Publications

  1. Prudova A*, Gocheva V*, Auf dem Keller U*, Eckhard U*, Olson OC, Akkari L, Butler GS, Fortelny N, Lange PF, McLeod J, Joyce JA, and Overall CM (2016). TAILS N-terminomics and proteomics show protein degradation dominates over proteolytic processing by cathepsins in pancreatic tumors. Cell Reports, 16(6):1762-1773. PMID: 27477282. [Open Access]
  2. Butler GS, Connor AR, Sounni NE, Eckhard U, Morrison CJ, Noël A., and Overall CM (2016). Degradomic and yeast 2-hybrid inactive catalytic domain substrate trapping identifies new membrane-type 1 matrix metalloproteinase (MMP14) substrates: CCN3 (Nov) and CCN5 (WISP2). Matrix Biology, pii: S0945-053X(16)30165-2. PMID: 27477282. [Open Access]
  3. Eckhard U*, Huesgen PF*, Schilling O*, Bellac CL, Butler GS, Cox JH, Dufour A, Goebeler V, Kappelhoff R, Auf dem Keller U, Klein T, Lange PF, Marino G, Morrison CJ, Prudova A, Rodriguez D, Starr AE, Wang Y, and Overall CM (2016). Active site specificity profiling datasets of matrix metalloproteinases (MMPs) 1, 2, 3, 7, 8, 9, 12, 13 and 14. Data in Brief, eCollection 2016, PMID: 26981551. [Open Access]
  4. Eckhard U, Marino G, Butler GS, and Overall CM (2016). Positional proteomics in the era of the human proteome project on the doorstep of precision medicine. Biochimie, pii: S0300-9084(15)00338-7. Review. PMID: 26542287. [Open Access]
  5. Eckhard U, Huesgen PF, Schilling O, Bellac CL, Butler GS, Cox JH, Dufour A, Goebeler V, Kappelhoff R, Keller UA, Klein T, Lange PF, Marino G, Morrison CJ, Prudova A, Rodriguez D, Starr AE, Wang Y, and Overall CM (2016). Active site specificity profiling of the matrix metalloproteinase family: Proteomic identification of 4300 cleavage sites by nine MMPs explored with structural and synthetic peptide cleavage analyses. Matrix Biology, 49:37-60. PMID: PMID: 26407638. [Open Access]
  6. Eckhard U, Marino G, Abbey SR, Matthew I, and Overall CM (2015). TAILS N-terminomic and proteomic datasets of healthy human dental pulp. Data in Brief, eCollection 2015, PMID: 26587561. [Open Access]
  7. Eckhard U, Marino G, Abbey SR, Tharmarajah G, Matthew I, and Overall CM (2015). The human dental pulp proteome and N-terminome: levering the unexplored potential of semitryptic peptides enriched by tails to identify missing proteins in the human proteome project in underexplored tissues. Journal of Proteome Research, 14(9): 3568-3582. PMID: 26258467. [Open Access]
  8. Marino G, Eckhard U, and Overall CM (2015). Protein termini and their modifications revealed by positional proteomics. ACS Chemical Biology, 10(8): 1754-1764. Review. PMID: 26042555. [Open Access]
  9. Huesgen PF, Lange PF, Rogers LD, Solis N, Eckhard U, Kleifeld O, Goulas T, Gomis-Rüth FX, and Overall CM (2015). LysargiNase mirrors trypsin for protein C-terminal and methylation-site identification. Nature Methods, 12:1, 55-58. PMID: 25419962. [ResearchGate]
  10. Prudova A, Serrano K, Eckhard U, Fortelny N, Devine DV, and Overall CM (2014). TAILS N-terminomics of human platelets reveals pervasive metalloproteinase-dependent proteolytic processing in storage. Blood, 124:26, e49-60. PMID: 25331112. [Open Access]
  11. Barré O, Dufour A, Eckhard U, Kappelhoff R, Béliveau F, Leduc R, Overall CM (2014). Cleavage specificity analysis of six type II transmembrane serine proteases (TTSPs) using PICS with proteome-derived peptide libraries. PLoS One, 9:9, e105984. 25211023. [Open Access]
  12. Eckhard U, Huesgen PF, Brandstetter H, and Overall CM (2014). Proteomic protease specificity profiling of clostridial collagenases reveals their intrinsic nature as dedicated degraders of collagen. Journal of Proteomics, 100, 102-114. PMID: 24125730. [Open Access]
  13. Marino G, Huesgen PF, Eckhard U, Overall CM, Schröder WP, and Funk C (2014). Family-wide characterization of Matrix Metallo-proteinases from Arabidopsis thaliana reveals their distinct proteolytic activity and cleavage site specificity. Biochemical Journal, 457:2, 335-346. PMID: 24156403. [ResearchGate]
  14. Eckhard U and Brandstetter H (2013). Structural basis for activity regulation and substrate preference of clostridial collagenases G, H, and T. The Journal of Biological Chemistry. 288:28, 20184-20194. PMID: 23703618. [Open Access]
  15. Auf dem Keller U, Prudova A, Eckhard U, Fingleton B, and Overall CM (2013). Systems-level analysis of proteolytic events in increased vascular permeability and complement activation in skin inflammation. Science Signaling, 6:258, rs2. PMID: 23322905. [ResearchGate]
  16. Kofler S, Asam C, Eckhard U, Wallner M, Ferreira F, Brandstetter H (2012). Crystallographically Mapped Ligand Binding Differs in High and Low IgE Binding Isoforms of Birch Pollen Allergen Bet v 1. Journal of Molecular Biology, 422:1, 109-123. PMID: 22634284. [Open Access]
  17. Eckhard U, Schönauer E, Nüss D & Brandstetter H (2011). Structure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysis. Nature Structural & Molecular Biology, 18:10, 1109-1114. PMID: 21947205. [Open Access]
  18. Eckhard U and Brandstetter H (2011). Polycystic kidney disease-like domains of clostridial collagenases and their role in collagen recruitment. Biological Chemistry, 392:11, 1039-1045. PMID: 21871007. [ResearchGate]
  19. Ducka P, Eckhard U, Schönauer E, Kofler S, Gottschalk G, Brandstetter H and Nüss D (2009). A universal strategy for high-yield production of soluble and functional clostridial collagenases in E. coli. Applied Microbiology and Biotechnology, 83:6. 1055-1065. PMID: 19333597. [Open Access]
  20. Eckhard U, Schönauer E, Ducka P, Briza P, Nüss D and Brandstetter H (2009). Biochemical characterization of the catalytic domains of three different clostridial collagenases. Biological Chemistry, 390:1, 11-18. PMID: 18937627. [ResearchGate]
  21. Eckhard U, Nüss D, Ducka P, Schönauer E and Brandstetter H (2008). Crystallization and preliminary X-ray characterization of the catalytic domain of collagenase G from Clostridium histolyticum. Acta Crystallographica Section F 64:5, 419-421. PMID: 18453715. [Open Access]
  22. Stolba R, Rezanka E, Eckhard U, and Wider G (2005). Genotyping of the LCT (T/C-13910) polymorphism on the LightCycler using fluorescent hybridisation probes. Journal of Laboratory Medicine, 29 (3), 194-197. doi: 10.1515/JLM.2005.027. [ResearchGate]