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Prof. Dr. Christoph Becker-Pauly

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

Publications

 
Original Publications & Reviews
Books
 

Original Publications & Reviews

 
76
Role of meprin metalloproteases in metastasis and tumor microenvironment.
Peters F, Becker-Pauly C.
Cancer Metastasis Rev. 2019 Sep 3. doi: 10.1007/s10555-019-09805-5. [Epub ahead of print] Review.
 
75
IL-6 trans-signaling in the brain influences the behavioral and physio-pathological phenotype of the Tg2576 and 3xTgAD mouse models of Alzheimer's disease.
Escrig A, Canal C, Sanchis P, Fernández-Gayol O, Montilla A, Comes G, Molinero A, Giralt M, Giménez-Llort L, Becker-Pauly C, Rose-John S, Hidalgo J.
Brain Behav Immun. 2019 Aug 8. pii: S0889-1591(19)30150-3. doi: 10.1016/j.bbi.2019.08.005. [Epub ahead of print]
 
74
Meprin β induces activities of A disintegrin and metalloproteinases 9, 10, and 17 by specific prodomain cleavage.
Wichert R, Scharfenberg F, Colmorgen C, Koudelka T, Schwarz J, Wetzel S, Potempa B, Potempa J, Bartsch JW, Sagi I, Tholey A, Saftig P, Rose-John S, Becker-Pauly C.
FASEB J. 2019 Aug 9:fj201801371R. doi: 10.1096/fj.201801371R. [Epub ahead of print]
 
73
Differences in Shedding of the Interleukin-11 Receptor by the Proteases ADAM9, ADAM10, ADAM17, Meprin α, Meprin β and MT1-MMP.
Sammel M, Peters F, Lokau J, Scharfenberg F, Werny L, Linder S, Garbers C, Rose-John S, Becker-Pauly C.
Int J Mol Sci. 2019 Jul 26;20(15)
 
72
Degradome of soluble ADAM10 and ADAM17 metalloproteases.
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.
Cell Mol Life Sci. 2019 Jun 17. doi: 10.1007/s00018-019-03184-4. [Epub ahead of print]
 
71
Regulation of the alternative β-secretase meprin β by ADAM-mediated shedding.
Scharfenberg F, Armbrust F, Marengo L, Pietrzik C, Becker-Pauly C.
Cell Mol Life Sci. 2019 Aug;76(16):3193-3206. Review
 
70
The cancer associated meprin β variant p.G32R provides an additional activation site and promotes cancer cell invasion.
Schäffler H, Li W, Helm O, Krüger S, Böger C, Peters F, Röcken C, Sebens S, Lucius R, Becker-Pauly C, Arnold P.
J Cell Sci. 2019 May 31;132(11)
 
69
Tethering soluble meprin α in an enzyme complex to the cell surface affects IBD-associated genes.
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.
FASEB J. 2019 Jun;33(6):7490-7504
 
68
Mammalian plasma fetuin-B is a selective inhibitor of ovastacin and meprin metalloproteinases.
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.
Sci Rep. 2019 Jan 24;9(1):546
 
67
Inhibitors of BMP-1/tolloid-like proteinases: efficacy, selectivity and cellular toxicity.
Talantikite M, Lécorché P, Beau F, Damour O, Becker-Pauly C, Ho WB, Dive V, Vadon-Le Goff S, Moali C.
FEBS Open Bio. 2018 Nov 12;8(12):2011-2021
 
66
The metalloprotease ADAMTS4 generates N-truncated Aβ4-x species and marks oligodendrocytes as a source of amyloidogenic peptides in Alzheimer's disease.
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.
Acta Neuropathol. 2019 Feb;137(2):239-257
 
65
Propeptide glycosylation and galectin-3 binding decrease proteolytic activation of human proMMP-9/progelatinase B.
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.
FEBS J. 2019 Mar;286(5):930-945
 
64
Docking of Meprin α to Heparan Sulphate Protects the Endothelium from Inflammatory Cell Extravasation.
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.
Thromb Haemost. 2018 Oct;118(10):1790-1802
 
63
ADAM17 is required for EGF-R-induced intestinal tumors via IL-6 trans-signaling.
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.
J Exp Med. 2018 Apr 2;215(4):1205-1225
 
62
Mucus Detachment by Host Metalloprotease Meprin β Requires Shedding of Its Inactive Pro-form, which Is Abrogated by the Pathogenic Protease RgpB.
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.
Cell Rep. 2017 Nov 21;21(8):2090-2103
 
61
Cancer-associated mutations in the canonical cleavage site do not influence CD99 shedding by the metalloprotease meprin β but alter cell migration in vitro.
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.
Oncotarget. 2017 Jul 4;8(33):54873-54888
 
60
Meprin metalloproteases: Molecular regulation and function in inflammation and fibrosis.
Arnold P, Otte A, Becker-Pauly C.
Biochim Biophys Acta Mol Cell Res. 2017 Nov;1864(11 Pt B):2096-2104. Review
 
59
Meprin β and BMP-1 are differentially regulated by CaCl2.
Schneppenheim J, Scharfenberg F, Lucius R, Becker-Pauly C, Arnold P.
Cell Calcium. 2017 Jul;65:8-13
 
58
Meprin Metalloproteases Generate Biologically Active Soluble Interleukin-6 Receptor to Induce Trans-Signaling.
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.
Sci Rep. 2017 Mar 9;7:44053
 
57
The Metalloprotease Meprin β Is an Alternative β-Secretase of APP.
Becker-Pauly C, Pietrzik CU.
Front Mol Neurosci. 2017 Jan 5;9:159. Review
 
56
Proteolytic Origin of the Soluble Human IL-6R In Vivo and a Decisive Role of N-Glycosylation.
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.
Front Mol Neurosci. 2017 Jan 5;9:159
 
55
Meprin β contributes to collagen deposition in lung fibrosis.
Biasin V, Wygrecka M, Marsh LM, Becker-Pauly C, Brcic L, Ghanim B, Klepetko W, Olschewski A, Kwapiszewska G.
Sci Rep. 2017 Jan 6;7:39969
 
54
Ectodomain shedding of CD99 within highly conserved regions is mediated by the metalloprotease meprin β and promotes transendothelial cell migration.
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.
FASEB J. 2017 Mar;31(3):1226-1237
 
53
Metalloproteinase meprin α regulates migration and invasion of human hepatocarcinoma cells and is a mediator of the oncoprotein Reptin.
Breig O, Yates M, Neaud V, Couchy G, Grigoletto A, Lucchesi C, Prox J, Zucman-Rossi J, Becker-Pauly C, Rosenbaum J.
Oncotarget. 2017 Jan 31;8(5):7839-7851
 
52
Novel Potent Proline-Based Metalloproteinase Inhibitors: Design, (Radio)Synthesis, and First in Vivo Evaluation as Radiotracers for Positron Emission Tomography.
Kalinin DV, Wagner S, Riemann B, Hermann S, Schmidt F, Becker-Pauly C, Rose-John S, Schäfers M, Holl R.
J Med Chem. 2016 Oct 27;59(20):9541-9559
 
51
Discovery of an enzyme and substrate selective inhibitor of ADAM10 using an exosite-binding glycosylated substrate.
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.
Sci Rep. 2016 Dec 5;6(1):11
 
50
Deficiency of the DSPP-cleaving enzymes meprin α and meprin β does not result in dentin malformation in mice.
Arnold P, Koopmann L, Peters F, Birkenfeld F, Goff SV, Damm T, Qin C, Moali C, Lucius R, Becker-Pauly C.
Cell Tissue Res. 2017 Feb;367(2):351-358
 
49
Mice are not Men: ADAM30 Findings Emphasize a Broader Look Towards Murine Alzheimer's Disease Models.
Becker-Pauly C, Pietrzik CU.
EBioMedicine. 2016 Jul;9:19-20
 
48
Tetraspanin 8 is an interactor of the metalloprotease meprin β within tetraspanin-enriched microdomains.
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.
Biol Chem. 2016 Sep 1;397(9):857-69
 
47
The intact Kunitz domain protects the amyloid precursor protein from being processed by matriptase-2.
Beckmann AM, Glebov K, Walter J, Merkel O, Mangold M, Schmidt F, Becker-Pauly C, Gütschow M, Stirnberg M.
Biol Chem. 2016 Aug 1;397(8):777-90
 
46
Development and Validation of a Small Single-domain Antibody That Effectively Inhibits Matrix Metalloproteinase 8.
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.
Mol Ther. 2016 May;24(5):890-902
 
45
Generation of aggregation prone N-terminally truncated amyloid β peptides by meprin β depends on the sequence specificity at the cleavage site.
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.
Mol Neurodegener. 2016 Feb 19;11:19
 
44
Human and murine Interleukin 23 receptors are novel substrates for a disintegrin and metalloproteases ADAM10 and ADAM17.
Franke M, Schröder J, Monhasery N, Ackfeld T, Hummel TM, Rabe B, Garbers C, Becker-Pauly C, Floss DM, Scheller J.
J Biol Chem. 2016 May 13;291(20):10551-61
 
43
The role of interleukin-6 signaling in nervous tissue.
Rothaug M, Becker-Pauly C, Rose-John S.
Biochim Biophys Acta. 2016 Jun;1863(6 Pt A):1218-27. Review
 
42
Determination of Cleavage Site of Reelin between Its Sixth and Seventh Repeat and Contribution of Meprin Metalloproteases to the Cleavage.
Sato Y, Kobayashi D, Kohno T, Kidani Y, Prox J, Becker-Pauly C, Hattori M.
J Biochem. 2016 Mar;159(3):305-12
 
41
Enhanced Peptide Stability Against Protease Digestion Induced by Intrinsic Factor Binding of a Vitamin B12 Conjugate of Exendin-4.
Bonaccorso RL, Chepurny OG, Becker-Pauly C, Holz GG, Doyle RP.
Mol Pharm. 2015 Sep 8;12(9):3502-6
 
40
Metalloprotease meprin β is activated by transmembrane serine protease matriptase-2 at the cell surface thereby enhancing APP shedding.
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.
Biochem J. 2015 Aug 15;470(1):91-103
 
39
Calcium negatively regulates meprin β activity and attenuates substrate cleavage.
Arnold P, Schmidt F, Prox J, Zunke F, Pietrzik C, Lucius R, Becker-Pauly C.
FASEB J. 2015 Aug;29(8):3549-57
 
38
Evaluation of ¹¹¹In-Labelled Exendin-4 Derivatives Containing Different Meprin β-Specific Cleavable Linkers.
Jodal A, Pape F, Becker-Pauly C, Maas O, Schibli R, Béhé M.
PLoS One. 2015 Apr 9;10(4):e0123443
 
37
Meprin α and meprin β: Procollagen proteinases in health and disease.
Prox J, Arnold P, Becker-Pauly C.
Matrix Biol. 2015 May-Jul;44-46:7-13
 
36
Microbial-induced meprin β cleavage in MUC2 mucin and a functional CFTR channel are required to release anchored small intestinal mucus.
Schütte A, Ermund A, Becker-Pauly C, Johansson ME, Rodriguez-Pineiro AM, Bäckhed F, Müller S, Lottaz D, Bond JS, Hansson GC.
Proc Natl Acad Sci U S A. 2014 Aug 26;111(34):12396-401
 
35
Development of high throughput screening assays and pilot screen for inhibitors of metalloproteases meprin α and β.
Madoux F, Tredup C, Spicer TP, Scampavia L, Chase PS, Hodder PS, Fields GB, Becker-Pauly C, Minond D.
Biopolymers. 2014 Sep;102(5):396-406
 
34
LC-MS based cleavage site profiling of the proteases ADAM10 and ADAM17 using proteome-derived peptide libraries.
Tucher J, Linke D, Koudelka T, Cassidy L, Tredup C, Wichert R, Pietrzik C, Becker-Pauly C, Tholey A.
J Proteome Res. 2014 Apr 4;13(4):2205-14
 
33
Mapping orphan proteases by proteomics: Meprin metalloproteases deciphered as potential therapeutic targets.
Becker-Pauly C, Broder C, Prox J, Koudelka T, Tholey A.
Proteomics Clin Appl. 2014 Jun;8(5-6):382-8
 
32
Short-term TNFα shedding is independent of cytoplasmic phosphorylation or furin cleavage of ADAM17.
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.
Biochim Biophys Acta. 2013 Dec;1833(12):3355-3367
 
31
Metalloproteases meprin α and meprin β are C- and N-procollagen proteinases important for collagen assembly and tensile strength.
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.
Proc Natl Acad Sci U S A. 2013 Aug 27;110(35):14219-24
 
30
TNFα cleavage beyond TACE/ADAM17: matrix metalloproteinase 13 is a potential therapeutic target in sepsis and colitis.
Becker-Pauly C, Rose-John S.
EMBO Mol Med. 2013 Jul;5(7):970-2
 
29
The metalloproteases meprin α and meprin β: unique enzymes in inflammation, neurodegeneration, cancer and fibrosis.
Broder C, Becker-Pauly C.
Biochem J. 2013 Mar 1;450(2):253-64
 
28
The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin β and ADAM10.
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.
Cell Mol Life Sci. 2013 Jan;70(2):309-33
 
27
Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane.
Arolas JL, Broder C, Jefferson T, Guevara T, Sterchi EE, Bode W, Stöcker W, Becker-Pauly C, Gomis-Rüth FX.
Proc Natl Acad Sci U S A. 2012 Oct 2;109(40):16131-6
 
26
Meprins process matrix metalloproteinase-9 (MMP-9)/gelatinase B and enhance the activation kinetics by MMP-3.
Geurts N, Becker-Pauly C, Martens E, Proost P, Van den Steen PE, Stöcker W, Opdenakker G.
FEBS Lett. 2012 Dec 14;586(24):4264-9
 
25
Sizzled is unique among secreted frizzled-related proteins for its ability to specifically inhibit bone morphogenetic protein-1 (BMP-1)/tolloid-like proteinases.
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.
J Biol Chem. 2012 Sep 28;287(40):33581-93
 
24
The metalloprotease meprin β generates amino terminal-truncated amyloid β peptide species.
Bien J, Jefferson T, Causević M, Jumpertz T, Munter L, Multhaup G, Weggen S, Becker-Pauly C, Pietrzik CU.
J Biol Chem. 2012 Sep 28;287(40):33304-13
 
23
TMPRSS4 is a type II transmembrane serine protease involved in cancer and viral infections.
Ohler A, Becker-Pauly C.
Biol Chem. 2012 Sep;393(9):907-14
 
22
Meprin α transactivates the epidermal growth factor receptor (EGFR) via ligand shedding, thereby enhancing colorectal cancer cell proliferation and migration.
Minder P, Bayha E, Becker-Pauly C, Sterchi EE.
JJ Biol Chem. 2012 Oct 12;287(42):35201-11
 
21
Enhanced activity of meprin-α, a pro-migratory and pro-angiogenic protease, in colorectal cancer.
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.
PLoS One. 2011;6(11):e26450
 
20
Proteomic identification of protease cleavage sites characterizes prime and non-prime specificity of cysteine cathepsins B, L, and S.
Biniossek ML, Nägler DK, Becker-Pauly C, Schilling O.
J Proteome Res. 2011 Dec 2;10(12):5363-73
 
19
A role for metalloendopeptidases in the breakdown of the gut hormone, PYY 3-36.
Addison ML, Minnion JS, Shillito JC, Suzuki K, Tan TM, Field BC, Germain-Zito N, Becker-Pauly C, Ghatei MA, Bloom SR, Murphy KG.
Endocrinology. 2011 Dec;152(12):4630-40
 
18
Metalloprotease meprin beta generates nontoxic N-terminal amyloid precursor protein fragments in vivo.
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.
J Biol Chem. 2011 Aug 5;286(31):27741-50
 
17
Proteomicanalyses reveal an acidic prime side specificity for the astacin metalloprotease family reflected by physiological substrates.
Becker-Pauly C, Barré O, Schilling O, Auf dem Keller U, Ohler A, Broder C, Schütte A, Kappelhoff R, Stöcker W, Overall CM.
Mol Cell Proteomics. 2011 Sep;10(9):M111.009233
 
16
Role of meprins to protect ileal mucosa of Crohn's disease patients from colonization by adherent-invasive E. coli.
Vazeille E, Bringer MA, Gardarin A, Chambon C, Becker-Pauly C, Pender SL, Jakob C, Müller S, Lottaz D, Darfeuille-Michaud A.
PLoS One. 2011;6(6):e21199
 
15
Morpholino knockdown of the ubiquitously expressed transmembrane serine protease TMPRSS4a in zebrafish embryos exhibits severe defects in organogenesis and cell adhesion.
Ohler A, Becker-Pauly C.
Biol Chem. 2011 Jul;392(7):653-64
 
14
Fetuin-A and cystatin C are endogenous inhibitors of human meprin metalloproteases.
Hedrich J, Lottaz D, Meyer K, Yiallouros I, Jahnen-Dechent W, Stöcker W, Becker-Pauly C.
Biochemistry. 2010 Oct 5;49(39):8599-607
 
13
Processing of procollagen III by meprins: new players in extracellular matrix assembly?
Kronenberg D, Bruns BC, Moali C, Vadon-Le Goff S, Sterchi EE, Traupe H, Böhm M, Hulmes DJ, Stöcker W, Becker-Pauly C.
J Invest Dermatol. 2010 Dec;130(12):2727-35
 
12
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.
Ohler A, Debela M, Wagner S, Magdolen V, Becker-Pauly C.
Biol Chem. 2010 Apr;391(4):455-60
 
11
Let it flow: Morpholino knockdown in zebrafish embryos reveals a pro-angiogenic effect of the metalloprotease meprin alpha2.
Schütte A, Hedrich J, Stöcker W, Becker-Pauly C.
PLoS One. 2010 Jan 21;5(1):e8835
 
10
Specific processing of tenascin-C by the metalloprotease meprinbeta neutralizes its inhibition of cell spreading.
Ambort D, Brellier F, Becker-Pauly C, Stöcker W, Andrejevic-Blant S, Chiquet M, Sterchi EE.
Matrix Biol. 2010 Jan;29(1):31-42
 
9
Transglutaminase-1 and bathing suit ichthyosis: molecular analysis of gene/environment interactions.
Aufenvenne K, Oji V, Walker T, Becker-Pauly C, Hennies HC, Stöcker W, Traupe H.
J Invest Dermatol. 2009 Aug;129(8):2068-71
 
8
News from an ancient world: two novel astacin metalloproteases from the horseshoe crab.
Becker-Pauly C, Bruns BC, Damm O, Schütte A, Hammouti K, Burmester T, Stöcker W.
J Mol Biol. 2009 Jan 9;385(1):236-48
 
7
Metalloprotease meprin beta in rat kidney: glomerular localization and differential expression in glomerulonephritis.
Oneda B, Lods N, Lottaz D, Becker-Pauly C, Stöcker W, Pippin J, Huguenin M, Ambort D, Marti HP, Sterchi EE.
PLoS One. 2008 May 28;3(5):e2278
 
6
Two alpha subunits and one beta subunit of meprin zinc-endopeptidases are differentially expressed in the zebrafish Danio rerio.
Schütte A, Lottaz D, Sterchi EE, Stöcker W, Becker-Pauly C.
Biol Chem. 2007 May;388(5):523-31
 
5
Identification and characterization of onchoastacin, an astacin-like metalloproteinase from the filaria Onchocerca volvulus.
Borchert N, Becker-Pauly C, Wagner A, Fischer P, Stöcker W, Brattig NW.
Microbes Infect. 2007 Apr;9(4):498-506
 
4
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.
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.
J Invest Dermatol. 2007 May;127(5):1115-25
 
3
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.
Hintze V, Höwel M, Wermter C, Grosse Berkhoff E, Becker-Pauly C, Beermann B, Yiallouros I, Stöcker W.
Biochemistry. 2006 May 30;45(21):6741-8
 
2
Human meprin alpha and beta homo-oligomers: cleavage of basement membrane proteins and sensitivity to metalloprotease inhibitors.
Kruse MN, Becker C, Lottaz D, Köhler D, Yiallouros I, Krell HW, Sterchi EE, Stöcker W.
Biochem J. 2004 Mar 1;378(Pt 2):383-9
 
1
Differences in the activation mechanism between the alpha and beta subunits of human meprin.
Becker C, Kruse MN, Slotty KA, Köhler D, Harris JR, Rösmann S, Sterchi EE, Stöcker W.
Biol Chem. 2003 May;384(5):825-31
 

Books

 
6
Metalloproteases Meprin α and Meprin β in Health and Disease.
Tredup C and Becker-Pauly C
Encyclopedia of Cell Biology. Editors-in-Chief: Ralph A Bradshaw and Philip D Stahl, Elsevier.
 
5
Meprin and ADAM Metalloproteases: Two sides of the same coin?
Becker-Pauly C. & Rose-John S.
Matrix Metalloproteinase Biology, First Edition. Edited by Irit Sagi & Jean Gaffney. John Wiley & Sons
 
4
Other astacin homologues
Stöcker W, Möhrlen F, Becker-Pauly C
In: Handbook of Proteolytic Enzymes, 3rd ed, Salvesen G, Rawlings ND, eds, Elsevier, 956-961
 
3
Kallikrein-Related Peptidases within the Proteolytic Web (editor Dr. Viktor Magdolen a.o. (ed.)
Beaufort N, Magdolen V., Sommerhoff C.P., Becker-Pauly C
Kallikrein-Related Peptidases: Characterization, regulation, and interactions within the protease web.
De Gruyter GmbH & Co. KG, Berlin / New York)
 
2
The Metalloproteases Meprin α and β: Pathophysiological roles in Inflammation, Cardiovascular Disease, Cancer, and Fibrosis.
Becker-Pauly, C.
(invited book chapter in: Dr. Ben Dunn (ed.) Proteinases as Drug Targets, RSC Publishing)
 
1
Insect cells for heterologous production of recombinant proteins.
Becker-Pauly, C. & Stöcker, W.
(invited book chapter in: Dr. Andreas Vilcinskas (ed.) Insect Biotechnology, Springer Publishing)
 
Original Publications
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Last Change/Letzte Änderung: September 6, 2019