Year |
Citation |
Score |
2017 |
Hofmann L, Alexander NS, Sun W, Zhang J, Orban T, Palczewski K. Hydrogen/Deuterium Exchange Mass Spectrometry of Human Green Opsin Reveals a Conserved Pro-Pro Motif in Extracellular Loop 2 of Monostable Visual G Protein-Coupled Receptors. Biochemistry. PMID 28402104 DOI: 10.1021/Acs.Biochem.7B00165 |
0.312 |
|
2016 |
Rajavel M, Orban T, Xu M, Hernandez-Sanchez W, de la Fuente M, Palczewski K, Taylor DJ. Dynamic peptides of human TPP1 fulfill diverse functions in telomere maintenance. Nucleic Acids Research. PMID 27655633 DOI: 10.1093/Nar/Gkw846 |
0.354 |
|
2015 |
Jastrzebska B, Chen Y, Orban T, Jin H, Hofmann L, Palczewski K. Disruption of Rhodopsin Dimerization with Synthetic Peptides Targeting an Interaction Interface. The Journal of Biological Chemistry. 290: 25728-44. PMID 26330551 DOI: 10.1074/Jbc.M115.662684 |
0.359 |
|
2013 |
Jastrzebska B, Orban T, Golczak M, Engel A, Palczewski K. Asymmetry of the rhodopsin dimer in complex with transducin. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 27: 1572-84. PMID 23303210 DOI: 10.1096/Fj.12-225383 |
0.31 |
|
2012 |
Orban T, Huang CC, Homan KT, Jastrzebska B, Tesmer JJ, Palczewski K. Substrate-induced changes in the dynamics of rhodopsin kinase (G protein-coupled receptor kinase 1). Biochemistry. 51: 3404-11. PMID 22480180 DOI: 10.1021/Bi300295Y |
0.313 |
|
2011 |
Huang CC, Orban T, Jastrzebska B, Palczewski K, Tesmer JJ. Activation of G protein-coupled receptor kinase 1 involves interactions between its N-terminal region and its kinase domain. Biochemistry. 50: 1940-9. PMID 21265573 DOI: 10.1021/Bi101606E |
0.35 |
|
2008 |
Barhoover MA, Orban T, Bukys MA, Kalafatis M. Cooperative regulation of the activity of factor Xa within prothrombinase by discrete amino acid regions from factor Va heavy chain. Biochemistry. 47: 12835-43. PMID 18991406 DOI: 10.1021/Bi801241R |
0.702 |
|
2008 |
Barhoover MA, Orban T, Beck DO, Bukys MA, Kalafatis M. Contribution of amino acid region 334-335 from factor Va heavy chain to the catalytic efficiency of prothrombinase. Biochemistry. 47: 6840-50. PMID 18537263 DOI: 10.1021/Bi800057R |
0.702 |
|
2008 |
Bukys MA, Orban T, Kim PY, Nesheim ME, Kalafatis M. The interaction of fragment 1 of prothrombin with the membrane surface is a prerequisite for optimum expression of factor Va cofactor activity within prothrombinase. Thrombosis and Haemostasis. 99: 511-22. PMID 18327399 DOI: 10.1160/Th07-08-0532 |
0.765 |
|
2007 |
Bukys MA, Orban T, Kim PY, Nesheim ME, Kalafatis M. Factor Va Cofactor Activity Is Dependent on the Interaction of Prothrombin with the Membrane Surface. Blood. 110: 2702-2702. DOI: 10.1182/Blood.V110.11.2702.2702 |
0.769 |
|
2006 |
Bukys MA, Orban T, Kim PY, Beck DO, Nesheim ME, Kalafatis M. The structural integrity of anion binding exosite I of thrombin is required and sufficient for timely cleavage and activation of factor V and factor VIII. The Journal of Biological Chemistry. 281: 18569-80. PMID 16624813 DOI: 10.1074/Jbc.M600752200 |
0.762 |
|
2006 |
Orban T, Kalafatis M. Human Coagulation Factor Va Interaction with Phospholipid Vesicles: A Molecular Dynamics Study. Blood. 108: 1699-1699. DOI: 10.1182/Blood.V108.11.1699.1699 |
0.69 |
|
2005 |
Orban T, Kalafatis M, Gogonea V. Completed three-dimensional model of human coagulation factor va. Molecular dynamics simulations and structural analyses. Biochemistry. 44: 13082-90. PMID 16185076 DOI: 10.1021/Bi050891T |
0.657 |
|
2005 |
Orban T, Kalafatis M. Human Prothrombin Fragment 1 Conformational Changes Following Binding to Phospholipid Vesicles: A Computational Study. Blood. 106: 4047-4047. DOI: 10.1182/Blood.V106.11.4047.4047 |
0.615 |
|
2005 |
Bukys MA, Orban T, Kim PY, Nesheim ME, Kalafatis M. Exposure of Anion Binding Exosite I of Thrombin Is Required and Sufficient for Timely Cleavage and Activation of Factor V and Factor VIII. Blood. 106: 1951-1951. DOI: 10.1182/Blood.V106.11.1951.1951 |
0.761 |
|
2005 |
Blum MA, Orban T, Beck DO, Kalafatis M. The Specific Contribution of Amino Acids 334 and 335 from Factor Va Heavy Chain to the Catalytic Efficiency of Prothrombinase. Blood. 106: 1027-1027. DOI: 10.1182/Blood.V106.11.1027.1027 |
0.74 |
|
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