539-5541.1999.

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ABSTRACT No periplasmic binding protein has been demonstrated for the ATP-binding cassette (ABC)-type cobalamin transporter BtuCD. New mutations (btuF) are described that affect inner-membrane transport. The BtuF protein has a signal sequence and resembles the periplasmic binding proteins of several other ABC transporters.

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33

Arana, Maite Rocío, and Guillermo Alejandro Altenberg. "ATP-binding Cassette Exporters: Structure and Mechanism with a Focus on P-glycoprotein and MRP1." Current Medicinal Chemistry 26, no. 7 (May 14, 2019): 1062–78. http://dx.doi.org/10.2174/0929867324666171012105143.

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Background:Proteins that belong to the ATP-binding cassette superfamily include transporters that mediate the efflux of substrates from cells. Among these exporters, P-glycoprotein and MRP1 are involved in cancer multidrug resistance, protection from endo and xenobiotics, determination of drug pharmacokinetics, and the pathophysiology of a variety of disorders. Objective:To review the information available on ATP-binding cassette exporters, with a focus on Pglycoprotein, MRP1 and related proteins. We describe tissue localization and function of these transporters in health and disease, and discuss the mechanisms of substrate transport. We also correlate recent structural information with the function of the exporters, and discuss details of their molecular mechanism with a focus on the nucleotide-binding domains. Methods: Evaluation of selected publications on the structure and function of ATP-binding cassette proteins. Conclusions:Conformational changes on the nucleotide-binding domains side of the exporters switch the accessibility of the substrate-binding pocket between the inside and outside, which is coupled to substrate efflux. However, there is no agreement on the magnitude and nature of the changes at the nucleotide- binding domains side that drive the alternate-accessibility. Comparison of the structures of Pglycoprotein and MRP1 helps explain differences in substrate selectivity and the bases for polyspecificity. P-glycoprotein substrates are hydrophobic and/or weak bases, and polyspecificity is explained by a flexible hydrophobic multi-binding site that has a few acidic patches. MRP1 substrates are mostly organic acids, and its polyspecificity is due to a single bipartite binding site that is flexible and displays positive charge.

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Tanaka, Arowu R., Kouichi Tanabe, Masashi Morita, Mikinori Kurisu, Yoshinori Kasiwayama, Michinori Matsuo, Noriyuki Kioka, Teruo Amachi, Tsuneo Imanaka, and Kazumitsu Ueda. "ATP Binding/Hydrolysis by and Phosphorylation of Peroxisomal ATP-binding Cassette Proteins PMP70 (ABCD3) and Adrenoleukodystrophy Protein (ABCD1)." Journal of Biological Chemistry 277, no. 42 (August 9, 2002): 40142–47. http://dx.doi.org/10.1074/jbc.m205079200.

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35

Sharma, Parul, Navneet Singh, and Siddharth Sharma. "ATP binding cassette transporters and cancer: revisiting their controversial role." Pharmacogenomics 22, no. 18 (December 2021): 1211–35. http://dx.doi.org/10.2217/pgs-2021-0116.

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The expression of ATP-binding cassette transporter (ABC transporters) has been reported in various tissues such as the lung, liver, kidney, brain and intestine. These proteins account for the efflux of different compounds and metabolites across the membrane, thus decreasing the concentration of the toxic compounds. ABC transporter genes play a vital role in the development of multidrug resistance, which is the main obstacle that hinders the success of chemotherapy. Preclinical and clinical trials have investigated the probability of overcoming drug-associated resistance and substantial toxicities. The focus has been put on several strategies to overcome multidrug resistance. These strategies include the development of modulators that can modulate ABC transporters. This knowledge can be translated for clinical oncology treatment in the future.

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36

Altenberg, Guillermo. "Structure of Multidrug-Resistance Proteins of the ATP-Binding Cassette (ABC) Superfamily." Current Medicinal Chemistry-Anti-Cancer Agents 4, no. 1 (January 1, 2004): 53–62. http://dx.doi.org/10.2174/1568011043482160.

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37

Masereeuw, Rosalinde, and Frans G. M. Russel. "Regulatory Pathways for ATP-binding Cassette Transport Proteins in Kidney Proximal Tubules." AAPS Journal 14, no. 4 (September 8, 2012): 883–94. http://dx.doi.org/10.1208/s12248-012-9404-z.

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38

Aittoniemi, Jussi, Constantina Fotinou, Tim J. Craig, Heidi de Wet, Peter Proks, and Frances M. Ashcroft. "SUR1: a unique ATP-binding cassette protein that functions as an ion channel regulator." Philosophical Transactions of the Royal Society B: Biological Sciences 364, no. 1514 (November 6, 2008): 257–67. http://dx.doi.org/10.1098/rstb.2008.0142.

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SUR1 is an ATP-binding cassette (ABC) transporter with a novel function. In contrast to other ABC proteins, it serves as the regulatory subunit of an ion channel. The ATP-sensitive (K ATP ) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR1 subunits, and it links cell metabolism to electrical activity in many cell types. ATPase activity at the nucleotide-binding domains of SUR results in an increase in K ATP channel open probability. Conversely, ATP binding to Kir6.2 closes the channel. Metabolic regulation is achieved by the balance between these two opposing effects. Precisely how SUR1 talks to Kir6.2 remains unclear, but recent studies have identified some residues and domains that are involved in both physical and functional interactions between the two proteins. The importance of these interactions is exemplified by the fact that impaired regulation of Kir6.2 by SUR1 results in human disease, with loss-of-function SUR1 mutations causing congenital hyperinsulinism and gain-of-function SUR1 mutations leading to neonatal diabetes. This paper reviews recent data on the regulation of Kir6.2 by SUR1 and considers the molecular mechanisms by which SUR1 mutations produce disease.

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39

Linton, Kenneth J. "Structure and Function of ABC Transporters." Physiology 22, no. 2 (April 2007): 122–30. http://dx.doi.org/10.1152/physiol.00046.2006.

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ATP binding cassette transporters are ubiquitous integral membrane proteins that actively transport ligands across biological membranes, a process critical for most aspects of cell physiology. These proteins are important clinically and economically. Their dysfunction underlies a number of human genetic diseases, and the ability of some to pump cytotoxic molecules from cells confers resistance to antibiotics, herbicides, and chemotherapeutic drugs. Recent structure analyses interpreted in light of a large body of biochemistry has resulted in the ATP-switch model for function in which the paired nucleotide binding domains switch between an ATP-dependent closed conformation and a nucleotide-free, open conformation to drive the translocation of ligand.

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40

Zhestkova, M. A., and D. Yu Ovsyannikov. "GENETIC DISORDERS OF SURFACTANT PROTEINS." Pediatria. Journal named after G.N. Speransky 100, no. 5 (October 11, 2021): 82–89. http://dx.doi.org/10.24110/0031-403x-2021-100-5-82-89.

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The literature review provides up-to-date information on rare interstitial lung diseases, manifesting both in children, starting from the neonatal period, and in adults, – genetic disorders of surfactant proteins B, C, ATP-binding cassette protein A3 (ABCA3), manifested by such histopathological patterns, as chronic pneumonitis of infants, pulmonary alveolar proteinosis, desquamative interstitial pneumonia , nonspecific interstitial pneumonia. Information on epidemiology, genetics, pathogenesis, clinical picture, diagnosis and differential diagnosis, treatment of these diseases is given.

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41

Krzyzanowski, Damian, Marcin Kruszewski, and Agnieszka Grzelak. "Differential Action of Silver Nanoparticles on ABCB1 (MDR1) and ABCC1 (MRP1) Activity in Mammalian Cell Lines." Materials 14, no. 12 (June 18, 2021): 3383. http://dx.doi.org/10.3390/ma14123383.

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Silver nanoparticles (AgNPs), due to their unique properties have been receiving immense attention in recent years. In addition to their antibacterial and antifungal activities, AgNPs also cause apoptosis, mitochondria disfunction, nucleic acid damage and show potent anticancer properties in both multidrug resistance (MDR) and sensitive tumors. The MDR phenomenon, caused by the presence of ATP-binding cassette (ABC) proteins, is responsible for the failure of chemotherapy. Thus, investigating the influence of widely used AgNPs on ABC transporters is crucial. In the present study, we have examined the cytotoxicity of silver nanoparticles of a nominal size of 20 nm (Ag20) on the cell lines of different tissue origins. In addition, we have checked the ATP-binding cassette transporters’ activity and expression under AgNP exposure. The results indicate that Ag20 shows a toxic effect on tested cells, as well as modulating the expression and transport activity of ABC proteins.

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42

Wu, Chao, Swapan Chakrabarty, Minghui Jin, Kaiyu Liu, and Yutao Xiao. "Insect ATP-Binding Cassette (ABC) Transporters: Roles in Xenobiotic Detoxification and Bt Insecticidal Activity." International Journal of Molecular Sciences 20, no. 11 (June 10, 2019): 2829. http://dx.doi.org/10.3390/ijms20112829.

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ATP-binding cassette (ABC) transporters, a large class of transmembrane proteins, are widely found in organisms and play an important role in the transport of xenobiotics. Insect ABC transporters are involved in insecticide detoxification and Bacillus thuringiensis (Bt) toxin perforation. The complete ABC transporter is composed of two hydrophobic transmembrane domains (TMDs) and two nucleotide binding domains (NBDs). Conformational changes that are needed for their action are mediated by ATP hydrolysis. According to the similarity among their sequences and organization of conserved ATP-binding cassette domains, insect ABC transporters have been divided into eight subfamilies (ABCA–ABCH). This review describes the functions and mechanisms of ABC transporters in insecticide detoxification, plant toxic secondary metabolites transport and insecticidal activity of Bt toxin. With improved understanding of the role and mechanisms of ABC transporter in resistance to insecticides and Bt toxins, we can identify valuable target sites for developing new strategies to control pests and manage resistance and achieve green pest control.

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43

Dugourd, Dominique, Christine Martin, Clément R. Rioux, Mario Jacques, and Josée Harel. "Characterization of a Periplasmic ATP-Binding Cassette Iron Import System of Brachyspira(Serpulina) hyodysenteriae." Journal of Bacteriology 181, no. 22 (November 15, 1999): 6948–57. http://dx.doi.org/10.1128/jb.181.22.6948-6957.1999.

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ABSTRACT The nucleotide sequence of the pathogenic spirocheteBrachyspira hyodysenteriae bit (for “Brachyspira iron transport”) genomic region has been determined. The bit region is likely to encode an iron ATP-binding cassette transport system with some homology to those encountered in gram-negative bacteria. Six open reading frames oriented in the same direction and physically linked have been identified. This system possesses a protein containing ATP-binding motifs (BitD), two hydrophobic cytoplasmic membrane permeases (BitE and BitF), and at least three lipoproteins (BitA, BitB, and BitC) with homology to iron periplasmic binding proteins. These periplasmic binding proteins exhibit lipoprotein features. They are labeled by [3H]palmitate when tested in recombinantEscherichia coli, and their signal peptides are typical for substrates of the type II secretory peptidase. The FURTA system and Congo red assay indicate that BitB and BitC are involved in iron binding. The Bit system is detected only in B. hyodysenteriae and is absent from B. innocens andB. pilosicoli.

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44

Lau, Gloria H. Y., Ross T. A. MacGillivray, and Michael E. P. Murphy. "Characterization of a Nucleotide-Binding Domain Associated with Neisserial Iron Transport." Journal of Bacteriology 186, no. 10 (May 15, 2004): 3266–69. http://dx.doi.org/10.1128/jb.186.10.3266-3269.2004.

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ABSTRACT The fbpABC operon in Neisseria gonorrhoeae encodes an ATP-binding cassette transporter required for iron uptake from the host ferric binding proteins. The gene for the nucleotide-binding domain (fbpC) expressed in Escherichia coli has intrinsic ATPase activity (0.5 mmol/min/mg) uncoupled from the iron transport process. The FbpC E164D mutant is found to have a 10-fold reduction in specific activity. FbpC is covalently modified by 8-azido-[γ32P]ATP, indicating that FbpC is a functional ATPase that likely combines with FbpB to form a ferric iron transporter.

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45

Kay, Christopher, Katharine D. Woodward, Karen Lawler, Tim J. Self, Sabrina D. Dyall, and Ian D. Kerr. "The ATP-Binding Cassette Proteins of the Deep-Branching Protozoan Parasite Trichomonas vaginalis." PLoS Neglected Tropical Diseases 6, no. 6 (June 19, 2012): e1693. http://dx.doi.org/10.1371/journal.pntd.0001693.

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46

Omori, Kenji, and Akiko Idei. "Gram-negative bacterial atp-binding cassette protein exporter family and diverse secretory proteins." Journal of Bioscience and Bioengineering 95, no. 1 (January 2003): 1–12. http://dx.doi.org/10.1016/s1389-1723(03)80141-x.

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47

Hooiveld, Guido J. E. J., Jessica E. van Montfoort, Dirk K. F. Meijer, and Michael Müller. "Function and regulation of ATP-binding cassette transport proteins involved in hepatobiliary transport." European Journal of Pharmaceutical Sciences 12, no. 1 (November 2000): 13–30. http://dx.doi.org/10.1016/s0928-0987(00)00186-x.

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48

Hooiveld, Guido J. E. J., Jessica E. van Montfoort, Dirk K. F. Meijer, and Michael Müller. "Function and regulation of ATP-binding cassette transport proteins involved in hepatobiliary transport." European Journal of Pharmaceutical Sciences 12, no. 4 (February 2001): 525–43. http://dx.doi.org/10.1016/s0928-0987(01)00101-4.

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49

OMORI, KENJI, and AKIKO IDEI. "Gram-Negative Bacterial ATP-Binding Cassette Protein Exporter Family and Diverse Secretory Proteins." Journal of Bioscience and Bioengineering 95, no. 1 (2003): 1–12. http://dx.doi.org/10.1263/jbb.95.1.

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50

Braiterman, L. "Suppression of peroxisomal membrane protein defects by peroxisomal ATP binding cassette (ABC) proteins." Human Molecular Genetics 7, no. 2 (February 1, 1998): 239–47. http://dx.doi.org/10.1093/hmg/7.2.239.

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