Prof. Dr. Christoph Becker-Pauly

Christoph Becker-Pauly
Christoph Becker-Pauly
Unit for Degradomics of the Protease Web


Original Publications & Reviews

Original Publications & Reviews

Scharfenberg F, Helbig A, Sammel M, Benzel J, Schlomann U, Peters F, Wichert R, Bettendorff M, Schmidt-Arras D, Rose-John S, Moali C, Lichtenthaler SF, Pietrzik CU, Bartsch JW, Tholey A, Becker-Pauly C. (2019)
Degradome of soluble ADAM10 and ADAM17 metalloproteases.
Cell Mol Life Sci. 2019 Jun 17. doi: 10.1007/s00018-019-03184-4. [Epub ahead of print]
Scharfenberg F, Armbrust F, Marengo L, Pietrzik C, Becker-Pauly C. (2019)
Regulation of the alternative β-secretase meprin β by ADAM-mediated shedding.
Cell Mol Life Sci. 2019 Aug;76(16):3193-3206. Review.
Schäffler H, Li W, Helm O, Krüger S, Böger C, Peters F, Röcken C, Sebens S, Lucius R, Becker-Pauly C, Arnold P. (2019)
The cancer associated meprin β variant p.G32R provides an additional activation site and promotes cancer cell invasion.
J Cell Sci 132(11).
Peters F, Scharfenberg F, Colmorgen C, Armbrust F, Wichert R, Arnold P, Potempa B, Potempa J, Pietrzik CU, Häsler R, Rosenstiel P, Becker-Pauly C. (2019)
Tethering soluble meprin α in an enzyme complex to the cell surface affects IBD-associated genes.
FASEB J 33(6):7490-7504
Karmilin K, Schmitz C, Kuske M, Körschgen H, Olf M, Meyer K, Hildebrand A, Felten M, Fridrich S, Yiallouros I, Becker-Pauly C, Weiskirchen R, Jahnen-Dechent W, Floehr J, Stöcker W. (2019)
Mammalian plasma fetuin-B is a selective inhibitor of ovastacin and meprin metalloproteinases.
Sci Rep 9(1):546
Talantikite M, Lécorché P, Beau F, Damour O, Becker-Pauly C, Ho WB, Dive V, Vadon-Le Goff S, Moali C. (2018)
Inhibitors of BMP-1/tolloid-like proteinases: efficacy, selectivity and cellular toxicity.
FEBS Open Bio 8(12):2011-2021
Walter S, Jumpertz T, Hüttenrauch M, Ogorek I, Gerber H, Storck SE, Zampar S, Dimitrov M, Lehmann S, Lepka K, Berndt C, Wiltfang J, Becker-Pauly C, Beher D, Pietrzik CU, Fraering PC, Wirths O, Weggen S. (2018)
The metalloprotease ADAMTS4 generates N-truncated Aβ4-x species and marks oligodendrocytes as a source of amyloidogenic peptides in Alzheimer's disease.
Acta Neuropathol 137(2):239-257
Boon L, Ugarte-Berzal E, Martens E, Vandooren J, Rybakin V, Colau D, Gordon-Alonso M, van der Bruggen P, Stöcker W, Becker-Pauly C, Witters P, Morava-Kozics E, Jaeken J, Proost P, Opdenakker G. (2018)
Propeptide glycosylation and galectin-3 binding decrease proteolytic activation of human proMMP-9/progelatinase B.
FEBS J 286(5):930-945
Biasin V, Wygrecka M, Bärnthaler T, Jandl K, Jain PP, Bálint Z, Kovacs G, Leitinger G, Kolb-Lenz D, Kornmueller K, Peters F, Sinn K, Klepetko W, Heinemann A, Olschewski A, Becker-Pauly C, Kwapiszewska G. (2018)
Docking of Meprin α to Heparan Sulphate Protects the Endothelium from Inflammatory Cell Extravasation.
Thromb Haemost 118(10):1790-1802
Schmidt S, Schumacher N, Schwarz J, Tangermann S, Kenner L, Schlederer M, Sibilia M, Linder M, Altendorf-Hofmann A, Knösel T, Gruber ES, Oberhuber G, Bolik J, Rehman A, Sinha A, Lokau J, Arnold P, Cabron AS, Zunke F, Becker-Pauly C, Preaudet A, Nguyen P, Huynh J, Afshar-Sterle S, Chand AL, Westermann J, Dempsey PJ, Garbers C, Schmidt-Arras D, Rosenstiel P, Putoczki T, Ernst M, Rose-John S. (2018)
ADAM17 is required for EGF-R-induced intestinal tumors via IL-6 trans-signaling.
J Exp Med 215(4):1205-1225
Wichert R, Ermund A, Schmidt S, Schweinlin M, Ksiazek M, Arnold P, Knittler K, Wilkens F, Potempa B, Rabe B, Stirnberg M, Lucius R, Bartsch JW, Nikolaus S, Falk-Paulsen M, Rosenstiel P, Metzger M, Rose-John S, Potempa J, Hansson GC, Dempsey PJ, Becker-Pauly C. (2017)
Mucus Detachment by Host Metalloprotease Meprin β Requires Shedding of Its Inactive Pro-form, which Is Abrogated by the Pathogenic Protease RgpB.
Cell Rep 21(8):2090-2103
Bedau T, Schumacher N, Peters F, Prox J, Arnold P, Koudelka T, Helm O, Schmidt F, Rabe B, Jentzsch M, Rosenstiel P, Sebens S, Tholey A, Rose-John S, Becker-Pauly C. (2017)
Cancer-associated mutations in the canonical cleavage site do not influence CD99 shedding by the metalloprotease meprin β but alter cell migration in vitro.
Oncotarget 8(33):54873-54888.
Arnold P, Otte A, Becker-Pauly C. (2017)
Meprin metalloproteases: Molecular regulation and function in inflammation and fibrosis.
Biochim Biophys Acta 1864(11 Pt B):2096-2104. Review
Schneppenheim J, Scharfenberg F, Lucius R, Becker-Pauly C, Arnold P. (2017)
Meprin β and BMP-1 are differentially regulated by CaCl2.
Cell Calcium 65:8-13
Arnold P, Boll I, Rothaug M, Schumacher N, Schmidt F, Wichert R, Schneppenheim J, Lokau J, Pickhinke U, Koudelka T, Tholey A, Rabe B, Scheller J, Lucius R, Garbers C, Rose-John S, Becker-Pauly C. (2017)
Meprin Metalloproteases Generate Biologically Active Soluble Interleukin-6 Receptor to Induce Trans-Signaling.
Sci Rep 7:44053
Becker-Pauly C, Pietrzik CU. (2017)
The Metalloprotease Meprin β Is an Alternative β-Secretase of APP.
Front Mol Neurosci 9:159. Review.
Riethmueller S, Somasundaram P, Ehlers JC, Hung CW, Flynn CM, Lokau J, Agthe M, Düsterhöft S, Zhu Y, Grötzinger J, Lorenzen I, Koudelka T, Yamamoto K, Pickhinke U, Wichert R, Becker-Pauly C, Rädisch M, Albrecht A, Hessefort M, Stahnke D, Unverzagt C, Rose-John S, Tholey A, Garbers C. (2017)
Proteolytic Origin of the Soluble Human IL-6R In Vivo and a Decisive Role of N-Glycosylation.
PLoS Biol 15(1):e2000080
Biasin V, Wygrecka M, Marsh LM, Becker-Pauly C, Brcic L, Ghanim B, Klepetko W, Olschewski A, Kwapiszewska G. (2017)
Meprin β contributes to collagen deposition in lung fibrosis.
Sci Rep 7:39969
Bedau T, Peters F, Prox J, Arnold P, Schmidt F, Finkernagel M, Köllmann S, Wichert R, Otte A, Ohler A, Stirnberg M, Lucius R, Koudelka T, Tholey A, Biasin V, Pietrzik CU, Kwapiszewska G, Becker-Pauly C. (2016)
Ectodomain shedding of CD99 within highly conserved regions is mediated by the metalloprotease meprin β and promotes transendothelial cell migration.
FASEB J 31(3):1226-1237
Breig O, Yates M, Neaud V, Couchy G, Grigoletto A, Lucchesi C, Prox J, Zucman-Rossi J, Becker-Pauly C, Rosenbaum J. (2016)
Metalloproteinase meprin α regulates migration and invasion of human hepatocarcinoma cells and is a mediator of the oncoprotein Reptin.
Oncotarget 8(5):7839-7851
Kalinin DV, Wagner S, Riemann B, Hermann S, Schmidt F, Becker-Pauly C, Rose-John S, Schäfers M, Holl R. (2016)
Novel Potent Proline-Based Metalloproteinase Inhibitors: Design, (Radio)Synthesis, and First in Vivo Evaluation as Radiotracers for Positron Emission Tomography.
J Med Chem 59(20):9541-9559.
Madoux F, Dreymuller D, Pettiloud JP, Santos R, Becker-Pauly C, Ludwig A, Fields GB, Bannister T, Spicer TP, Cudic M, Scampavia LD, Minond D. (2016)
Discovery of an enzyme and substrate selective inhibitor of ADAM10 using an exosite-binding glycosylated substrate.
Sci Rep 6(1):11
Arnold P, Koopmann L, Peters F, Birkenfeld F, Goff SV, Damm T, Qin C, Moali C, Lucius R, Becker-Pauly C. (2016)
Deficiency of the DSPP-cleaving enzymes meprin α and meprin β does not result in dentin malformation in mice.
Cell Tissue Res 367(2):351-358
Becker-Pauly C, Pietrzik CU. (2016)
Mice are not Men: ADAM30 Findings Emphasize a Broader Look Towards Murine Alzheimer's Disease Models.
EBioMedicine. 9:19-20
Schmidt F, Müller M, Prox J, Arnold P, Schönherr C, Tredup C, Minder P, Ebsen H, Janssen O, Annaert W, Pietrzik C, Schmidt-Arras D, Sterchi EE, Becker-Pauly C. (2016)
Tetraspanin 8 is an interactor of the metalloprotease meprin β within tetraspanin-enriched microdomains.
Biol Chem. 397(9):857-69
Beckmann AM, Glebov K, Walter J, Merkel O, Mangold M, Schmidt F, Becker-Pauly C, Gütschow M, Stirnberg M. (2016)
The intact Kunitz domain protects the amyloid precursor protein from being processed by matriptase-2.
Biol Chem. 397(8):777-90
Demeestere D, Dejonckheere E, Steeland S, Hulpiau P, Haustraete J, Devoogdt N, Wichert R, Becker-Pauly C, Van Wonterghem E, Dewaele S, Van Imschoot G, Aerts J, Arckens L, Saeys Y, Libert C, Vandenbroucke RE. (2016)
Development and Validation of a Small Single-domain Antibody That Effectively Inhibits Matrix Metalloproteinase 8.
Mol Ther. 24(5): 890-902
Schönherr C, Bien J, Isbert S, Wichert R, Prox J, Altmeppen H, Kumar S, Walter J, Lichtenthaler SF, Weggen S, Glatzel M, Becker-Pauly C, Pietrzik CU. (2016)
Generation of aggregation prone N-terminally truncated amyloid β peptides by meprin β depends on the sequence specificity at the cleavage site.
Mol Neurodegener. 11(1):19
Franke M, Schröder J, Monhasery N, Ackfeld T, Hummel TM, Rabe B, Garbers C, Becker-Pauly C, Floss DM, Scheller J. (2016)
Human and murine Interleukin 23 receptors are novel substrates for a disintegrin and metalloproteases ADAM10 and ADAM17.
J Biol Chem 291 (20): 10551-61
Rothaug M, Becker-Pauly C, Rose-John S. (2016)
The role of interleukin-6 signaling in nervous tissue.
Biochim Biophys Acta 1863(6 Pt A): 1218-27 Review.
Sato Y, Kobayashi D, Kohno T, Kidani Y, Prox J, Becker-Pauly C, Hattori M. (2015)
Determination of Cleavage Site of Reelin between Its Sixth and Seventh Repeat and Contribution of Meprin Metalloproteases to the Cleavage.
J Biochem. 159(3):305-12
Bonaccorso RL, Chepurny OG, Becker-Pauly C, Holz GG, Doyle RP. (2015)
Enhanced Peptide Stability Against Protease Digestion Induced by Intrinsic Factor Binding of a Vitamin B12 Conjugate of Exendin-4.
Mol Pharm. 12(9):3502-6
Jäckle F, Schmidt F, Wichert R, Arnold P, Prox J, Mangold M, Ohler A, Pietrzik CU, Koudelka T, Tholey A, Gütschow M, Stirnberg M, Becker-Pauly C. (2015)
Metalloprotease meprin β is activated by transmembrane serine protease matriptase-2 at the cell surface thereby enhancing APP shedding.
Biochem J. 470(1):91-103
Arnold P, Schmidt F, Prox J, Zunke F, Pietrzik C, Lucius R, Becker-Pauly C. (2015)
Calcium negatively regulates meprin β activity and attenuates substrate cleavage.
FASEB J. 29(8):3549-57
Jodal A, Pape F, Becker-Pauly C, Maas O, Schibli R, Béhé M. (2015)
Evaluation of ¹¹¹In-Labelled Exendin-4 Derivatives Containing Different Meprin β-Specific Cleavable Linkers.
PLoS One 10(4):e0123443
Prox J, Arnold P, Becker-Pauly C. (2015)
Meprin α and meprin β: Procollagen proteinases in health and disease.
Matrix Biol. 2015 Jan 21. pii: S0945-053X(15)00024-4
Schütte A, Ermund A, Becker-Pauly C, Johansson ME, Rodriguez-Pineiro AM, Bäckhed F, Müller S, Lottaz D, Bond JS, Hansson GC. (2014)
Microbial-induced meprin β cleavage in MUC2 mucin and a functional CFTR channel are required to release anchored small intestinal mucus.
Proc Natl Acad Sci U S A 111(34):12396-401.
Madoux F, Tredup C, Spicer TP, Scampavia L, Chase PS, Hodder PS, Fields GB, Becker-Pauly C, Minond D. (2014)
Development of high throughput screening assays and pilot screen for inhibitors of metalloproteases meprin α and β.
Biopolymers 102(5):396-406.
Tucher J, Linke D, Koudelka T, Cassidy L, Tredup C, Wichert R, Pietrzik C, Becker-Pauly C, Tholey A. (2014)
LC-MS based cleavage site profiling of the proteases ADAM10 and ADAM17 using proteome-derived peptide libraries.
J Proteome Res 13(4):2205-14.
Becker-Pauly C, Broder C, Prox J, Koudelka T, Tholey A. (2014)
Mapping orphan proteases by proteomics: Meprin metalloproteases deciphered as potential therapeutic targets.
Proteomics Clin Appl 8(5-6):382-8.
Schwarz J, Broder C, Helmstetter A, Schmidt S, Yan I, Müller M, Schmidt-Arras D, Becker-Pauly C, Koch-Nolte F, Mittrücker HW, Rabe B, Rose-John S, Chalaris A. (2013)
Short-term TNFα shedding is independent of cytoplasmic phosphorylation or furin cleavage of ADAM17.
Biochim Biophys Acta 1833(12):3355-67.
Broder C, Arnold P, Vadon-Le Goff S, Konerding MA, Bahr K, Müller S, Overall CM, Bond JS, Koudelka T, Tholey A, Hulmes DJ, Moali C, Becker-Pauly C. (2013)
Metalloproteases meprin α and meprin β are C- and N-procollagen proteinases important for collagen assembly and tensile strength.
Proc Natl Acad Sci U S A 110(35):14219-24.
Becker-Pauly C, Rose-John S. (2013)
TNFα cleavage beyond TACE/ADAM17: matrix metalloproteinase 13 is a potential therapeutic target in sepsis and colitis.
EMBO Mol Med 5(7):902-4.
Broder C, Becker-Pauly C. (2013)
The metalloproteases meprin α and meprin β: unique enzymes in inflammation, neurodegeneration, cancer and fibrosis.
Biochem J 450(2):253-64.
Jefferson T, Auf dem Keller U, Bellac C, Metz VV, Broder C, Hedrich J, Ohler A, Maier W, Magdolen V, Sterchi E, Bond JS, Jayakumar A, Traupe H, Chalaris A, Rose-John S, Pietrzik CU, Postina R, Overall CM, Becker-Pauly C. (2013)
The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin β and ADAM10.
Cell Mol Life Sci 70(2):309-33.
Arolas JL, Broder C, Jefferson T, Guevara T, Sterchi EE, Bode W, Stöcker W, Becker-Pauly C, Gomis-Rüth FX. (2012)
Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane.
Proc Natl Acad Sci U S A 109(40):16131-6.
Geurts N, Becker-Pauly C, Martens E, Proost P, Van den Steen PE, Stöcker W, Opdenakker G. (2012)
Meprins process matrix metalloproteinase-9 (MMP-9)/gelatinase B and enhance the activation kinetics by MMP-3.
FEBS Lett 586(24):4264-9.
Bijakowski C, Vadon-Le Goff S, Delolme F, Bourhis JM, Lécorché P, Ruggiero F, Becker-Pauly C, Yiallouros I, Stöcker W, Dive V, Hulmes DJ, Moali C. (2012)
Sizzled is unique among secreted frizzled-related proteins for its ability to specifically inhibit bone morphogenetic protein-1 (BMP-1)/tolloid-like proteinases.
J Biol Chem 287(40):33581-93.
Bien J, Jefferson T, Causević M, Jumpertz T, Munter L, Multhaup G, Weggen S, Becker-Pauly C, Pietrzik CU. (2012)
The metalloprotease meprin β generates amino terminal-truncated amyloid β peptide species.
J Biol Chem 287(40):33304-13.
Ohler A, Becker-Pauly C. (2012)
TMPRSS4 is a type II transmembrane serine protease involved in cancer and viral infections.
Biol Chem 393(9):907-14.
Minder P, Bayha E, Becker-Pauly C, Sterchi EE. (2012)
Meprin α transactivates the epidermal growth factor receptor (EGFR) via ligand shedding, thereby enhancing colorectal cancer cell proliferation and migration.
J Biol Chem 287(42):35201-11.
Lottaz D, Maurer CA, Noël A, Blacher S, Huguenin M, Nievergelt A, Niggli V, Kern A, Müller S, Seibold F, Friess H, Becker-Pauly C, Stöcker W, Sterchi EE. (2011)
Enhanced activity of meprin-α, a pro-migratory and pro-angiogenic protease, in colorectal cancer.
PLoS One 6(11):e26450.
Biniossek ML, Nägler DK, Becker-Pauly C, Schilling O. (2011)
Proteomic identification of protease cleavage sites characterizes prime and non-prime specificity of cysteine cathepsins B, L, and S.
J Proteome Res 10(12):5363-73.
Addison ML, Minnion JS, Shillito JC, Suzuki K, Tan TM, Field BC, Germain-Zito N, Becker-Pauly C, Ghatei MA, Bloom SR, Murphy KG. (2011)
A role for metalloendopeptidases in the breakdown of the gut hormone, PYY 3-36.
Endocrinology 152(12):4630-40.
Jefferson T, Čaušević M, auf dem Keller U, Schilling O, Isbert S, Geyer R, Maier W, Tschickardt S, Jumpertz T, Weggen S, Bond JS, Overall CM, Pietrzik CU, Becker-Pauly C. (2011)
Metalloprotease meprin beta generates nontoxic N-terminal amyloid precursor protein fragments in vivo.
J Biol Chem 286(31):27741-50.
Becker-Pauly C, Barré O, Schilling O, Auf dem Keller U, Ohler A, Broder C, Schütte A, Kappelhoff R, Stöcker W, Overall CM. (2011)
Proteomicanalyses reveal an acidic prime side specificity for the astacin metalloprotease family reflected by physiological substrates.
Mol Cell Proteomics 10(9):M111.009233.
Vazeille E, Bringer MA, Gardarin A, Chambon C, Becker-Pauly C, Pender SL, Jakob C, Müller S, Lottaz D, Darfeuille-Michaud A. (2011)
Role of meprins to protect ileal mucosa of Crohn's disease patients from colonization by adherent-invasive E. coli.
PLoS One 6(6):e21199.
Ohler A, Becker-Pauly C. (2011)
Morpholino knockdown of the ubiquitously expressed transmembrane serine protease TMPRSS4a in zebrafish embryos exhibits severe defects in organogenesis and cell adhesion.
Biol Chem 392(7):653-64.
Hedrich J, Lottaz D, Meyer K, Yiallouros I, Jahnen-Dechent W, Stöcker W, Becker-Pauly C. (2010)
Fetuin-A and cystatin C are endogenous inhibitors of human meprin metalloproteases.
Biochemistry 49(39):8599-607.
Kronenberg D, Bruns BC, Moali C, Vadon-Le Goff S, Sterchi EE, Traupe H, Böhm M, Hulmes DJ, Stöcker W, Becker-Pauly C. (2010)
Processing of procollagen III by meprins: new players in extracellular matrix assembly?
J Invest Dermatol 130(12):2727-35.
Ohler A, Debela M, Wagner S, Magdolen V, Becker-Pauly C. (2010)
Analyzing the protease web in skin: meprin metalloproteases are activated specifically by KLK4, 5 and 8 vice versa leading to processing of proKLK7 thereby triggering its activation.
Biol Chem 391(4):455-60.
Schütte A, Hedrich J, Stöcker W, Becker-Pauly C. (2010)
Let it flow: Morpholino knockdown in zebrafish embryos reveals a pro-angiogenic effect of the metalloprotease meprin alpha2.
PLoS One 5(1):e8835.
Ambort D, Brellier F, Becker-Pauly C, Stöcker W, Andrejevic-Blant S, Chiquet M, Sterchi EE. (2010)
Specific processing of tenascin-C by the metalloprotease meprinbeta neutralizes its inhibition of cell spreading.
Matrix Biol 29(1):31-42.
Aufenvenne K, Oji V, Walker T, Becker-Pauly C, Hennies HC, Stöcker W, Traupe H. (2009)
Transglutaminase-1 and bathing suit ichthyosis: molecular analysis of gene/environment interactions.
J Invest Dermatol 129(8):2068-71.
Becker-Pauly C, Bruns BC, Damm O, Schütte A, Hammouti K, Burmester T, Stöcker W. (2009)
News from an ancient world: two novel astacin metalloproteases from the horseshoe crab.
J Mol Biol 385(1):236-48.
Oneda B, Lods N, Lottaz D, Becker-Pauly C, Stöcker W, Pippin J, Huguenin M, Ambort D, Marti HP, Sterchi EE. (2008)
Metalloprotease meprin beta in rat kidney: glomerular localization and differential expression in glomerulonephritis.
PLoS One 3(5):e2278.
Schütte A, Lottaz D, Sterchi EE, Stöcker W, Becker-Pauly C. (2007)
Two alpha subunits and one beta subunit of meprin zinc-endopeptidases are differentially expressed in the zebrafish Danio rerio.
Biol Chem. 2007 May;388(5):523-31.
Borchert N, Becker-Pauly C, Wagner A, Fischer P, Stöcker W, Brattig NW. (2007)
Identification and characterization of onchoastacin, an astacin-like metalloproteinase from the filaria Onchocerca volvulus.
Microbes Infect 9(4):498-506.
Becker-Pauly C, Höwel M, Walker T, Vlad A, Aufenvenne K, Oji V, Lottaz D, Sterchi EE, Debela M, Magdolen V, Traupe H, Stöcker W. (2007)
The alpha and beta subunits of the metalloprotease meprin are expressed in separate layers of human epidermis, revealing different functions in keratinocyte proliferation and differentiation.
J Invest Dermatol 127(5):1115-25.
Hintze V, Höwel M, Wermter C, Grosse Berkhoff E, Becker-Pauly C, Beermann B, Yiallouros I, Stöcker W. (2006)
The interaction of recombinant subdomains of the procollagen C-proteinase with procollagen I provides a quantitative explanation for functional differences between the two splice variants, mammalian tolloid and bone morphogenetic protein 1.
Biochemistry 45(21):6741-8.
Kruse MN, Becker C, Lottaz D, Köhler D, Yiallouros I, Krell HW, Sterchi EE, Stöcker W. (2004)
Human meprin alpha and beta homo-oligomers: cleavage of basement membrane proteins and sensitivity to metalloprotease inhibitors.
Biochem J 378(Pt 2):383-9.
Becker C, Kruse MN, Slotty KA, Köhler D, Harris JR, Rösmann S, Sterchi EE, Stöcker W. (2003)
Differences in the activation mechanism between the alpha and beta subunits of human meprin.
Biol Chem 384(5):825-31.


Tredup C and Becker-Pauly C (2016)
Metalloproteases Meprin α and Meprin β in Health and Disease.
Encyclopedia of Cell Biology. Editors-in-Chief: Ralph A Bradshaw and Philip D Stahl, Elsevier.
Becker-Pauly C. & Rose-John S. (2015)
Meprin and ADAM Metalloproteases: Two sides of the same coin?
Matrix Metalloproteinase Biology, First Edition. Edited by Irit Sagi & Jean Gaffney. John Wiley & Sons
Stöcker W, Möhrlen F, Becker-Pauly C (2013)
Other astacin homologues
In: Handbook of Proteolytic Enzymes, 3rd ed, Salvesen G, Rawlings ND, eds, Elsevier, 956-961
Beaufort N, Magdolen V., Sommerhoff C.P., Becker-Pauly C (2012)
Kallikrein-Related Peptidases within the Proteolytic Web (editor Dr. Viktor Magdolen a.o. (ed.)
Kallikrein-Related Peptidases: Characterization, regulation, and interactions within the protease web.
De Gruyter GmbH & Co. KG, Berlin / New York)
Becker-Pauly, C. (2011)
The Metalloproteases Meprin α and β: Pathophysiological roles in Inflammation, Cardiovascular Disease, Cancer, and Fibrosis.
(invited book chapter in: Dr. Ben Dunn (ed.) Proteinases as Drug Targets, RSC Publishing)
Becker-Pauly, C. & Stöcker, W. (2010)
Insect cells for heterologous production of recombinant proteins.
(invited book chapter in: Dr. Andreas Vilcinskas (ed.) Insect Biotechnology, Springer Publishing)
Original Publications
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