Klaus Maskos

Summary

Country: Germany

Publications

  1. pmc Engineering N-terminal domain of tissue inhibitor of metalloproteinase (TIMP)-3 to be a better inhibitor against tumour necrosis factor-alpha-converting enzyme
    Meng Huee Lee
    School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, U K
    Biochem J 364:227-34. 2002
  2. ncbi request reprint Crystal structures of MMPs in complex with physiological and pharmacological inhibitors
    Klaus Maskos
    Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, Martinsried bei munchen 82152, Germany
    Biochimie 87:249-63. 2005
  3. ncbi request reprint DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo
    Klaus Maskos
    Institut fur Molekularbiologie und Biophysik, Eidgenossische Technische Hochschule Honggerberg, CH 8093 Zurich, Switzerland
    J Mol Biol 325:495-513. 2003
  4. ncbi request reprint Flexibility and variability of TIMP binding: X-ray structure of the complex between collagenase-3/MMP-13 and TIMP-2
    K Maskos
    Max Planck Institut fur Biochemie, Forschungsgruppe Proteinasen, Am Klopferspitz 18, D 82152 Martinsried, Germany
    J Mol Biol 366:1222-31. 2007
  5. ncbi request reprint 1.2 A crystal structure of the serine carboxyl proteinase pro-kumamolisin; structure of an intact pro-subtilase
    Mireia Comellas-Bigler
    Department of Structure Research, Max Planck Institute for Biochemistry, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    Structure 12:1313-23. 2004
  6. ncbi request reprint Crystal structure of the human carboxypeptidase N (kininase I) catalytic domain
    Cora Keil
    Arbeitsgruppe Proteinaseforschung, Max Planck Institut fur Biochemie, Am Klopferspitz 18, D 82152 Planegg Martinsried, Germany
    J Mol Biol 366:504-16. 2007
  7. ncbi request reprint Crystal structures of MMP-9 complexes with five inhibitors: contribution of the flexible Arg424 side-chain to selectivity
    Anna Tochowicz
    Arbeitsgruppe Proteinaseforschung, Max Planck Institut fur Biochemie, Am Klopferspitz 18, D 82152 Martinsried, Germany
    J Mol Biol 371:989-1006. 2007
  8. ncbi request reprint Crystal structure of the dinuclear zinc aminopeptidase PepV from Lactobacillus delbrueckii unravels its preference for dipeptides
    Daniela Jozic
    Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    Structure 10:1097-106. 2002
  9. ncbi request reprint Structural basis of matrix metalloproteinases and tissue inhibitors of metalloproteinases
    Klaus Maskos
    Max Planck Institut fur Biochemie, D 82152 Martinsried, Germany
    Mol Biotechnol 25:241-66. 2003
  10. pmc Structure-kinetic relationship study of CDK8/CycC specific compounds
    Elisabeth V Schneider
    Max Planck Institut fur Biochemie, D 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 110:8081-6. 2013

Collaborators

Detail Information

Publications25

  1. pmc Engineering N-terminal domain of tissue inhibitor of metalloproteinase (TIMP)-3 to be a better inhibitor against tumour necrosis factor-alpha-converting enzyme
    Meng Huee Lee
    School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, U K
    Biochem J 364:227-34. 2002
    ....
  2. ncbi request reprint Crystal structures of MMPs in complex with physiological and pharmacological inhibitors
    Klaus Maskos
    Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, Martinsried bei munchen 82152, Germany
    Biochimie 87:249-63. 2005
    ....
  3. ncbi request reprint DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo
    Klaus Maskos
    Institut fur Molekularbiologie und Biophysik, Eidgenossische Technische Hochschule Honggerberg, CH 8093 Zurich, Switzerland
    J Mol Biol 325:495-513. 2003
    ..This shows that DsbC is the bacterial enzyme of choice for improving the periplasmic folding yields of proteins with very complex disulfide bond patterns...
  4. ncbi request reprint Flexibility and variability of TIMP binding: X-ray structure of the complex between collagenase-3/MMP-13 and TIMP-2
    K Maskos
    Max Planck Institut fur Biochemie, Forschungsgruppe Proteinasen, Am Klopferspitz 18, D 82152 Martinsried, Germany
    J Mol Biol 366:1222-31. 2007
    ....
  5. ncbi request reprint 1.2 A crystal structure of the serine carboxyl proteinase pro-kumamolisin; structure of an intact pro-subtilase
    Mireia Comellas-Bigler
    Department of Structure Research, Max Planck Institute for Biochemistry, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    Structure 12:1313-23. 2004
    ..The structure strongly points to an initial intramolecular activation cleavage in subtilases, as presumed for pro-subtilisin and pro-furin...
  6. ncbi request reprint Crystal structure of the human carboxypeptidase N (kininase I) catalytic domain
    Cora Keil
    Arbeitsgruppe Proteinaseforschung, Max Planck Institut fur Biochemie, Am Klopferspitz 18, D 82152 Planegg Martinsried, Germany
    J Mol Biol 366:504-16. 2007
    ....
  7. ncbi request reprint Crystal structures of MMP-9 complexes with five inhibitors: contribution of the flexible Arg424 side-chain to selectivity
    Anna Tochowicz
    Arbeitsgruppe Proteinaseforschung, Max Planck Institut fur Biochemie, Am Klopferspitz 18, D 82152 Martinsried, Germany
    J Mol Biol 371:989-1006. 2007
    ..These novel structural details should facilitate the design of more selective MMP-9 inhibitors...
  8. ncbi request reprint Crystal structure of the dinuclear zinc aminopeptidase PepV from Lactobacillus delbrueckii unravels its preference for dipeptides
    Daniela Jozic
    Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    Structure 10:1097-106. 2002
    ..The cocrystallized inhibitor illustrates the two roles of the two catalytic zinc ions, namely stabilization of the tetrahedral intermediate and activation of the catalytic water molecule...
  9. ncbi request reprint Structural basis of matrix metalloproteinases and tissue inhibitors of metalloproteinases
    Klaus Maskos
    Max Planck Institut fur Biochemie, D 82152 Martinsried, Germany
    Mol Biotechnol 25:241-66. 2003
    ..Many of the MMP structures have been determined as complexes with synthetic inhibitors, facilitating knowledge-based drug design. This review focuses on the currently available 3D structural information about MMPs and TIMPs...
  10. pmc Structure-kinetic relationship study of CDK8/CycC specific compounds
    Elisabeth V Schneider
    Max Planck Institut fur Biochemie, D 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 110:8081-6. 2013
    ..Hydrogen bonding with the kinase hinge region contributes to the residence time but has less impact than hydrophobic complementarities within the kinase front pocket...
  11. doi request reprint Structural determinants of the ADAM inhibition by TIMP-3: crystal structure of the TACE-N-TIMP-3 complex
    Magdalena Wisniewska
    Max Planck Institut fur Biochemie, Proteinase Research Group, Am Klopferspitz 18, D 82152 Martinsried, Germany
    J Mol Biol 381:1307-19. 2008
    ..The combination of favourable functional epitopes together with a considerable flexibility renders TIMP-3 an efficient TACE inhibitor. This structure might provide means to design more efficient TIMP inhibitors of TACE...
  12. ncbi request reprint X-ray structure of isoaspartyl dipeptidase from E.coli: a dinuclear zinc peptidase evolved from amidohydrolases
    Daniela Jozic
    Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    J Mol Biol 332:243-56. 2003
    ..Thus, nature has adapted an existing fold with catalytic tools suitable for hydrolysis of amide bonds to the binding requirements of a peptidase...
  13. ncbi request reprint X-ray structure of human proMMP-1: new insights into procollagenase activation and collagen binding
    Daniela Jozic
    Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    J Biol Chem 280:9578-85. 2005
    ..This is the first evidence of mobility of the Hpx domain in relation to the catalytic domain, providing an important clue toward the understanding of the collagenase-collagen interaction and subsequent collagenolysis...
  14. ncbi request reprint Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity
    David Reverter
    Abteilung für Strukturforschung, Max Planck Institut fur Biochemie, Am Klopferspitz 18a, D 82152 Planegg Martinsried, Germany
    J Mol Biol 338:257-69. 2004
    ....
  15. ncbi request reprint Structural basis of the matrix metalloproteinases and their physiological inhibitors, the tissue inhibitors of metalloproteinases
    Wolfram Bode
    Max Planck Institut fur Biochemie, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    Biol Chem 384:863-72. 2003
    ..This review will outline our current structural knowledge of the MMPs and the TIMPs...
  16. doi request reprint Structural and functional studies of the yeast class II Hda1 histone deacetylase complex
    Jung Hoon Lee
    Max Planck Institute of Biochemistry, Martinsried, Germany
    J Mol Biol 391:744-57. 2009
    ..Our structural and functional analyses of the budding yeast class II Hda1 HDAC complex provide insight into DNA recognition and deacetylation of histones in nucleosomes...
  17. ncbi request reprint The 1.4 a crystal structure of kumamolysin: a thermostable serine-carboxyl-type proteinase
    Mireia Comellas-Bigler
    Abteilung für Strukturforschung, Max Planck Institut fur Biochemie, Am Klopferspitz 18 A, D82152, Planegg Martinsried, Germany
    Structure 10:865-76. 2002
    ..An additional Glu/Trp pair, unique to kumamolysin, might further facilitate proton delocalization during nucleophilic attack, in particular at high temperature...
  18. pmc The dimer interface of the membrane type 1 matrix metalloproteinase hemopexin domain: crystal structure and biological functions
    Anna Tochowicz
    Arbeitsgruppe Proteinaseforschung, Max Planck Institut fuer Biochemie, Am Klopferspitz 18, D 82152 Martinsried, Germany
    J Biol Chem 286:7587-600. 2011
    ..These results shed light on the structural basis of MT1-MMP dimerization that is crucial to promote cellular invasion...
  19. doi request reprint Phosphorylation of the human full-length protein kinase Ciota
    Boris Macek
    Abteilung Proteomics and Signaltransduktion, Max Planck Institut fur Biochemie, Am Klopferspitz 18, 82152 Martinsried, Germany
    J Proteome Res 7:2928-35. 2008
    ..The most interesting new phosphorylation site was detected in a well-accessible loop of the PB1 domain (pSer35/pSer37) and may be involved in the interactions of the PB1 domain with different partners in the relevant signaling pathways...
  20. ncbi request reprint The crystal structure of the secreted aspartic proteinase 3 from Candida albicans and its complex with pepstatin A
    Claudia Borelli
    Department of Dermatology and Allergy, Ludwig Maximilian University of Munich, Frauenlobstr 9 11, 80337 Munich, Germany
    Proteins 68:738-48. 2007
    ..Inhibitor binding causes active site closure by the movement of a flap segment. Comparison of the structures of Sap3 and Sap2 identifies elements responsible for the specificity of each isoenzyme...
  21. pmc Tailoring tissue inhibitor of metalloproteinases-3 to overcome the weakening effects of the cysteine-rich domains of tumour necrosis factor-alpha converting enzyme
    Meng Huee Lee
    School of Biological Sciences, University of East Anglia, Norwich, NR4 7TJ, UK
    Biochem J 371:369-76. 2003
    ..Further expression of one of the mutants, Lys(26/27/30/76)-->Glu, in a mammalian expression system confirmed that TIMP-3 associates with the extracellular matrix via its C-terminal domain...
  22. pmc Structural basis of the resistance of an insect carboxypeptidase to plant protease inhibitors
    Alex Bayes
    Departament de Bioquimica i Biologia Molecular, Facultat de Ciencies, and Institut de Biotecnologia i de Biomedicina, Universitat Autonoma de Barcelona, Bellaterra, Spain
    Proc Natl Acad Sci U S A 102:16602-7. 2005
    ..This report explains a crystal structure of an insect protease and its adaptation to defensive plant protease inhibitors...
  23. pmc Mapping and characterization of the functional epitopes of tissue inhibitor of metalloproteinases (TIMP)-3 using TIMP-1 as the scaffold: a new frontier in TIMP engineering
    Meng Huee Lee
    School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK
    Protein Sci 11:2493-503. 2002
    ..Most importantly, our findings confirm that the individual characteristics of TIMP could be transplanted from one variant to another...
  24. ncbi request reprint The C-terminal domains of TACE weaken the inhibitory action of N-TIMP-3
    Meng Huee Lee
    School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK
    FEBS Lett 520:102-6. 2002
    ..Our findings highlight the potential role of the C-terminal domains of ADAM proteinases in influencing TIMP interactions...
  25. ncbi request reprint Matrix metalloproteinases, tissue inhibitors of MMPs and TACE in experimental cerebral malaria
    Philippe E Van Den Steen
    Laboratory of Immunobiology, Rega Institute, University of Leuven, Leuven, Belgium
    Lab Invest 86:873-88. 2006
    ..berghei ANKA. Furthermore, in comparison with C57Bl/6 mice, a larger increase in TIMP-1 and a marked, >30-fold induction in MMP-3 were found in the brains of Balb/C mice, suggesting possible protective roles for TIMP-1 and MMP-3...