Search results for: Ulrich Eckhard

Items from 1 to 11 out of 11 results

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Repositioning small molecule drugs as allosteric inhibitors of the BFT‐3 toxin from enterotoxigenic Bacteroides fragilis

Ana Jimenez‐Alesanco, Ulrich Eckhard, Marta Asencio del Rio, Sonia Vega, more

Bacteroides fragilis is an abundant commensal component of the healthy human colon. However, under dysbiotic conditions, enterotoxigenic B. fragilis (ETBF) may arise and elicit diarrhea, anaerobic bacteremia, inflammatory bowel disease, and colorectal cancer. Most worrisome, ETBF is resistant to many disparate antibiotics. ETBF's only recognized specific virulence factor is a zinc‐dependent metallopeptidase...

article

Melanocyte development in the mouse tail epidermis requires the Adamts9 metalloproteinase

Grace Tharmarajah, Ulrich Eckhard, Fagun Jain, Giada Marino, more

Pigment Cell & Melanoma Research > 31 > 6 > 693 - 707

The mouse tail has an important role in the study of melanogenesis, because mouse tail skin can be used to model human skin pigmentation. To better understand the development of melanocytes in the mouse tail, we cloned two dominant ENU‐generated mutations of the Adamts9 gene, Und3 and Und4, which cause an unpigmented ring of epidermis in the middle of the tail, but do not alter pigmentation in the...

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Degradomic and yeast 2-hybrid inactive catalytic domain substrate trapping identifies new membrane-type 1 matrix metalloproteinase (MMP14) substrates: CCN3 (Nov) and CCN5 (WISP2)

Georgina S. Butler, Andrea R. Connor, Nor Eddine Sounni, Ulrich Eckhard, more

Matrix Biology > 2017 > 59 > C > 23-38

Members of the CCN family of matricellular proteins are cytokines linking cells to the extracellular matrix. We report that CCN3 (Nov) and CCN5 (WISP2) are novel substrates of MMP14 (membrane-type 1-matrix metalloproteinase, MT1-MMP) that we identified using MMP14 “inactive catalytic domain capture” (ICDC) as a yeast two-hybrid protease substrate trapping platform in parallel with degradomics mass...

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TAILS N-Terminomics and Proteomics Show Protein Degradation Dominates over Proteolytic Processing by Cathepsins in Pancreatic Tumors

Anna Prudova, Vasilena Gocheva, Ulrich auf dem Keller, Ulrich Eckhard, more

Cell Reports > 2016 > 16 > 6 > 1762-1773

Deregulated cathepsin proteolysis occurs across numerous cancers, but in vivo substrates mediating tumorigenesis remain ill-defined. Applying 8-plex iTRAQ terminal amine isotopic labeling of substrates (TAILS), a systems-level N-terminome degradomics approach, we identified cathepsin B, H, L, S, and Z in vivo substrates and cleavage sites with the use of six different cathepsin knockout genotypes...

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Active site specificity profiling datasets of matrix metalloproteinases (MMPs) 1, 2, 3, 7, 8, 9, 12, 13 and 14

Ulrich Eckhard, Pitter F. Huesgen, Oliver Schilling, Caroline L. Bellac, more

Data in Brief > 2016 > 7 > C > 299-310

The data described provide a comprehensive resource for the family-wide active site specificity portrayal of the human matrix metalloproteinase family. We used the high-throughput proteomic technique PICS (Proteomic Identification of protease Cleavage Sites) to comprehensively assay 9 different MMPs. We identified more than 4300 peptide cleavage sites, spanning both the prime and non-prime sides of...

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Positional proteomics in the era of the human proteome project on the doorstep of precision medicine

Ulrich Eckhard, Giada Marino, Georgina S. Butler, Christopher M. Overall

Biochimie > 2016 > 122 > C > 110-118

Proteolytic processing is a pervasive and irreversible post-translational modification that expands the protein universe by generating new proteoforms (protein isoforms). Unlike signal peptide or prodomain removal, protease-generated proteoforms can rarely be predicted from gene sequences. Positional proteomic techniques that enrich for N- or C-terminal peptides from proteomes are indispensable for...

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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

Ulrich Eckhard, Pitter F. Huesgen, Oliver Schilling, Caroline L. Bellac, more

Matrix Biology > 2016 > 49 > C > 37-60

Secreted and membrane tethered matrix metalloproteinases (MMPs) are key homeostatic proteases regulating the extracellular signaling and structural matrix environment of cells and tissues. For drug targeting of proteases, selectivity for individual molecules is highly desired and can be met by high yield active site specificity profiling. Using the high throughput Proteomic Identification of protease...

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TAILS N-terminomic and proteomic datasets of healthy human dental pulp

Ulrich Eckhard, Giada Marino, Simon R. Abbey, Ian Matthew, more

Data in Brief > 2015 > 5 > C > 542-548

The Data described here provide the in depth proteomic assessment of the human dental pulp proteome and N-terminome (Eckhard et al., 2015) [1]. A total of 9 human dental pulps were processed and analyzed by the positional proteomics technique TAILS (Terminal Amine Isotopic Labeling of Substrates) N-terminomics. 38 liquid chromatography tandem mass spectrometry (LC-MS/MS) datasets were collected and...

article

Proteomic protease specificity profiling of clostridial collagenases reveals their intrinsic nature as dedicated degraders of collagen

Ulrich Eckhard, Pitter F. Huesgen, Hans Brandstetter, Christopher M. Overall

Journal of Proteomics > 2014 > 100 > Complete > 102-114

Clostridial collagenases are among the most efficient degraders of collagen. Most clostridia are saprophytes and secrete proteases to utilize proteins in their environment as carbon sources; during anaerobic infections, collagenases play a crucial role in host colonization. Several medical and biotechnological applications have emerged utilizing their high collagenolytic efficiency. However, the contribution...

article

Crystallographically Mapped Ligand Binding Differs in High and Low IgE Binding Isoforms of Birch Pollen Allergen Bet v 1

Stefan Kofler, Claudia Asam, Ulrich Eckhard, Michael Wallner, more

Journal of Molecular Biology > 2012 > 422 > 1 > 109-123

The ability of pathogenesis-related proteins of family 10 to bind a broad spectrum of ligands is considered to play a key role for their physiological and pathological functions. In particular, Bet v 1, an archetypical allergen from birch pollen, is described as a highly promiscuous ligand acceptor. However, the detailed recognition mechanisms, including specificity factors discriminating binding...

article

A universal strategy for high-yield production of soluble and functional clostridial collagenases in E. coli

Paulina Ducka, Ulrich Eckhard, Esther Schönauer, Stefan Kofler, more

Applied Microbiology and Biotechnology > 2009 > 83 > 6 > 1055-1065

Clostridial collagenases are foe and friend: on the one hand, these enzymes enable host infiltration and colonization by pathogenic clostridia, and on the other hand, they are valuable biotechnological tools due to their capacity to degrade various types of collagen and gelatine. However, the demand for high-grade preparations exceeds supply due to their pathogenic origin and the intricate purification...

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