Year |
Citation |
Score |
2021 |
Ferreira IM, Edwin N Quesñay J, Bastos AC, Rodrigues CT, Vollmar M, Krojer T, Strain-Damerell C, Burgess-Brown NA, von Delft F, Yue WW, Dias SM, Ambrosio AL. Structure and activation mechanism of the human liver-type glutaminase GLS2. Biochimie. PMID 33746066 DOI: 10.1016/j.biochi.2021.03.009 |
0.354 |
|
2019 |
Pfeffer I, Brewitz L, Krojer T, Jensen SA, Kochan GT, Kershaw NJ, Hewitson KS, McNeill LA, Kramer H, Münzel M, Hopkinson RJ, Oppermann U, Handford PA, McDonough MA, Schofield CJ. Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern. Nature Communications. 10: 4910. PMID 31659163 DOI: 10.1038/S41467-019-12711-7 |
0.36 |
|
2014 |
Chowdhury R, Sekirnik R, Brissett NC, Krojer T, Ho CH, Ng SS, Clifton IJ, Ge W, Kershaw NJ, Fox GC, Muniz JR, Vollmar M, Phillips C, Pilka ES, Kavanagh KL, et al. Ribosomal oxygenases are structurally conserved from prokaryotes to humans. Nature. 510: 422-6. PMID 24814345 DOI: 10.1038/Nature13263 |
0.407 |
|
2014 |
Horita S, Scotti J, McDonough M, Sekirnik R, Chowdhury R, Krojer T, Thalhammer A, Aik W, Oppermann U, Schofield C. Crystal structures of 2OG oxygenases involved in ribosomal protein hydroxylation Acta Crystallographica Section a Foundations and Advances. 70: C304-C304. DOI: 10.1107/S2053273314096958 |
0.321 |
|
2013 |
Froese DS, Forouhar F, Tran TH, Vollmar M, Kim YS, Lew S, Neely H, Seetharaman J, Shen Y, Xiao R, Acton TB, Everett JK, Cannone G, Puranik S, Savitsky P, ... Krojer T, et al. Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Structure (London, England : 1993). 21: 1182-92. PMID 23791943 DOI: 10.1016/J.Str.2013.05.001 |
0.349 |
|
2013 |
Canning P, Cooper CD, Krojer T, Murray JW, Pike AC, Chaikuad A, Keates T, Thangaratnarajah C, Hojzan V, Ayinampudi V, Marsden BD, Gileadi O, Knapp S, von Delft F, Bullock AN. Structural basis for Cul3 protein assembly with the BTB-Kelch family of E3 ubiquitin ligases. The Journal of Biological Chemistry. 288: 7803-14. PMID 23349464 DOI: 10.1074/jbc.M112.437996 |
0.406 |
|
2012 |
Froese DS, Krojer T, Wu X, Shrestha R, Kiyani W, von Delft F, Gravel RA, Oppermann U, Yue WW. Structure of MMACHC reveals an arginine-rich pocket and a domain-swapped dimer for its B12 processing function. Biochemistry. 51: 5083-90. PMID 22642810 DOI: 10.1021/bi300150y |
0.399 |
|
2011 |
Sawa J, Malet H, Krojer T, Canellas F, Ehrmann M, Clausen T. Molecular adaptation of the DegQ protease to exert protein quality control in the bacterial cell envelope. The Journal of Biological Chemistry. 286: 30680-30690. PMID 21685389 DOI: 10.1074/jbc.M111.243832 |
0.663 |
|
2011 |
Kochan G, Krojer T, Harvey D, Fischer R, Chen L, Vollmar M, von Delft F, Kavanagh KL, Brown MA, Bowness P, Wordsworth P, Kessler BM, Oppermann U. Crystal structures of the endoplasmic reticulum aminopeptidase-1 (ERAP1) reveal the molecular basis for N-terminal peptide trimming. Proceedings of the National Academy of Sciences of the United States of America. 108: 7745-50. PMID 21508329 DOI: 10.1073/Pnas.1101262108 |
0.335 |
|
2011 |
Truebestein L, Tennstaedt A, Mönig T, Krojer T, Canellas F, Kaiser M, Clausen T, Ehrmann M. Substrate-induced remodeling of the active site regulates human HTRA1 activity. Nature Structural & Molecular Biology. 18: 386-8. PMID 21297635 DOI: 10.1038/nsmb.2013 |
0.65 |
|
2010 |
Mantri M, Krojer T, Bagg EA, Webby CA, Butler DS, Kochan G, Kavanagh KL, Oppermann U, McDonough MA, Schofield CJ. Crystal Structure of the 2-Oxoglutarate- and Fe(II)-Dependent Lysyl Hydroxylase JMJD6. Journal of Molecular Biology. PMID 20685276 DOI: 10.1016/J.Jmb.2010.05.054 |
0.326 |
|
2010 |
Mantri M, Krojer T, Bagg EA, Webby CJ, Butler DS, Kochan G, Kavanagh KL, Oppermann U, McDonough MA, Schofield CJ. Crystal structure of the 2-oxoglutarate- and Fe(II)-dependent lysyl hydroxylase JMJD6. Journal of Molecular Biology. 401: 211-22. PMID 20684070 |
0.327 |
|
2010 |
Krojer T, Sawa J, Huber R, Clausen T. HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues. Nature Structural & Molecular Biology. 17: 844-52. PMID 20581825 DOI: 10.1038/Nsmb.1840 |
0.755 |
|
2009 |
Meltzer M, Hasenbein S, Mamant N, Merdanovic M, Poepsel S, Hauske P, Kaiser M, Huber R, Krojer T, Clausen T, Ehrmann M. Structure, function and regulation of the conserved serine proteases DegP and DegS of Escherichia coli. Research in Microbiology. 160: 660-6. PMID 19695325 DOI: 10.1016/J.Resmic.2009.07.012 |
0.687 |
|
2009 |
Hauske P, Meltzer M, Ottmann C, Krojer T, Clausen T, Ehrmann M, Kaiser M. Selectivity profiling of DegP substrates and inhibitors. Bioorganic & Medicinal Chemistry. 17: 2920-4. PMID 19233659 DOI: 10.1016/j.bmc.2009.01.073 |
0.625 |
|
2008 |
Krojer T, Pangerl K, Kurt J, Sawa J, Stingl C, Mechtler K, Huber R, Ehrmann M, Clausen T. Interplay of PDZ and protease domain of DegP ensures efficient elimination of misfolded proteins Proceedings of the National Academy of Sciences of the United States of America. 105: 7702-7707. PMID 18505836 DOI: 10.1073/Pnas.0803392105 |
0.746 |
|
2008 |
Krojer T, Sawa J, Schäfer E, Saibil HR, Ehrmann M, Clausen T. Structural basis for the regulated protease and chaperone function of DegP. Nature. 453: 885-90. PMID 18496527 DOI: 10.1038/nature07004 |
0.691 |
|
2008 |
Meltzer M, Hasenbein S, Hauske P, Kucz N, Merdanovic M, Grau S, Beil A, Jones D, Krojer T, Clausen T, Ehrmann M, Kaiser M. Allosteric activation of HtrA protease DegP by stress signals during bacterial protein quality control. Angewandte Chemie (International Ed. in English). 47: 1332-4. PMID 18175296 DOI: 10.1002/anie.200703273 |
0.635 |
|
2007 |
Hasselblatt H, Kurzbauer R, Wilken C, Krojer T, Sawa J, Kurt J, Kirk R, Hasenbein S, Ehrmann M, Clausen T. Regulation of the σE stress response by DegS: How the PDZ domain keeps the protease inactive in the resting state and allows integration of different OMP-derived stress signals upon folding stress Genes and Development. 21: 2659-2670. PMID 17938245 DOI: 10.1101/gad.445307 |
0.662 |
|
2007 |
Krojer T, Sawa J, Fuhrmann J, Gazda L, Kirk R, Kurt J, Nussbaumer B, Schmidt B, Clausen T. The protease state of the heat-shock protein DegP fromEscherichia coli Acta Crystallographica Section a Foundations of Crystallography. 63: s120-s120. DOI: 10.1107/S0108767307097413 |
0.702 |
|
2006 |
Chatwell L, Krojer T, Fidler A, Römisch W, Eisenreich W, Bacher A, Huber R, Fischer M. Biosynthesis of Riboflavin: Structure and Properties of 2,5-Diamino-6-ribosylamino-4(3H)-pyrimidinone 5′-phosphate Reductase of Methanocaldococcus jannaschii Journal of Molecular Biology. 359: 1334-1351. PMID 16730025 DOI: 10.1016/J.Jmb.2006.04.045 |
0.411 |
|
2006 |
Ramsperger A, Augustin M, Schott AK, Gerhardt S, Krojer T, Eisenreich W, Illarionov B, Cushman M, Bacher A, Huber R, Fischer M. Crystal structure of an archaeal pentameric riboflavin synthase in complex with a substrate analog inhibitor: Stereochemical implications Journal of Biological Chemistry. 281: 1224-1232. PMID 16272154 DOI: 10.1074/Jbc.M509440200 |
0.465 |
|
2002 |
Krojer T, Garrido-Franco M, Huber R, Ehrmann M, Clausen T. Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine Nature. 416: 455-459. PMID 11919638 DOI: 10.1038/416455A |
0.733 |
|
2002 |
Krojer T, Garrido-Franco M, Huber R, Ehrmann M, Clausen T. Erratum: corrigendum: Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine Nature. 417: 102-102. DOI: 10.1038/417102c |
0.609 |
|
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