| Year |
Citation |
Score |
| 2019 |
Goettig P, Brandstetter H, Magdolen V. Surface loops of trypsin-like serine proteases as determinants of function. Biochimie. 166: 52-76. PMID 31505212 DOI: 10.1016/j.biochi.2019.09.004 |
0.47 |
|
| 2018 |
Debela M, Magdolen V, Skala W, Elsässer B, Schneider EL, Craik CS, Biniossek ML, Schilling O, Bode W, Brandstetter H, Goettig P. Structural determinants of specificity and regulation of activity in the allosteric loop network of human KLK8/neuropsin. Scientific Reports. 8: 10705. PMID 30013126 DOI: 10.1038/S41598-018-29058-6 |
0.396 |
|
| 2018 |
Guo S, Briza P, Magdolen V, Brandstetter H, Goettig P. Activation and activity of glycosylated KLKs 3, 4 and 11. Biological Chemistry. PMID 29975661 DOI: 10.1515/hsz-2018-0148 |
0.626 |
|
| 2018 |
Schinagl A, Kerschbaumer RJ, Sabarth N, Douillard P, Scholz P, Voelkel D, Hollerweger JC, Goettig P, Brandstetter H, Scheiflinger F, Thiele M. Role of the Cysteine 81 Residue of Macrophage Migration Inhibitory Factor as a Molecular Redox Switch. Biochemistry. 57: 1523-1532. PMID 29412660 DOI: 10.1021/acs.biochem.7b01156 |
0.326 |
|
| 2017 |
Debela M, Magdolen V, Bode W, Brandstetter H, Goettig P. Structural basis for the Zn2+ inhibition of the zymogen-like kallikrein-related peptidase 10. Biological Chemistry. 397: 1251-1264. PMID 27611765 DOI: 10.1515/hsz-2016-0205 |
0.465 |
|
| 2016 |
Goettig P. Effects of Glycosylation on the Enzymatic Activity and Mechanisms of Proteases. International Journal of Molecular Sciences. 17. PMID 27898009 DOI: 10.3390/ijms17121969 |
0.443 |
|
| 2016 |
Jung S, Fischer J, Spudy B, Kerkow T, Sönnichsen FD, Xue L, Bonvin AM, Goettig P, Magdolen V, Meyer-Hoffert U, Grötzinger J. The solution structure of the kallikrein-related peptidases inhibitor SPINK6. Biochemical and Biophysical Research Communications. PMID 26828269 DOI: 10.1016/J.Bbrc.2016.01.172 |
0.31 |
|
| 2015 |
Guo S, Skala W, Magdolen V, Briza P, Biniossek ML, Schilling O, Kellermann J, Brandstetter H, Goettig P. A Single glycan at the 99-loop of human kallikrein-related peptidase 2 regulates activation and enzymatic activity. The Journal of Biological Chemistry. PMID 26582203 DOI: 10.1074/jbc.M115.691097 |
0.588 |
|
| 2015 |
Guo S, Skala W, Magdolen V, Brandstetter H, Goettig P. Sweetened kallikrein-related peptidases (KLKs): glycan trees as potential regulators of activation and activity. Biological Chemistry. 395: 959-76. PMID 25153382 DOI: 10.1515/hsz-2014-0140 |
0.639 |
|
| 2014 |
Skala W, Utzschneider DT, Magdolen V, Debela M, Guo S, Craik CS, Brandstetter H, Goettig P. Structure-function analyses of human kallikrein-related peptidase 2 establish the 99-loop as master regulator of activity. The Journal of Biological Chemistry. 289: 34267-83. PMID 25326387 DOI: 10.1074/Jbc.M114.598201 |
0.629 |
|
| 2010 |
Goettig P, Magdolen V, Brandstetter H. Natural and synthetic inhibitors of kallikrein-related peptidases (KLKs). Biochimie. 92: 1546-67. PMID 20615447 DOI: 10.1016/j.biochi.2010.06.022 |
0.348 |
|
| 2010 |
Seiz L, Kotzsch M, Grebenchtchikov NI, Geurts-Moespot AJ, Fuessel S, Goettig P, Gkazepis A, Wirth MP, Schmitt M, Lossnitzer A, Sweep FC, Magdolen V. Polyclonal antibodies against kallikrein-related peptidase 4 (KLK4): immunohistochemical assessment of KLK4 expression in healthy tissues and prostate cancer. Biological Chemistry. 391: 391-401. PMID 20180634 DOI: 10.1515/BC.2010.033 |
0.401 |
|
| 2009 |
Yoon H, Blaber SI, Debela M, Goettig P, Scarisbrick IA, Blaber M. A completed KLK activome profile: investigation of activation profiles of KLK9, 10, and 15. Biological Chemistry. 390: 373-7. PMID 19090718 DOI: 10.1515/Bc.2009.026 |
0.431 |
|
| 2008 |
Debela M, Beaufort N, Magdolen V, Schechter NM, Craik CS, Schmitt M, Bode W, Goettig P. Structures and specificity of the human kallikrein-related peptidases KLK 4, 5, 6, and 7. Biological Chemistry. 389: 623-32. PMID 18627343 DOI: 10.1515/Bc.2008.075 |
0.384 |
|
| 2007 |
Debela M, Hess P, Magdolen V, Schechter NM, Steiner T, Huber R, Bode W, Goettig P. Chymotryptic specificity determinants in the 1.0 A structure of the zinc-inhibited human tissue kallikrein 7. Proceedings of the National Academy of Sciences of the United States of America. 104: 16086-91. PMID 17909180 DOI: 10.1073/Pnas.0707811104 |
0.368 |
|
| 2007 |
Debela M, Goettig P, Magdolen V, Huber R, Schechter NM, Bode W. Structural Basis of the Zinc Inhibition of Human Tissue Kallikrein 5 Journal of Molecular Biology. 373: 1017-1031. PMID 17881000 DOI: 10.1016/J.Jmb.2007.08.042 |
0.304 |
|
| 2006 |
Debela M, Magdolen V, Grimminger V, Sommerhoff C, Messerschmidt A, Huber R, Friedrich R, Bode W, Goettig P. Crystal structures of human tissue kallikrein 4: activity modulation by a specific zinc binding site. Journal of Molecular Biology. 362: 1094-107. PMID 16950394 DOI: 10.1016/J.Jmb.2006.08.003 |
0.607 |
|
| 2006 |
Debela M, Magdolen V, Schechter N, Valachova M, Lottspeich F, Craik CS, Choe Y, Bode W, Goettig P. Specificity profiling of seven human tissue kallikreins reveals individual subsite preferences. The Journal of Biological Chemistry. 281: 25678-88. PMID 16740631 DOI: 10.1074/Jbc.M602372200 |
0.423 |
|
| 2002 |
Goettig P, Groll M, Kim JS, Huber R, Brandstetter H. Structures of the tricorn-interacting aminopeptidase F1 with different ligands explain its catalytic mechanism. The Embo Journal. 21: 5343-52. PMID 12374735 DOI: 10.1093/Emboj/Cdf552 |
0.31 |
|
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