The Experts below are selected from a list of 324 Experts worldwide ranked by ideXlab platform
Christian Gotting - One of the best experts on this subject based on the ideXlab platform.
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new insights into the pathogenesis of pseudoxanthoma elasticum and related soft tissue calcification disorders by identifying genetic interactions and modifiers
Frontiers in Genetics, 2013Co-Authors: Doris Hendig, Cornelius Knabbe, Christian GottingAbstract:Screening of the ATP binding cassette transporter Protein Subfamily C member 6 gene (ABCC6) in Pseudoxanthoma elasticum (PXE) revealed a mutation detection rate of approximately 87%. Although 25% of the unidentified disease alleles underlie deletions/insertions, there remain several PXE patients with no clear genotype. The recent identification of PXE-related diseases and the high intra-familiar and inter-individual clinical variability of PXE led to the assumption that secondary genetic cofactors exist. Here, we summarize current knowledge of the genetics underlying PXE and PXE-related disorders based on human and animal studies. Furthermore, we discuss the role of genetic interactions and modifier genes in PXE and PXE-related diseases characterized by soft tissue calcification.
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New insights into the pathogenesis of pseudoxanthoma elasticum and related soft tissue calcification disorders by identifying genetic interactions and modifiers.
Frontiers in genetics, 2013Co-Authors: Doris Hendig, Cornelius Knabbe, Christian GottingAbstract:Screening of the adenosine triphosphate binding cassette transporter Protein Subfamily C member 6 gene (ABCC6) in pseudoxanthoma elasticum (PXE) revealed a mutation detection rate of approximately 87%. Although 25% of the unidentified disease alleles underlie deletions/insertions, there remain several PXE patients with no clear genotype. The recent identification of PXE-related diseases and the high intra-familiar and inter-individual clinical variability of PXE led to the assumption that secondary genetic co-factors exist. Here, we summarize current knowledge of the genetics underlying PXE and PXE-related disorders based on human and animal studies. Furthermore, we discuss the role of genetic interactions and modifier genes in PXE and PXE-related diseases characterized by soft tissue calcification.
Doris Hendig - One of the best experts on this subject based on the ideXlab platform.
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new insights into the pathogenesis of pseudoxanthoma elasticum and related soft tissue calcification disorders by identifying genetic interactions and modifiers
Frontiers in Genetics, 2013Co-Authors: Doris Hendig, Cornelius Knabbe, Christian GottingAbstract:Screening of the ATP binding cassette transporter Protein Subfamily C member 6 gene (ABCC6) in Pseudoxanthoma elasticum (PXE) revealed a mutation detection rate of approximately 87%. Although 25% of the unidentified disease alleles underlie deletions/insertions, there remain several PXE patients with no clear genotype. The recent identification of PXE-related diseases and the high intra-familiar and inter-individual clinical variability of PXE led to the assumption that secondary genetic cofactors exist. Here, we summarize current knowledge of the genetics underlying PXE and PXE-related disorders based on human and animal studies. Furthermore, we discuss the role of genetic interactions and modifier genes in PXE and PXE-related diseases characterized by soft tissue calcification.
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New insights into the pathogenesis of pseudoxanthoma elasticum and related soft tissue calcification disorders by identifying genetic interactions and modifiers.
Frontiers in genetics, 2013Co-Authors: Doris Hendig, Cornelius Knabbe, Christian GottingAbstract:Screening of the adenosine triphosphate binding cassette transporter Protein Subfamily C member 6 gene (ABCC6) in pseudoxanthoma elasticum (PXE) revealed a mutation detection rate of approximately 87%. Although 25% of the unidentified disease alleles underlie deletions/insertions, there remain several PXE patients with no clear genotype. The recent identification of PXE-related diseases and the high intra-familiar and inter-individual clinical variability of PXE led to the assumption that secondary genetic co-factors exist. Here, we summarize current knowledge of the genetics underlying PXE and PXE-related disorders based on human and animal studies. Furthermore, we discuss the role of genetic interactions and modifier genes in PXE and PXE-related diseases characterized by soft tissue calcification.
Cornelius Knabbe - One of the best experts on this subject based on the ideXlab platform.
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new insights into the pathogenesis of pseudoxanthoma elasticum and related soft tissue calcification disorders by identifying genetic interactions and modifiers
Frontiers in Genetics, 2013Co-Authors: Doris Hendig, Cornelius Knabbe, Christian GottingAbstract:Screening of the ATP binding cassette transporter Protein Subfamily C member 6 gene (ABCC6) in Pseudoxanthoma elasticum (PXE) revealed a mutation detection rate of approximately 87%. Although 25% of the unidentified disease alleles underlie deletions/insertions, there remain several PXE patients with no clear genotype. The recent identification of PXE-related diseases and the high intra-familiar and inter-individual clinical variability of PXE led to the assumption that secondary genetic cofactors exist. Here, we summarize current knowledge of the genetics underlying PXE and PXE-related disorders based on human and animal studies. Furthermore, we discuss the role of genetic interactions and modifier genes in PXE and PXE-related diseases characterized by soft tissue calcification.
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New insights into the pathogenesis of pseudoxanthoma elasticum and related soft tissue calcification disorders by identifying genetic interactions and modifiers.
Frontiers in genetics, 2013Co-Authors: Doris Hendig, Cornelius Knabbe, Christian GottingAbstract:Screening of the adenosine triphosphate binding cassette transporter Protein Subfamily C member 6 gene (ABCC6) in pseudoxanthoma elasticum (PXE) revealed a mutation detection rate of approximately 87%. Although 25% of the unidentified disease alleles underlie deletions/insertions, there remain several PXE patients with no clear genotype. The recent identification of PXE-related diseases and the high intra-familiar and inter-individual clinical variability of PXE led to the assumption that secondary genetic co-factors exist. Here, we summarize current knowledge of the genetics underlying PXE and PXE-related disorders based on human and animal studies. Furthermore, we discuss the role of genetic interactions and modifier genes in PXE and PXE-related diseases characterized by soft tissue calcification.
Tsuneo Imanaka - One of the best experts on this subject based on the ideXlab platform.
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Characterization of human ATP-binding cassette Protein Subfamily D reconstituted into proteoliposomes.
Biochemical and biophysical research communications, 2018Co-Authors: Takumi Okamoto, Kosuke Kawaguchi, Shiro Watanabe, Rina Agustina, Toshiki Ikejima, Keisuke Ikeda, Minoru Nakano, Masashi Morita, Tsuneo ImanakaAbstract:Abstract In mammals, four ATP-binding cassette (ABC) Proteins belonging to Subfamily D have been identified. ABCD1‒3 are located on peroxisomal membrane and play an important role in the transportation of various fatty acid-CoA derivatives, including very long chain fatty acid-CoA, into peroxisomes. ABCD4 is located on lysosomal membrane and is suggested to be involved in the transport of vitamin B12 from lysosomes to the cytosol. However, the precise transport mechanism by which these ABC transporters facilitate the import or export of substrate has yet to be well elucidated. In this study, the overexpression of human ABCD1‒4 in the methylotrophic yeast Pichia pastoris and a purification procedure were developed. The detergent-solubilized Proteins were reconstituted into liposomes. ABCD1‒4 displayed stable ATPase activity, which was inhibited by AlF3. Furthermore, ABCD1‒4 were found to possess an equal levels of acyl-CoA thioesterase activity. Proteoliposomes is expected to be an aid in the further biochemical characterization of ABCD transporters.
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Role of NH2-terminal hydrophobic motif in the subcellular localization of ATP-binding cassette Protein Subfamily D: common features in eukaryotic organisms.
Biochemical and biophysical research communications, 2014Co-Authors: Asaka Lee, Takumi Okamoto, Kosuke Kawaguchi, Tsuneo Imanaka, Kota Asahina, Dzmitry G. Kostsin, Yoshinori Kashiwayama, Kojiro Takanashi, Kazufumi Yazaki, Masashi MoritaAbstract:Abstract In mammals, four ATP-binding cassette (ABC) Proteins belonging to Subfamily D have been identified. ABCD1–3 possesses the NH 2 -terminal hydrophobic region and are targeted to peroxisomes, while ABCD4 lacking the region is targeted to the endoplasmic reticulum (ER). Based on hydropathy plot analysis, we found that several eukaryotes have ABCD Protein homologs lacking the NH 2 -terminal hydrophobic segment (H0 motif). To investigate whether the role of the NH 2 -terminal H0 motif in subcellular localization is conserved across species, we expressed ABCD Proteins from several species (metazoan, plant and fungi) in fusion with GFP in CHO cells and examined their subcellular localization. ABCD Proteins possessing the NH 2 -terminal H0 motif were localized to peroxisomes, while ABCD Proteins lacking this region lost this capacity. In addition, the deletion of the NH 2 -terminal H0 motif of ABCD Protein resulted in their localization to the ER. These results suggest that the role of the NH 2 -terminal H0 motif in organelle targeting is widely conserved in living organisms.
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70 kda peroxisomal membrane Protein related Protein p70r abcd4 localizes to endoplasmic reticulum not peroxisomes and nh2 terminal hydrophobic property determines the subcellular localization of abc Subfamily d Proteins
Experimental Cell Research, 2009Co-Authors: Yoshinori Kashiwayama, Masashi Morita, Midori Seki, Akina Yasui, Yoshiyuki Murasaki, Yukari Yamashita, Masao Sakaguchi, Yoshitaka Tanaka, Tsuneo ImanakaAbstract:70-kDa peroxisomal membrane Protein related Protein (P70R/ABCD4) is a member of ATP-binding cassette (ABC) Protein Subfamily D. ABC Subfamily D Proteins are also known as peroxisomal ABC Proteins. Therefore, P70R is thought to be a peroxisomal membrane Protein. However, the subcellular localization of P70R is not extensively investigated. In this study, we transiently expressed P70R in fusion with HA (P70R-HA) in CHO cells and examined subcellular localization by immunofluorescence. Surprisingly, P70R-HA was localized to the endoplasmic reticulum (ER), not to peroxisomes. To examine the ER-targeting property of P70R, we expressed various NH2-terminal deletion constructs of P70R. Among the NH2-terminal deletion constructs, mutant Proteins starting with hydrophobic transmembrane segment (TMS) were localized to ER, but the ones containing the NH2-terminal hydrophilic cytosolic domain were not. ABC Subfamily D Proteins destined for peroxisomes have NH2-terminal hydrophilic region adjacent to TMS1. However, only P70R lacks the region and is translated with NH2-terminal hydrophobic TMS1. Furthermore, attachment of the NH2-terminal hydrophilic domain to the NH2-terminus of P70R excluded P70R from the ER-targeting pathway. These data suggest that P70R resides in the ER but not the peroxisomal membranes, and the hydrophobic property of NH2-terminal region determines the subcellular localization of ABC Subfamily D Proteins.
Héctor Riveros-rosas - One of the best experts on this subject based on the ideXlab platform.
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Diversity and Evolutionary Analysis of Iron-Containing (Type-III) Alcohol Dehydrogenases in Eukaryotes.
PloS one, 2016Co-Authors: Carlos Gaona-lópez, Adriana Julián-sánchez, Héctor Riveros-rosasAbstract:Alcohol dehydrogenase (ADH) activity is widely distributed in the three domains of life. Currently, there are three non-homologous NAD(P)+-dependent ADH families reported: Type I ADH comprises Zn-dependent ADHs; type II ADH comprises short-chain ADHs described first in Drosophila; and, type III ADH comprises iron-containing ADHs (FeADHs). These three families arose independently throughout evolution and possess different structures and mechanisms of reaction. While types I and II ADHs have been extensively studied, analyses about the evolution and diversity of (type III) FeADHs have not been published yet. Therefore in this work, a phylogenetic analysis of FeADHs was performed to get insights into the evolution of this Protein family, as well as explore the diversity of FeADHs in eukaryotes. Results showed that FeADHs from eukaryotes are distributed in thirteen Protein subfamilies, eight of them possessing Protein sequences distributed in the three domains of life. Interestingly, none of these Protein subfamilies possess Protein sequences found simultaneously in animals, plants and fungi. Many FeADHs are activated by or contain Fe2+, but many others bind to a variety of metals, or even lack of metal cofactor. Animal FeADHs are found in just one Protein Subfamily, the hydroxyacid-oxoacid transhydrogenase (HOT) Subfamily, which includes Protein sequences widely distributed in fungi, but not in plants), and in several taxa from lower eukaryotes, bacteria and archaea. Fungi FeADHs are found mainly in two subfamilies: HOT and maleylacetate reductase (MAR), but some can be found also in other three different Protein subfamilies. Plant FeADHs are found only in chlorophyta but not in higher plants, and are distributed in three different Protein subfamilies. FeADHs are a diverse and ancient Protein family that shares a common 3D scaffold with a patchy distribution in eukaryotes. The majority of sequenced FeADHs from eukaryotes are distributed in just two subfamilies, HOT and MAR (found mainly in animals and fungi). These two subfamilies comprise almost 85% of all sequenced FeADHs in eukaryotes.
