Year |
Citation |
Score |
2017 |
Lindner R, Hartmann E, Tarnawski M, Winkler A, Frey D, Reinstein J, Meinhart A, Schlichting I. Photoactivation mechanism of a bacterial light-regulated adenylyl cyclase. Journal of Molecular Biology. PMID 28336405 DOI: 10.1016/j.jmb.2017.03.020 |
0.332 |
|
2017 |
Schirò G, Woodhouse J, Weik M, Schlichting I, Shoeman RL. Simple and efficient system for photoconverting light-sensitive proteins in serial crystallography experiments Journal of Applied Crystallography. 50: 932-939. DOI: 10.1107/S1600576717006264 |
0.348 |
|
2016 |
Dagliyan O, Tarnawski M, Chu PH, Shirvanyants D, Schlichting I, Dokholyan NV, Hahn KM. Engineering extrinsic disorder to control protein activity in living cells. Science (New York, N.Y.). 354: 1441-1444. PMID 27980211 DOI: 10.1126/Science.Aah3404 |
0.393 |
|
2016 |
Wang H, Vilela M, Winkler A, Tarnawski M, Schlichting I, Yumerefendi H, Kuhlman B, Liu R, Danuser G, Hahn KM. LOVTRAP: an optogenetic system for photoinduced protein dissociation. Nature Methods. PMID 27427858 DOI: 10.1038/Nmeth.3926 |
0.36 |
|
2014 |
Arnlund D, Johansson LC, Wickstrand C, Barty A, Williams GJ, Malmerberg E, Davidsson J, Milathianaki D, DePonte DP, Shoeman RL, Wang D, James D, Katona G, Westenhoff S, White TA, ... ... Schlichting I, et al. Visualizing a protein quake with time-resolved X-ray scattering at a free-electron laser. Nature Methods. 11: 923-6. PMID 25108686 DOI: 10.1038/Nmeth.3067 |
0.307 |
|
2014 |
Winkler A, Udvarhelyi A, Hartmann E, Reinstein J, Menzel A, Shoeman RL, Schlichting I. Characterization of elements involved in allosteric light regulation of phosphodiesterase activity by comparison of different functional BlrP1 states. Journal of Molecular Biology. 426: 853-68. PMID 24291457 DOI: 10.1016/j.jmb.2013.11.018 |
0.312 |
|
2014 |
Barends TR, Foucar L, Botha S, Doak RB, Shoeman RL, Nass K, Koglin JE, Williams GJ, Boutet S, Messerschmidt M, Schlichting I. De novo protein crystal structure determination from X-ray free-electron laser data. Nature. 505: 244-7. PMID 24270807 DOI: 10.1038/Nature12773 |
0.333 |
|
2009 |
Wu YI, Frey D, Lungu OI, Jaehrig A, Schlichting I, Kuhlman B, Hahn KM. A genetically encoded photoactivatable Rac controls the motility of living cells. Nature. 461: 104-8. PMID 19693014 DOI: 10.1038/Nature08241 |
0.354 |
|
2009 |
Barends TR, Hartmann E, Griese JJ, Beitlich T, Kirienko NV, Ryjenkov DA, Reinstein J, Shoeman RL, Gomelsky M, Schlichting I. Structure and mechanism of a bacterial light-regulated cyclic nucleotide phosphodiesterase. Nature. 459: 1015-8. PMID 19536266 DOI: 10.1038/Nature07966 |
0.33 |
|
2006 |
Jung A, Reinstein J, Domratcheva T, Shoeman RL, Schlichting I. Crystal structures of the AppA BLUF domain photoreceptor provide insights into blue light-mediated signal transduction. Journal of Molecular Biology. 362: 717-32. PMID 16949615 DOI: 10.1016/J.JMB.2006.07.024 |
0.323 |
|
2005 |
Jung A, Domratcheva T, Tarutina M, Wu Q, Ko WH, Shoeman RL, Gomelsky M, Gardner KH, Schlichting I. Structure of a bacterial BLUF photoreceptor: Insights into blue light-mediated signal transduction Proceedings of the National Academy of Sciences of the United States of America. 102: 12350-12355. PMID 16107542 DOI: 10.1073/Pnas.0500722102 |
0.363 |
|
2005 |
Meilleur F, Dauvergne MT, Schlichting I, Myles DA. Production and X-ray crystallographic analysis of fully deuterated cytochrome P450cam. Acta Crystallographica. Section D, Biological Crystallography. 61: 539-44. PMID 15858263 DOI: 10.1107/S0907444905003872 |
0.305 |
|
2003 |
Fedorov R, Schlichting I, Hartmann E, Domratcheva T, Fuhrmann M, Hegemann P. Crystal structures and molecular mechanism of a light-induced signaling switch: The Phot-LOV1 domain from Chlamydomonas reinhardtii. Biophysical Journal. 84: 2474-82. PMID 12668455 DOI: 10.1016/S0006-3495(03)75052-8 |
0.367 |
|
1990 |
Reinstein J, Schlichting I, Wittinghofer A. Structurally and catalytically important residues in the phosphate binding loop of adenylate kinase of Escherichia coli. Biochemistry. 29: 7451-9. PMID 2223776 DOI: 10.1021/bi00484a014 |
0.305 |
|
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