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Proteins represent one of the most abundant classes of biological macromolecules and play crucial roles in a vast array of physiological and pathological processes. The knowledge of the 3D structure of a protein, as well as the possible conformational transitions occurring upon interaction with diverse ligands, are essential to fully comprehend its biological function.In addition to globular, well-folded proteins, over the past few years, intrinsically disordered proteins (IDPs) have received a lot of attention. IDPs are usually aggregation-prone and may form toxic amyloid fibers and oligomers associated with several human pathologies. Peptides are smaller in size than proteins but similarly represent key elements of cells. A few peptides are able to work as tumor markers and find applications in the diagnostic and therapeutic fields. The conformational analysis of bioactive peptides is important to design novel potential drugs acting as selective modulators of specific receptors or enzymes. Nevertheless, synthetic peptides reproducing different protein fragments have frequently been implemented as model systems in folding studies relying on structural investigations in water and/or other environments.This book contains contributions (seven original research articles and five reviews published in the journal Molecules) on the above-described topics and, in detail, it includes structural studies on globular folded proteins, IDPs and bioactive peptides. These works were conducted usingdifferent experimental methods.

Research & information: general --- mass spectrometric epitope mapping --- gas phase immune complex dissociation --- apparent gas phase dissociation constants --- apparent gas phase activation energies --- ITEM-TWO --- native mass spectrometry --- TRIOBP --- cancer --- deafness --- hearing loss --- mental illness --- schizophrenia --- actin --- cytoskeleton --- disordered structure --- protein aggregation --- solid-state NMR --- ELDOR-detected NMR --- ATP hydrolysis --- ATP analogues --- DnaB helicase --- ABC transporter --- biopesticides --- antifungal activity --- insecticidal activity --- mechanism of action --- transgenic crops --- protein folding --- NMR --- High Hydrostatic Pressure --- ACE2 --- viral spike receptor-binding domain --- SARS-CoV-2 --- transmission --- bioinformatics --- IDP 1 --- binding 2 --- molecular dynamics 3 --- MELD×MD 4 --- advanced sampling 5 --- p53 6 --- MDM2 7 --- NAD(P)H-dependent oxidoreductase --- zinc-containing alcohol dehydrogenase --- cofactor binding and release --- interdomain cleft dynamics --- molecular dynamics simulations --- denatured state ensemble --- protein coil library --- peptides --- intrinsically disordered proteins --- ion-pairing interaction --- side-chain length --- charged amino acids --- β-hairpin --- peptide --- Friedman’s test --- backbone atom coordinate variances and uncertainties --- superimposition --- nanobody --- protein structure --- immunoglobulin domain --- n/a --- Friedman's test

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Proteins represent one of the most abundant classes of biological macromolecules and play crucial roles in a vast array of physiological and pathological processes. The knowledge of the 3D structure of a protein, as well as the possible conformational transitions occurring upon interaction with diverse ligands, are essential to fully comprehend its biological function.In addition to globular, well-folded proteins, over the past few years, intrinsically disordered proteins (IDPs) have received a lot of attention. IDPs are usually aggregation-prone and may form toxic amyloid fibers and oligomers associated with several human pathologies. Peptides are smaller in size than proteins but similarly represent key elements of cells. A few peptides are able to work as tumor markers and find applications in the diagnostic and therapeutic fields. The conformational analysis of bioactive peptides is important to design novel potential drugs acting as selective modulators of specific receptors or enzymes. Nevertheless, synthetic peptides reproducing different protein fragments have frequently been implemented as model systems in folding studies relying on structural investigations in water and/or other environments.This book contains contributions (seven original research articles and five reviews published in the journal Molecules) on the above-described topics and, in detail, it includes structural studies on globular folded proteins, IDPs and bioactive peptides. These works were conducted usingdifferent experimental methods.

mass spectrometric epitope mapping --- gas phase immune complex dissociation --- apparent gas phase dissociation constants --- apparent gas phase activation energies --- ITEM-TWO --- native mass spectrometry --- TRIOBP --- cancer --- deafness --- hearing loss --- mental illness --- schizophrenia --- actin --- cytoskeleton --- disordered structure --- protein aggregation --- solid-state NMR --- ELDOR-detected NMR --- ATP hydrolysis --- ATP analogues --- DnaB helicase --- ABC transporter --- biopesticides --- antifungal activity --- insecticidal activity --- mechanism of action --- transgenic crops --- protein folding --- NMR --- High Hydrostatic Pressure --- ACE2 --- viral spike receptor-binding domain --- SARS-CoV-2 --- transmission --- bioinformatics --- IDP 1 --- binding 2 --- molecular dynamics 3 --- MELD×MD 4 --- advanced sampling 5 --- p53 6 --- MDM2 7 --- NAD(P)H-dependent oxidoreductase --- zinc-containing alcohol dehydrogenase --- cofactor binding and release --- interdomain cleft dynamics --- molecular dynamics simulations --- denatured state ensemble --- protein coil library --- peptides --- intrinsically disordered proteins --- ion-pairing interaction --- side-chain length --- charged amino acids --- β-hairpin --- peptide --- Friedman’s test --- backbone atom coordinate variances and uncertainties --- superimposition --- nanobody --- protein structure --- immunoglobulin domain --- n/a --- Friedman's test

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Mammalian ATP-binding cassette (ABC) transporters constitute a superfamily of proteins involved in many essential cellular processes. Most of these transporters are transmembrane proteins and allow the active transport of solutes, small molecules, and lipids across biological membranes. On the one hand, some of these transporters are involved in drug resistance (also referred to as MDR or multidrug resistance), a process known to be a major brake in most anticancer treatments, and the medical challenge is thus to specifically inhibit their function. On the other hand, molecular defects in some of these ABC transporters are correlated with several rare human diseases, the most well-documented of which being cystic fibrosis, which is caused by genetic variations in ABCC7/CFTR (cystic fibrosis transmembrane conductance regulator). In the latter case, the goal is to rescue the function of the deficient transporters using various means, such as targeted pharmacotherapies and cell or gene therapy. The aim of this Special Issue, “ABC Transporters in Human Diseases”, is to present, through original articles and reviews, the state-of-the-art of our current knowledge about the role of ABC transporters in human diseases and the proposed therapeutic options based on studies ranging from cell and animal models to patients.

Research & information: general --- Biology, life sciences --- ABC transporters --- drug action --- regulatory extension --- regulatory insertion --- mechanism of action --- MRP1 --- MRP4 --- breast cancer --- proliferation --- migration --- invasion --- cAMP --- ABCG2 --- ABCB1 --- blood-brain barrier --- PET --- Alzheimer's disease --- beta-amyloid --- tariquidar --- erlotinib --- ABCG5 --- ABCG8 --- ATP-binding cassette transporter --- cholesterol --- polar relay --- sitosterolemia --- 5' untranslated region --- cis-acting elements --- ABCA subfamily --- bioinformatics --- ABC transporter --- therapy response --- disease-free survival --- next-generation sequencing --- competitive allele-specific PCR --- P-glycoprotein --- amyloid-beta --- neuron --- SK-N-SH --- gene therapy --- AAV --- PFIC --- BSEP --- ABCB11 --- bile salts --- intrahepatic cholestasis --- chaperones --- PFIC2 --- BRIC --- ATP-binding cassette transporter A1 (ABCA1) --- cholesterol homeostasis --- reverse cholesterol transport --- HDL-C --- dyslipidemia --- type 2 diabetes --- microparticles --- ABCG2 genotype --- clinico-genetic analysis --- ethnic specificity --- genetic variations --- precision medicine --- rare variant --- Roma --- serum uric acid --- SUA-lowering therapy --- urate transporter --- bile secretion --- ABCB4 --- ABCC2 --- ABCG5/G8 --- molecular partners --- phytosterol --- xenosterol --- atherosclerosis --- gall stone --- ABC --- transporter --- ABC (ATP-binding cassette) transporters --- multidrug resistance --- transport --- trafficking --- urate --- mutations --- polymorphisms --- ABCC6 --- TNAP --- NT5E --- Pseudoxanthoma elasticum (PXE) --- cancer --- membrane protein --- functional divergence --- calcification --- pseudoxanthoma elasticum --- generalized arterial calcification of infancy --- pyrophosphate --- therapies --- ABCA7 --- phagocytosis --- Aβ peptides --- yeast --- multidrug transporter --- anticancer --- antifungal resistance --- mechanism --- peroxisome --- adrenoleukodystrophy --- fatty acids --- gout --- early-onset gout --- hyperuricemia --- uric acid --- BCRP --- single nucleotide polymorphism --- SNP --- homology modeling --- substrate-binding site --- cellular ATP efflux --- mutagenesis --- intracellular traffic --- MDR3 --- phosphatidylcholine --- RAB GTPase --- taxol --- drug transport --- ABC transporters --- drug action --- regulatory extension --- regulatory insertion --- mechanism of action --- MRP1 --- MRP4 --- breast cancer --- proliferation --- migration --- invasion --- cAMP --- ABCG2 --- ABCB1 --- blood-brain barrier --- PET --- Alzheimer's disease --- beta-amyloid --- tariquidar --- erlotinib --- ABCG5 --- ABCG8 --- ATP-binding cassette transporter --- cholesterol --- polar relay --- sitosterolemia --- 5' untranslated region --- cis-acting elements --- ABCA subfamily --- bioinformatics --- ABC transporter --- therapy response --- disease-free survival --- next-generation sequencing --- competitive allele-specific PCR --- P-glycoprotein --- amyloid-beta --- neuron --- SK-N-SH --- gene therapy --- AAV --- PFIC --- BSEP --- ABCB11 --- bile salts --- intrahepatic cholestasis --- chaperones --- PFIC2 --- BRIC --- ATP-binding cassette transporter A1 (ABCA1) --- cholesterol homeostasis --- reverse cholesterol transport --- HDL-C --- dyslipidemia --- type 2 diabetes --- microparticles --- ABCG2 genotype --- clinico-genetic analysis --- ethnic specificity --- genetic variations --- precision medicine --- rare variant --- Roma --- serum uric acid --- SUA-lowering therapy --- urate transporter --- bile secretion --- ABCB4 --- ABCC2 --- ABCG5/G8 --- molecular partners --- phytosterol --- xenosterol --- atherosclerosis --- gall stone --- ABC --- transporter --- ABC (ATP-binding cassette) transporters --- multidrug resistance --- transport --- trafficking --- urate --- mutations --- polymorphisms --- ABCC6 --- TNAP --- NT5E --- Pseudoxanthoma elasticum (PXE) --- cancer --- membrane protein --- functional divergence --- calcification --- pseudoxanthoma elasticum --- generalized arterial calcification of infancy --- pyrophosphate --- therapies --- ABCA7 --- phagocytosis --- Aβ peptides --- yeast --- multidrug transporter --- anticancer --- antifungal resistance --- mechanism --- peroxisome --- adrenoleukodystrophy --- fatty acids --- gout --- early-onset gout --- hyperuricemia --- uric acid --- BCRP --- single nucleotide polymorphism --- SNP --- homology modeling --- substrate-binding site --- cellular ATP efflux --- mutagenesis --- intracellular traffic --- MDR3 --- phosphatidylcholine --- RAB GTPase --- taxol --- drug transport

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Mammalian ATP-binding cassette (ABC) transporters constitute a superfamily of proteins involved in many essential cellular processes. Most of these transporters are transmembrane proteins and allow the active transport of solutes, small molecules, and lipids across biological membranes. On the one hand, some of these transporters are involved in drug resistance (also referred to as MDR or multidrug resistance), a process known to be a major brake in most anticancer treatments, and the medical challenge is thus to specifically inhibit their function. On the other hand, molecular defects in some of these ABC transporters are correlated with several rare human diseases, the most well-documented of which being cystic fibrosis, which is caused by genetic variations in ABCC7/CFTR (cystic fibrosis transmembrane conductance regulator). In the latter case, the goal is to rescue the function of the deficient transporters using various means, such as targeted pharmacotherapies and cell or gene therapy. The aim of this Special Issue, “ABC Transporters in Human Diseases”, is to present, through original articles and reviews, the state-of-the-art of our current knowledge about the role of ABC transporters in human diseases and the proposed therapeutic options based on studies ranging from cell and animal models to patients.

ABC transporters --- drug action --- regulatory extension --- regulatory insertion --- mechanism of action --- MRP1 --- MRP4 --- breast cancer --- proliferation --- migration --- invasion --- cAMP --- ABCG2 --- ABCB1 --- blood-brain barrier --- PET --- Alzheimer’s disease --- beta-amyloid --- tariquidar --- erlotinib --- ABCG5 --- ABCG8 --- ATP-binding cassette transporter --- cholesterol --- polar relay --- sitosterolemia --- 5′ untranslated region --- cis-acting elements --- ABCA subfamily --- bioinformatics --- ABC transporter --- therapy response --- disease-free survival --- next-generation sequencing --- competitive allele-specific PCR --- P-glycoprotein --- amyloid-beta --- neuron --- SK-N-SH --- gene therapy --- AAV --- PFIC --- BSEP --- ABCB11 --- bile salts --- intrahepatic cholestasis --- chaperones --- PFIC2 --- BRIC --- ATP-binding cassette transporter A1 (ABCA1) --- cholesterol homeostasis --- reverse cholesterol transport --- HDL-C --- dyslipidemia --- type 2 diabetes --- microparticles --- ABCG2 genotype --- clinico-genetic analysis --- ethnic specificity --- genetic variations --- precision medicine --- rare variant --- Roma --- serum uric acid --- SUA-lowering therapy --- urate transporter --- bile secretion --- ABCB4 --- ABCC2 --- ABCG5/G8 --- molecular partners --- phytosterol --- xenosterol --- atherosclerosis --- gall stone --- ABC --- transporter --- ABC (ATP-binding cassette) transporters --- multidrug resistance --- transport --- trafficking --- urate --- mutations --- polymorphisms --- ABCC6 --- TNAP --- NT5E --- Pseudoxanthoma elasticum (PXE) --- cancer --- membrane protein --- functional divergence --- calcification --- pseudoxanthoma elasticum --- generalized arterial calcification of infancy --- pyrophosphate --- therapies --- ABCA7 --- phagocytosis --- Aβ peptides --- yeast --- multidrug transporter --- anticancer --- antifungal resistance --- mechanism --- peroxisome --- adrenoleukodystrophy --- fatty acids --- gout --- early-onset gout --- hyperuricemia --- uric acid --- BCRP --- single nucleotide polymorphism --- SNP --- homology modeling --- substrate-binding site --- cellular ATP efflux --- mutagenesis --- intracellular traffic --- MDR3 --- phosphatidylcholine --- RAB GTPase --- taxol --- drug transport --- n/a --- Alzheimer's disease --- 5' untranslated region

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Mitochondrial transporters are membrane-inserted proteins which provide a link between metabolic reactions occurring within the mitochondrial matrix and outside the organelles by catalyzing the translocation of numerous solutes across the mitochondrial membrane. They include the mitochondrial carrier family members, the proteins involved in pyruvate transport, ABC transporters and channels, and are, therefore, essential for many biological processes and cell homeostasis. Identification and functional studies of many mitochondrial transporters have been performed over the years using both in vitro and in vivo systems. The few recently solved structures of these transporters have paved the way for further investigations. Furthermore, alterations in their function are responsible for several diseases.

Research & information: general --- Biology, life sciences --- hypoxia --- resistance to hypoxia --- mitochondria --- mitochondrial calcium transport --- mitochondrial calcium uniporter complex --- mitochondrial Ca2+-induced permeability transition pore --- cyclophilin D --- ATP synthase --- disease --- error of metabolism --- mitochondrial carrier --- mitochondrial carrier disease --- mitochondrial disease --- mitochondrial transporter --- membrane transport --- mutation --- SLC25. --- mitochondrial permeability transition --- apoptosis --- necrosis --- ischemia/reperfusion --- cancer --- neurodegeneration --- cyclosporin A --- metabolite transport --- mitochondrial pyruvate carrier --- sideroflexin --- TOM --- TIM chaperones --- TIM22 --- protein translocation --- mitochondrial biogenesis --- amino acid --- biological function --- ion --- inner mitochondrial membrane --- mitochondrial carrier family --- organic acid --- substrate specificity --- transport mechanism --- vitamin --- USMG5/DAPIT --- glucose-stimulated insulin secretion --- glucose-induced expression --- membrane subunits of ATP synthase --- ATP synthase oligomers mitochondrial cristae morphology --- metabolism --- metabolic disorders --- adult-onset type II citrullinemia (CTLN2) --- aspartate/glutamate carrier (AGC) --- animal model --- argininosuccinate synthetase (ASS) --- aversion to carbohydrates --- citrin --- food taste --- neonatal intrahepatic cholestasis caused by citrin deficiency (NICCD) --- protein–protein interaction --- MPC --- lifespan --- pyruvate metabolism --- mitochondrial transport --- peroxisomes --- carrier --- cofactor --- ABC transporter --- aquaporin --- ion channels --- potassium channels --- ATP --- calcium --- ROS --- potassium channel openers --- MCF --- function --- plant metabolism --- plant development --- diseases --- VDAC1 --- virus --- pancreatic islets --- β-cell --- diabetes --- glucotoxicity --- glucolipotoxicity --- lipotoxicity --- mitochondrial carriers --- SLC transporters --- SLC25 --- SLC54 --- SLC55 --- LETM --- SLC56 --- sequence analysis --- protein targeting --- Voltage-Dependent Anion selective Channel --- isoforms --- oxidative post-translational modification --- gene promoter --- yeast --- bioenergetics --- SLC25A1 --- CIC --- CTP --- citrate --- inflammation --- 22.q11.2 --- NAFLD/NASH --- carnitine --- carnitine acyl-carnitine carrier --- carnitine acyl-carnitine translocase --- post-translational modification --- solute carrier family 25 --- SLC25A20 --- MCU --- mitochondrial Ca2+ uniporter --- Ca2+ signaling --- mitochondrial metabolism --- skeletal muscle mitochondria --- SLC25A51 --- NAD+ transporters --- NAD --- electrophysiology --- ATP-dependent potassium channel --- hypoxia --- resistance to hypoxia --- mitochondria --- mitochondrial calcium transport --- mitochondrial calcium uniporter complex --- mitochondrial Ca2+-induced permeability transition pore --- cyclophilin D --- ATP synthase --- disease --- error of metabolism --- mitochondrial carrier --- mitochondrial carrier disease --- mitochondrial disease --- mitochondrial transporter --- membrane transport --- mutation --- SLC25. --- mitochondrial permeability transition --- apoptosis --- necrosis --- ischemia/reperfusion --- cancer --- neurodegeneration --- cyclosporin A --- metabolite transport --- mitochondrial pyruvate carrier --- sideroflexin --- TOM --- TIM chaperones --- TIM22 --- protein translocation --- mitochondrial biogenesis --- amino acid --- biological function --- ion --- inner mitochondrial membrane --- mitochondrial carrier family --- organic acid --- substrate specificity --- transport mechanism --- vitamin --- USMG5/DAPIT --- glucose-stimulated insulin secretion --- glucose-induced expression --- membrane subunits of ATP synthase --- ATP synthase oligomers mitochondrial cristae morphology --- metabolism --- metabolic disorders --- adult-onset type II citrullinemia (CTLN2) --- aspartate/glutamate carrier (AGC) --- animal model --- argininosuccinate synthetase (ASS) --- aversion to carbohydrates --- citrin --- food taste --- neonatal intrahepatic cholestasis caused by citrin deficiency (NICCD) --- protein–protein interaction --- MPC --- lifespan --- pyruvate metabolism --- mitochondrial transport --- peroxisomes --- carrier --- cofactor --- ABC transporter --- aquaporin --- ion channels --- potassium channels --- ATP --- calcium --- ROS --- potassium channel openers --- MCF --- function --- plant metabolism --- plant development --- diseases --- VDAC1 --- virus --- pancreatic islets --- β-cell --- diabetes --- glucotoxicity --- glucolipotoxicity --- lipotoxicity --- mitochondrial carriers --- SLC transporters --- SLC25 --- SLC54 --- SLC55 --- LETM --- SLC56 --- sequence analysis --- protein targeting --- Voltage-Dependent Anion selective Channel --- isoforms --- oxidative post-translational modification --- gene promoter --- yeast --- bioenergetics --- SLC25A1 --- CIC --- CTP --- citrate --- inflammation --- 22.q11.2 --- NAFLD/NASH --- carnitine --- carnitine acyl-carnitine carrier --- carnitine acyl-carnitine translocase --- post-translational modification --- solute carrier family 25 --- SLC25A20 --- MCU --- mitochondrial Ca2+ uniporter --- Ca2+ signaling --- mitochondrial metabolism --- skeletal muscle mitochondria --- SLC25A51 --- NAD+ transporters --- NAD --- electrophysiology --- ATP-dependent potassium channel