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Blue light-induced LOV domain dimerization enhances the affinity of Aureochrome 1a for its target DNA sequence.
Heintz U, Schlichting I. Heintz U, et al. Among authors: schlichting i. Elife. 2016 Jan 12;5:e11860. doi: 10.7554/eLife.11860. Elife. 2016. PMID: 26754770 Free PMC article.
Three-dimensional structures of H-ras p21 mutants: molecular basis for their inability to function as signal switch molecules.
Krengel U, Schlichting I, Scherer A, Schumann R, Frech M, John J, Kabsch W, Pai EF, Wittinghofer A. Krengel U, et al. Among authors: schlichting i. Cell. 1990 Aug 10;62(3):539-48. doi: 10.1016/0092-8674(90)90018-a. Cell. 1990. PMID: 2199064
Crystal structure of photolysed carbonmonoxy-myoglobin.
Schlichting I, Berendzen J, Phillips GN Jr, Sweet RM. Schlichting I, et al. Nature. 1994 Oct 27;371(6500):808-12. doi: 10.1038/371808a0. Nature. 1994. PMID: 7935843
The structure of Trypanosoma cruzi trypanothione reductase in the oxidized and NADPH reduced state.
Lantwin CB, Schlichting I, Kabsch W, Pai EF, Krauth-Siegel RL. Lantwin CB, et al. Among authors: schlichting i. Proteins. 1994 Feb;18(2):161-73. doi: 10.1002/prot.340180208. Proteins. 1994. PMID: 8159665
Crystal structure of the Trypanosoma cruzi trypanothione reductase.mepacrine complex.
Jacoby EM, Schlichting I, Lantwin CB, Kabsch W, Krauth-Siegel RL. Jacoby EM, et al. Among authors: schlichting i. Proteins. 1996 Jan;24(1):73-80. doi: 10.1002/(SICI)1097-0134(199601)24:1<73::AID-PROT5>3.0.CO;2-P. Proteins. 1996. PMID: 8628734
Out of the blue: the photocycle of the photoactive yellow protein.
Schlichting I, Berendzen J. Schlichting I, et al. Structure. 1997 Jun 15;5(6):735-9. doi: 10.1016/s0969-2126(97)00228-1. Structure. 1997. PMID: 9261074 Review.
Structures of active conformations of UMP kinase from Dictyostelium discoideum suggest phosphoryl transfer is associative.
Schlichting I, Reinstein J. Schlichting I, et al. Biochemistry. 1997 Aug 5;36(31):9290-6. doi: 10.1021/bi970974c. Biochemistry. 1997. PMID: 9280438
Crystal structure of cytochrome P-450cam complexed with the (1S)-camphor enantiomer.
Schlichting I, Jung C, Schulze H. Schlichting I, et al. FEBS Lett. 1997 Oct 6;415(3):253-7. doi: 10.1016/s0014-5793(97)01135-6. FEBS Lett. 1997. PMID: 9357977
The major binding mode of (1S)-camphor resembles the one of the (1R)-enantiomer in that there is a hydrogen bond between Tyr-96 and the quinone group of camphor, and the 10-methyl group points towards the I-helix. ...
The major binding mode of (1S)-camphor resembles the one of the (1R)-enantiomer in that there is a hydrogen bond between Tyr-96 and the quin …
Loop closure and intersubunit communication in tryptophan synthase.
Schneider TR, Gerhardt E, Lee M, Liang PH, Anderson KS, Schlichting I. Schneider TR, et al. Among authors: schlichting i. Biochemistry. 1998 Apr 21;37(16):5394-406. doi: 10.1021/bi9728957. Biochemistry. 1998. PMID: 9548921
Iron center, substrate recognition and mechanism of peptide deformylase.
Becker A, Schlichting I, Kabsch W, Groche D, Schultz S, Wagner AF. Becker A, et al. Among authors: schlichting i. Nat Struct Biol. 1998 Dec;5(12):1053-8. doi: 10.1038/4162. Nat Struct Biol. 1998. PMID: 9846875
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