| Year |
Citation |
Score |
| 2019 |
Coskuner O, Uversky VN. Intrinsically disordered proteins in various hypotheses on the pathogenesis of Alzheimer's and Parkinson's diseases. Progress in Molecular Biology and Translational Science. 166: 145-223. PMID 31521231 DOI: 10.1016/Bs.Pmbts.2019.05.007 |
0.399 |
|
| 2017 |
Coskuner O, Uversky VN. BMP-2 and BMP-9 binding specificities with ALK-3 in aqueous solution with dynamics. Journal of Molecular Graphics & Modelling. 77: 181-188. PMID 28869862 DOI: 10.1016/J.Jmgm.2017.08.005 |
0.384 |
|
| 2017 |
Coskuner O, Uversky VN. Tyrosine Regulates β-Sheet Structure Formation in Amyloid-β42: A New Clustering Algorithm for Disordered Proteins. Journal of Chemical Information and Modeling. PMID 28474890 DOI: 10.1021/Acs.Jcim.6B00761 |
0.502 |
|
| 2016 |
Coskuner O. Divalent copper ion bound amyloid-β(40) and amyloid-β(42) alloforms are less preferred than divalent zinc ion bound amyloid-β(40) and amyloid-β(42) alloforms. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 27659954 DOI: 10.1007/S00775-016-1392-5 |
0.424 |
|
| 2014 |
Wise O, Coskuner O. New force field parameters for metalloproteins I: Divalent copper ion centers including three histidine residues and an oxygen-ligated amino acid residue. Journal of Computational Chemistry. 35: 1278-89. PMID 24777820 DOI: 10.1002/Jcc.23622 |
0.677 |
|
| 2014 |
Coskuner O, Murray IV. Adenosine triphosphate (ATP) reduces amyloid-β protein misfolding in vitro. Journal of Alzheimer's Disease : Jad. 41: 561-74. PMID 24625803 DOI: 10.3233/Jad-132300 |
0.371 |
|
| 2013 |
Coskuner O, Wise-Scira O. Arginine and disordered amyloid-β peptide structures: molecular level insights into the toxicity in Alzheimer's disease. Acs Chemical Neuroscience. 4: 1549-58. PMID 24041422 DOI: 10.1021/Cn4001389 |
0.47 |
|
| 2013 |
Coskuner O, Wise-Scira O. Structures and free energy landscapes of the A53T mutant-type α-synuclein protein and impact of A53T mutation on the structures of the wild-type α-synuclein protein with dynamics. Acs Chemical Neuroscience. 4: 1101-13. PMID 23607785 DOI: 10.1021/Cn400041J |
0.498 |
|
| 2013 |
Coskuner O, Wise-Scira O, Perry G, Kitahara T. The structures of the E22Δ mutant-type amyloid-β alloforms and the impact of E22Δ mutation on the structures of the wild-type amyloid-β alloforms. Acs Chemical Neuroscience. 4: 310-20. PMID 23421682 DOI: 10.1021/Cn300149J |
0.598 |
|
| 2013 |
Wise-Scira O, Dunn A, Aloglu AK, Sakallioglu IT, Coskuner O. Structures of the E46K mutant-type α-synuclein protein and impact of E46K mutation on the structures of the wild-type α-synuclein protein. Acs Chemical Neuroscience. 4: 498-508. PMID 23374074 DOI: 10.1021/Cn3002027 |
0.483 |
|
| 2013 |
Wise-Scira O, Aloglu AK, Dunn A, Sakallioglu IT, Coskuner O. Structures and free energy landscapes of the wild-type and A30P mutant-type α-synuclein proteins with dynamics. Acs Chemical Neuroscience. 4: 486-97. PMID 23374072 DOI: 10.1021/Cn300198Q |
0.445 |
|
| 2012 |
Fawver JN, Duong KT, Wise-Scira O, Petrofes Chapa R, Schall HE, Coskuner O, Zhu X, Colom LV, Murray IV. Probing and trapping a sensitive conformation: amyloid-β fibrils, oligomers, and dimers. Journal of Alzheimer's Disease : Jad. 32: 197-215. PMID 22785403 DOI: 10.3233/Jad-2012-120880 |
0.392 |
|
| 2012 |
Wise-Scira O, Xu L, Perry G, Coskuner O. Structures and free energy landscapes of aqueous zinc(II)-bound amyloid-β(1-40) and zinc(II)-bound amyloid-β(1-42) with dynamics. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 17: 927-38. PMID 22674434 DOI: 10.1007/S00775-012-0909-9 |
0.445 |
|
| 2011 |
Wise-Scira O, Xu L, Kitahara T, Perry G, Coskuner O. Amyloid-β peptide structure in aqueous solution varies with fragment size. The Journal of Chemical Physics. 135: 205101. PMID 22128957 DOI: 10.1063/1.3662490 |
0.6 |
|
| 2009 |
Coskuner O, Allison TC. Dynamic and structural properties of aqueous arsenic solutions. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 10: 1187-9. PMID 19308977 DOI: 10.1002/Cphc.200800650 |
0.338 |
|
| 2009 |
Coskuner O, Bergeron DE, Rincon L, Hudgens JW, Gonzalez CA. Identification of active sites of biomolecules II: Saccharide and transition metal ion in aqueous solution. The Journal of Physical Chemistry. A. 113: 2491-9. PMID 19236000 DOI: 10.1021/Jp805747F |
0.494 |
|
| 2008 |
Coskuner O, Bergeron DE, Rincon L, Hudgens JW, Gonzalez CA. Glycosidic linkage conformation of methyl-alpha-mannopyranoside. The Journal of Chemical Physics. 129: 045102. PMID 18681681 DOI: 10.1063/1.2958916 |
0.486 |
|
| 2008 |
Coskuner O, Bergeron DE, Rincon L, Hudgens JW, Gonzalez CA. Identification of active sites of biomolecules. 1. Methyl-alpha-mannopyranoside and Fe(III). The Journal of Physical Chemistry. A. 112: 2940-7. PMID 18302355 DOI: 10.1021/Jp711759Q |
0.509 |
|
| 2007 |
Coskuner O. Preferred conformation of the glycosidic linkage of methyl-beta-mannose. The Journal of Chemical Physics. 127: 015101. PMID 17627368 DOI: 10.1063/1.2747238 |
0.348 |
|
| 2007 |
Coskuner O, Deiters UK. Hydrophobic interactions of xenon by Monte Carlo simulations Zeitschrift Fur Physikalische Chemie. 221: 785-799. DOI: 10.1524/Zpch.2007.221.6.785 |
0.567 |
|
| 2006 |
Coskuner O, Deiters UK. Hydrophobic interactions by Monte Carlo simulations Zeitschrift Fur Physikalische Chemie. 220: 349-369. DOI: 10.1524/Zpch.2006.220.3.349 |
0.57 |
|
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