Illme Schlichting - Publications

Affiliations: 
Max Planck Heidelberg, Heidelberg, Baden-Württemberg, Germany 

14 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

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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