Institution
Chonbuk National University
Education•Jeonju, South Korea•
About: Chonbuk National University is a education organization based out in Jeonju, South Korea. It is known for research contribution in the topics: Apoptosis & Graphene. The organization has 14820 authors who have published 28884 publications receiving 554131 citations.
Topics: Apoptosis, Graphene, Nanofiber, Population, Electrospinning
Papers published on a yearly basis
Papers
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TL;DR: The crystallite size was decreased to constant value for Cell 2 treated at >or= 15 wt% NaOH, and the crystalliteSize of Cell 2-C (cellulose II) was smaller than that of Cell 1 ( cellulose I) treated at 5-10 wt%, and the CI(XD) was calculated by the method of Jayme and Knolle.
1,113 citations
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TL;DR: The 3.2 Å crystal structure of the bovine Ops*–GαCT peptide complex is presented and signal transfer from the receptor to the G protein nucleotide-binding site is discussed.
Abstract: Opsin, the ligand-free form of the G-protein-coupled receptor rhodopsin, at low pH adopts a conformationally distinct, active G-protein-binding state known as Ops*. A synthetic peptide derived from the main binding site of the heterotrimeric G protein-the carboxy terminus of the alpha-subunit (GalphaCT)-stabilizes Ops*. Here we present the 3.2 A crystal structure of the bovine Ops*-GalphaCT peptide complex. GalphaCT binds to a site in opsin that is opened by an outward tilt of transmembrane helix (TM) 6, a pairing of TM5 and TM6, and a restructured TM7-helix 8 kink. Contacts along the inner surface of TM5 and TM6 induce an alpha-helical conformation in GalphaCT with a C-terminal reverse turn. Main-chain carbonyl groups in the reverse turn constitute the centre of a hydrogen-bonded network, which links the two receptor regions containing the conserved E(D)RY and NPxxY(x)(5,6)F motifs. On the basis of the Ops*-GalphaCT structure and known conformational changes in Galpha, we discuss signal transfer from the receptor to the G protein nucleotide-binding site.
1,069 citations
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TL;DR: Findings link abnormalities in ubiquilin 2 to defects in the protein degradation pathway, abnormal protein aggregation and neurodegeneration, indicating a common pathogenic mechanism that can be exploited for therapeutic intervention.
Abstract: ing cases of familial ALS and of the vast majority of sporadic ALS are unknown. Despite extensive studies of previously identified ALS-causing genes, the pathogenic mechanism underlying motorneuron degeneration in ALS remains largely obscure. Dementia, usually of the frontotemporal lobar type, may occur in some ALS cases. It is unclear whether ALS and dementia share common aetiology and pathogenesis in ALS/dementia. Here we show that mutations in UBQLN2, which encodes the ubiquitin-like protein ubiquilin 2, cause dominantly inherited, chromosome-X-linked ALS and ALS/dementia. We describe novel ubiquilin 2 pathology in the spinal cords of ALS cases and in the brains of ALS/dementia cases with or without UBQLN2 mutations. Ubiquilin 2 is a member of the ubiquilin family, which regulates the degradation of ubiquitinated proteins. Functional analysis showed that mutations in UBQLN2 lead to an impairment of protein degradation. Therefore, our findings link abnormalities in ubiquilin 2 to defects in the protein degradation pathway, abnormal protein aggregation and neurodegeneration, indicating a common pathogenic mechanism that can be exploited for therapeutic intervention.
1,068 citations
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TL;DR: It is shown that reoxygenation after prolonged hypoxia reduces the reactive oxygen species (ROS) threshold for the mitochondrial permeability transition (MPT) in cardiomyocytes and that cell survival is steeply negatively correlated with the fraction of depolarized mitochondria.
Abstract: Environmental stresses converge on the mitochondria that can trigger or inhibit cell death. Excitable, postmitotic cells, in response to sublethal noxious stress, engage mechanisms that afford protection from subsequent insults. We show that reoxygenation after prolonged hypoxia reduces the reactive oxygen species (ROS) threshold for the mitochondrial permeability transition (MPT) in cardiomyocytes and that cell survival is steeply negatively correlated with the fraction of depolarized mitochondria. Cell protection that exhibits a memory (preconditioning) results from triggered mitochondrial swelling that causes enhanced substrate oxidation and ROS production, leading to redox activation of PKC, which inhibits glycogen synthase kinase-3beta (GSK-3beta). Alternatively, receptor tyrosine kinase or certain G protein-coupled receptor activation elicits cell protection (without mitochondrial swelling or durable memory) by inhibiting GSK-3beta, via protein kinase B/Akt and mTOR/p70(s6k) pathways, PKC pathways, or protein kinase A pathways. The convergence of these pathways via inhibition of GSK-3beta on the end effector, the permeability transition pore complex, to limit MPT induction is the general mechanism of cardiomyocyte protection.
963 citations
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TL;DR: The crystal structure of ligand-free native opsin from bovine retinal rod cells is presented and shows prominent structural changes in the conserved E(D)RY and NPxxY(x)5,6F regions and in TM5–TM7.
Abstract: In the G-protein-coupled receptor (GPCR) rhodopsin, the inactivating ligand 11-cis-retinal is bound in the seven-transmembrane helix (TM) bundle and is cis/trans isomerized by light to form active metarhodopsin II. With metarhodopsin II decay, all-trans-retinal is released, and opsin is reloaded with new 11-cis-retinal. Here we present the crystal structure of ligand-free native opsin from bovine retinal rod cells at 2.9 angstrom (A) resolution. Compared to rhodopsin, opsin shows prominent structural changes in the conserved E(D)RY and NPxxY(x)(5,6)F regions and in TM5-TM7. At the cytoplasmic side, TM6 is tilted outwards by 6-7 A, whereas the helix structure of TM5 is more elongated and close to TM6. These structural changes, some of which were attributed to an active GPCR state, reorganize the empty retinal-binding pocket to disclose two openings that may serve the entry and exit of retinal. The opsin structure sheds new light on ligand binding to GPCRs and on GPCR activation.
899 citations
Authors
Showing all 14943 results
Name | H-index | Papers | Citations |
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Hyun-Chul Kim | 176 | 4076 | 183227 |
Andrew Ivanov | 142 | 1812 | 97390 |
Dong-Chul Son | 138 | 1370 | 98686 |
C. Haber | 135 | 1507 | 98014 |
Tae Jeong Kim | 132 | 1420 | 93959 |
Alessandro Cerri | 129 | 1244 | 103225 |
Paul M. Vanhoutte | 127 | 868 | 62177 |
Jason Nielsen | 125 | 893 | 72688 |
Chi Lin | 125 | 1313 | 102710 |
Paul Lujan | 123 | 1255 | 76799 |
Young Hee Lee | 122 | 1168 | 61107 |
Min Suk Kim | 119 | 975 | 66214 |
Alexandre Sakharov | 119 | 582 | 56771 |
Yang-Kook Sun | 117 | 781 | 58912 |
Rui L. Reis | 115 | 1608 | 63223 |