Year |
Citation |
Score |
2019 |
Steccanella F, Savalli N, Yusifov T, Battista Luciani G, Neely A, Olcese R. How Does the α2δ-1 Subunit Modulate Skeletal CaV1.1 Channels? Biophysical Journal. 116: 113a. DOI: 10.1016/J.Bpj.2018.11.639 |
0.674 |
|
2019 |
Angelini M, Savalli N, Yusifov T, Olcese R. Skeletal γ1 Subunit Modulation of Human CaV1.1 and CaV1.2 Channels Biophysical Journal. 116: 112a-113a. DOI: 10.1016/J.Bpj.2018.11.637 |
0.675 |
|
2017 |
Yusifov T, Savalli N, Pantazis A, Heinemann SH, Hoshi T, Olcese R. Carbon Monoxide May Regulate BK slo1 Channel Activity by Partially Disrupting Heme Coordination Biophysical Journal. 112: 112a. DOI: 10.1016/J.Bpj.2016.11.631 |
0.702 |
|
2016 |
Savalli N, Angelini M, Pantazis A, Yusifov T, Neely A, Olcese R. Eminence of VSD I in the Voltage-Dependent Inactivation of the Human CaV1.2 Channel Biophysical Journal. 110: 444a. DOI: 10.1016/J.Bpj.2015.11.2388 |
0.711 |
|
2015 |
Yusifov T, Savalli N, Heinemann SH, Hoshi T, Olcese R. The Heme-Bound Human BK Channel Gating Ring is a Co Sensor Biophysical Journal. 108: 122a. DOI: 10.1016/J.Bpj.2014.11.682 |
0.738 |
|
2015 |
Yusifov T, Savalli N, Park S, Pantazis A, Olcese R. The Role of Met-691 in Heme-Dependent Regulation Supports the Presence of a Cytochrome-C-Like Structure in Human BK Channels Biophysical Journal. 108: 121a-122a. DOI: 10.1016/J.Bpj.2014.11.681 |
0.723 |
|
2014 |
Yusifov T, Savalli N, Pantazis A, Olcese R. Enzymatic Activity of the Human BK Channel: A Function Beyond Electrical Signaling Biophysical Journal. 106: 535a. DOI: 10.1016/J.Bpj.2013.11.2986 |
0.713 |
|
2014 |
Yusifov T, Madhvani RV, Olcese R. The Cytochrome C-Like Domain of the Human BK Channel Biophysical Journal. 106: 535a. DOI: 10.1016/J.Bpj.2013.11.2985 |
0.701 |
|
2013 |
Yusifov T, Gandhi CS, Pantazis A, Olcese R. Structural Studies of the Apo and Ca2+-Bound States of the Human BK (SLO1) Channel Gating Ring in Solution Biophysical Journal. 104: 473a. DOI: 10.1016/J.Bpj.2012.11.2614 |
0.72 |
|
2012 |
Savalli N, Pantazis A, Yusifov T, Sigg D, Olcese R. The contribution of RCK domains to human BK channel allosteric activation. The Journal of Biological Chemistry. 287: 21741-50. PMID 22556415 DOI: 10.1074/Jbc.M112.346171 |
0.742 |
|
2012 |
Yusifov T, Javaherian AD, Heinemann SH, Hoshi T, Olcese R. Evidence for Lipid-Induced Structural Rearrangements in the Human BK (Slo1) Channel Gating Ring Biophysical Journal. 102: 688a. DOI: 10.1016/J.Bpj.2011.11.3738 |
0.714 |
|
2012 |
Yusifov T, Javaherian AD, Heinemann SH, Hoshi T, Olcese R. Calcium and Heme Induce Distinct Conformational States of the Human BK (Slo1) Channel Gating Ring Biophysical Journal. 102: 687a-688a. DOI: 10.1016/J.Bpj.2011.11.3737 |
0.702 |
|
2011 |
Javaherian AD, Yusifov T, Pantazis A, Franklin S, Gandhi CS, Olcese R. Metal-driven operation of the human large-conductance voltage- and Ca2+-dependent potassium channel (BK) gating ring apparatus. The Journal of Biological Chemistry. 286: 20701-9. PMID 21471215 DOI: 10.1074/Jbc.M111.235234 |
0.744 |
|
2011 |
Yusifov T, Javaherian A, Pantazis A, Gandhi C, Olcese R. On the Properties of the RCK1 Domain of the Human BK (SLO1) Channel Biophysical Journal. 100: 581a. DOI: 10.1016/J.Bpj.2010.12.3359 |
0.717 |
|
2011 |
Yusifov T, Javaherian A, Gandhi C, Olcese R. Calcium-Dependent Operation of the Human BK Channel Gating Ring Apparatus Biophysical Journal. 100: 581a. DOI: 10.1016/J.Bpj.2010.12.3358 |
0.774 |
|
2010 |
Yusifov T, Javaherian AD, Pantazis A, Gandhi CS, Olcese R. The RCK1 domain of the human BKCa channel transduces Ca2+ binding into structural rearrangements. The Journal of General Physiology. 136: 189-202. PMID 20624858 DOI: 10.1085/Jgp.200910374 |
0.716 |
|
2010 |
Yusifov T, Javaherian A, Gandhi C, Hou S, Heinemann S, Hoshi T, Olcese R. Heme-Driven Conformational Changes in the Human Slo1 BKCa Channel Gating Ring Biophysical Journal. 98: 126a. DOI: 10.1016/J.Bpj.2009.12.684 |
0.731 |
|
2009 |
Yusifov T, Javaherian A, Nicoll D, Gandhi C, Olcese R. Calcium Sensing Properties of the RCK1 Domain of the Human BK Channel: Effects of the D362/367A Mutation Biophysical Journal. 96: 481a. DOI: 10.1016/J.Bpj.2008.12.2482 |
0.713 |
|
2009 |
Javaherian A, Yusifov T, Nicoll D, Gandhi C, Olcese R. Structural and Functional Analysis of the Purified Cytosolic C-Terminus of the Human BK Channel Biophysical Journal. 96: 481a. DOI: 10.1016/J.Bpj.2008.12.2481 |
0.693 |
|
2008 |
Yusifov T, Savalli N, Gandhi CS, Ottolia M, Olcese R. The RCK2 domain of the human BKCa channel is a calcium sensor. Proceedings of the National Academy of Sciences of the United States of America. 105: 376-81. PMID 18162557 DOI: 10.1073/Pnas.0705261105 |
0.748 |
|
Low-probability matches (unlikely to be authored by this person) |
2002 |
Glasgow BJ, Abduragimov AR, Gassymov OK, Faull KF, Yusifov TN, Lehrer RI. Characterization of a lipophilin in rabbit tears Advances in Experimental Medicine and Biology. 506: 573-580. PMID 12613962 DOI: 10.1007/978-1-4615-0717-8_80 |
0.256 |
|
2002 |
Gasymov OK, Abduragimov AR, Yusifov TN, Glasgow BJ. RET and anisotropy measurements establish the proximity of the conserved Trp17 to Ile98 and Phe99 of tear lipocalin. Biochemistry. 41: 8837-48. PMID 12102626 |
0.233 |
|
1998 |
Glasgow BJ, Abduragimov AR, Yusifov TN, Gasymov OK, Horwitz J, Hubbell WL, Faull KF. A conserved disulfide motif in human tear lipocalins influences ligand binding. Biochemistry. 37: 2215-25. PMID 9485367 DOI: 10.1021/bi9720888 |
0.226 |
|
2002 |
Gasymov OK, Abduragimov AR, Yusifov TN, Glasgow BJ. Relaxation of beta-structure in tear lipocalin and enhancement of retinoid binding. Investigative Ophthalmology & Visual Science. 43: 3165-73. PMID 12356820 |
0.214 |
|
1999 |
Gasymov OK, Abduragimov AR, Yusifov TN, Glasgow BJ. Binding studies of tear lipocalin: the role of the conserved tryptophan in maintaining structure, stability and ligand affinity. Biochimica Et Biophysica Acta. 1433: 307-20. PMID 10515687 DOI: 10.1016/S0167-4838(99)00133-8 |
0.21 |
|
1999 |
Zhao C, Nguyen T, Yusifov T, Glasgow BJ, Lehrer RI. Lipophilins: human peptides homologous to rat prostatein. Biochemical and Biophysical Research Communications. 256: 147-55. PMID 10066439 DOI: 10.1006/Bbrc.1999.0274 |
0.209 |
|
2000 |
Gasymov OK, Abduragimov AR, Yusifov TN, Glasgow BJ. Resolution of ligand positions by site-directed tryptophan fluorescence in tear lipocalin. Protein Science : a Publication of the Protein Society. 9: 325-31. PMID 10716184 DOI: 10.1110/PS.9.2.325 |
0.207 |
|
2000 |
YUSIFOV TN, ABDURAGIMOV AR, GASYMOV OK, GLASGOW BJ. Endonuclease activity in lipocalins Biochemical Journal. 347: 815-819. DOI: 10.1042/BJ3470815 |
0.192 |
|
1998 |
Gasymov OK, Abduragimov AR, Yusifov TN, Glasgow BJ. Structural changes in human tear lipocalins associated with lipid binding. Biochimica Et Biophysica Acta. 1386: 145-56. PMID 9675263 DOI: 10.1016/S0167-4838(98)00092-2 |
0.192 |
|
2002 |
Gasymov OK, Abduragimov AR, Yusifov TN, Glasgow BJ. Site-directed tryptophan fluorescence reveals the solution structure of tear lipocalin: evidence for features that confer promiscuity in ligand binding. Biochemistry. 40: 14754-62. PMID 11732894 DOI: 10.1021/BI0110342 |
0.176 |
|
2004 |
Gasymov OK, Abduragimov AR, Yusifov TN, Glasgow BJ. Interstrand loops CD and EF act as pH-dependent gates to regulate fatty acid ligand binding in tear lipocalin. Biochemistry. 43: 12894-904. PMID 15461462 DOI: 10.1021/bi049076o |
0.17 |
|
2004 |
Gasymov OK, Abduragimov AR, Gasimov EO, Yusifov TN, Dooley AN, Glasgow BJ. Tear lipocalin: potential for selective delivery of rifampin. Biochimica Et Biophysica Acta. 1688: 102-11. PMID 14990340 DOI: 10.1016/j.bbadis.2003.11.006 |
0.158 |
|
1999 |
Gasymov OK, Abduragimov AR, Yusifov TN, Glasgow BJ. Interaction of tear lipocalin with lysozyme and lactoferrin. Biochemical and Biophysical Research Communications. 265: 322-5. PMID 10558865 DOI: 10.1006/BBRC.1999.1668 |
0.154 |
|
1999 |
Glasgow BJ, Gasymov OK, Abduragimov AR, Yusifov TN, Altenbach C, Hubbell WL. Side chain mobility and ligand interactions of the G strand of tear lipocalins by site-directed spin labeling. Biochemistry. 38: 13707-16. PMID 10521278 DOI: 10.1021/bi9913449 |
0.153 |
|
1997 |
Gasymov OK, Abduragimov AR, Yusifov TN, Glasgow BJ. Solution structure by site directed tryptophan fluorescence in tear lipocalin. Biochemical and Biophysical Research Communications. 239: 191-6. PMID 9345294 DOI: 10.1006/BBRC.1997.7451 |
0.146 |
|
1998 |
Glasgow BJ, Abduragimov AR, Yusifov TN, Gasymov OK. Studies of ligand binding and CD analysis with apo- and holo-tear lipocalins. Advances in Experimental Medicine and Biology. 438: 105-12. PMID 9634872 DOI: 10.1007/978-1-4615-5359-5_14 |
0.131 |
|
2002 |
Glasgow BJ, Abduragimov AR, Gasymov OK, Yusifov TN. Tear lipocalin: structure, function and molecular mechanisms of action. Advances in Experimental Medicine and Biology. 506: 555-65. PMID 12613960 |
0.113 |
|
2001 |
Abduragimov AR, Gasymov OK, Yusifov TN, Glasgow BJ. Functional cavity dimensions of tear lipocalin. Current Eye Research. 21: 824-32. PMID 11120574 DOI: 10.1076/ceyr.21.4.824.5551 |
0.093 |
|
2003 |
Gasymov OK, Abduragimov AR, Yusifov TN, Glasgow BJ. Resolving near-ultraviolet circular dichroism spectra of single trp mutants in tear lipocalin. Analytical Biochemistry. 318: 300-8. PMID 12814635 |
0.091 |
|
2005 |
Gasymov OK, Abduragimov AR, Prasher P, Yusifov TN, Glasgow BJ. Tear lipocalin: evidence for a scavenging function to remove lipids from the human corneal surface. Investigative Ophthalmology & Visual Science. 46: 3589-96. PMID 16186338 DOI: 10.1167/iovs.05-0569 |
0.076 |
|
2002 |
Glasgow BJ, Abduragimov AR, Gassymov OK, Yusifov TN, Ruth EC, Faull KF. Vitamin E associated with the lipocalin fraction of human tears Advances in Experimental Medicine and Biology. 506: 567-572. PMID 12613961 DOI: 10.1007/978-1-4615-0717-8_79 |
0.05 |
|
2008 |
Yusifov TN, Abduragimov AR, Narsinh K, Gasymov OK, Glasgow BJ. Tear lipocalin is the major endonuclease in tears. Molecular Vision. 14: 180-8. PMID 18334931 |
0.046 |
|
2005 |
Glasgow BJ, Gasymov OK, Abduragimov AR, Yusifov TN. Tear Lipocalin: A Multifunctional Protein in the Tear Film The Ocular Surface. 3: S66. DOI: 10.1016/S1542-0124(12)70416-0 |
0.026 |
|
Hide low-probability matches. |