E. Sterchi

发表

Expression and intracellular transport of microvillus membrane hydrolases in human intestinal epithelial cells

H. Hauri, J. Fransen, E. Sterchi, 1985, The Journal of cell biology.

Expression Membrane and Intracellular Transport of Microvillus Hydrolases in Human Intestinal Epithelial Cells

Erwin, H. Hauri, J. Fransen, 2002 .

Meprins, membrane-bound and secreted astacin metalloproteinases.

J. S. Bond, E. Sterchi, W. Stöcker, 2008, Molecular aspects of medicine.

Human lactase‐phlorizin hydrolase expressed in COS‐1 cells is proteolytically processed by the lysosomal pathway

E. Sterchi, M. Wüthrich, 1997, FEBS letters.

The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin β and ADAM10

A. Chalaris, S. Rose-John, C. Overall, 2012, Cellular and Molecular Life Sciences.

Sucrase-isomaltase deficiency in humans. Different mutations disrupt intracellular transport, processing, and function of an intestinal brush border enzyme.

H. Hauri, H. Naim, P. Milla, 1988, The Journal of clinical investigation.

A Novel Type of Detergent-resistant Membranes May Contribute to an Early Protein Sorting Event in Epithelial Cells*

R. Busche, H. Naim, K. Zimmer, 2005, Journal of Biological Chemistry.

C-cytosolic and transmembrane domains of the N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase alpha subunit (human meprin alpha) are essential for its retention in the endoplasmic reticulum and C-terminal processing.

E. Sterchi, D. Lottaz, D. Hahn, 1997, European journal of biochemistry.

Activation of the Epidermal Growth Factor Receptor (EGFR) by a Novel Metalloprotease Pathway*

N. McElvaney, C. Greene, S. O’Neill, 2008, Journal of Biological Chemistry.

Cloning of the PABA peptide hydrolase alpha subunit (PPHα) from human small intestine and its expression in COS‐1 cells

E. Sterchi, Weiping Jiang, J. Grünberg, 1993, FEBS letters.

Compartmentalised expression of meprin in small intestinal mucosa: enhanced expression in lamina propria in coeliac disease

T. Macdonald, E. Sterchi, G. Monteleone, 2007, Biological chemistry.

Immunohistological evidence, obtained with monoclonal antibodies, of small intestinal brush border hydrolases in human colon cancers and foetal colons

H. Hauri, A. Zweibaum, B. Sordat, 1984, International journal of cancer.

Tetraspanin 8 is an interactor of the metalloprotease meprin β within tetraspanin-enriched microdomains

W. Annaert, D. Schmidt-Arras, O. Janssen, 2016, Biological chemistry.

Tetraspanin 8 is an interactor of the metalloprotease meprin β within tetraspanin-enriched microdomains.

W. Annaert, D. Schmidt-Arras, O. Janssen, 2016, Biological chemistry.

Human meprin α and β homo-oligomers: cleavage of basement membrane proteins and sensitivity to metalloprotease inhibitors

H. Krell, E. Sterchi, D. Lottaz, 2004 .

Hydrolysis of proteins and proteolytic activity.

M. Lentze, E. Sterchi, 1983, Journal of pediatric gastroenterology and nutrition.

Human lactase-phlorizin hydrolase is not processed by furin, PC1/PC3, PC2, PACE4 and PC5/PC6A of the family of subtilisin-like proprotein processing proteases.

W. V. D. Van de Ven, J. Creemers, E. Sterchi, 1996, Biochimica et biophysica acta.

Proteolytic enzymes : tools and targets

E. Sterchi, W. Stöcker, 1999 .

Activation of Human Meprin-α in a Cell Culture Model of Colorectal Cancer Is Triggered by the Plasminogen-activating System*

E. Sterchi, D. Lottaz, W. Stöcker, 2002, The Journal of Biological Chemistry.

Maturation of human lactase‐phlorizin hydrolase Proteolytic cleavage of precursor occurs after passage through the Golgi complex

G. Semenza, E. Sterchi, D. Lottaz, 1992, FEBS letters.

Specific processing of tenascin-C by the metalloprotease meprinbeta neutralizes its inhibition of cell spreading.

S. Andrejevic-Blant, M. Chiquet, E. Sterchi, 2010, Matrix biology : journal of the International Society for Matrix Biology.

The Metalloprotease Meprinβ Processes E-Cadherin and Weakens Intercellular Adhesion

B. Oneda, E. Sterchi, D. Lottaz, 2008, PloS one.

Metalloprotease Meprinβ in Rat Kidney: Glomerular Localization and Differential Expression in Glomerulonephritis

J. Pippin, H. Marti, B. Oneda, 2008, PloS one.

The α and β Subunits of the Metalloprotease Meprin Are Expressed in Separate Layers of Human Epidermis, Revealing Different Functions in Keratinocyte Proliferation and Differentiation

V. Magdolen, E. Sterchi, C. Becker-Pauly, 2007 .

Differences in the Activation Mechanism between the α and β Subunits of Human Meprin

J. Harris, E. Sterchi, W. Stöcker, 2003 .

Secretion of human meprin from intestinal epithelial cells depends on differential expression of the α and β subunits

E. Sterchi, D. Lottaz, D. Hahn, 1999 .

Biogenesis of intestinal lactase-phlorizin hydrolase in adults with lactose intolerance. Evidence for reduced biosynthesis and slowed-down maturation in enterocytes.

H. Hauri, J. Fransen, H. Naim, 1990, The Journal of clinical investigation.

Molecular aspects of disaccharidase deficiencies.

H. Naim, M. Lentze, E. Sterchi, 1990, Bailliere's clinical gastroenterology.

Congenital Maltase-Glucoamylase Deficiency Associated With Lactase and Sucrase Deficiencies

D. Swallow, P. Sen, B. Nichols, 2002, Journal of pediatric gastroenterology and nutrition.

Structure, biosynthesis, and glycosylation of human small intestinal maltase-glucoamylase.

H. Naim, M. Lentze, E. Sterchi, 1988, The Journal of biological chemistry.

Proteolytic processing of human intestinal lactase‐phlorizin hydrolase precursor is not a prerequisite for correct sorting in Madin Darby canine kidney (MDCK) cells

E. Sterchi, J. Grünberg, U. Luginbühl, 1992, FEBS letters.

Expression of the alpha subunit of PABA peptide hydrolase (EC 3.4.24.18) in MDCK cells

E. Sterchi, J. Grünberg, J. Eldering, 1993, FEBS letters.

Processing of procollagen III by meprins: new players in extracellular matrix assembly?

S. Vadon-Le Goff, C. Moali, D. Hulmes, 2010, The Journal of investigative dermatology.

Biosynthesis of N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase: disulfide-linked dimers are formed at the site of synthesis in the rough endoplasmic reticulum.

H. Naim, M. Lentze, E. Sterchi, 1988, Archives of biochemistry and biophysics.

Peptide hydrolases of the human small intestinal mucosa: distribution of activities between brush border membranes and cytosol.

E. Sterchi, J. Woodley, 1980, Clinica chimica acta; international journal of clinical chemistry.

Inhibition of recombinant human maltase glucoamylase by salacinol and derivatives

B. M. Pinto, D. Kuntz, B. Nichols, 2006, The FEBS journal.

Peptide hydrolases of the human small intestinal mucosa: identification of six distinct enzymes in the brush border membrane.

E. Sterchi, J. Woodley, 1980, Clinica chimica acta; international journal of clinical chemistry.

Luminal Substrate “Brake” on Mucosal Maltase-glucoamylase Activity Regulates Total Rate of Starch Digestion to Glucose

G. Brayer, B. Hamaker, S. Baker, 2007, Journal of pediatric gastroenterology and nutrition.

Luminal starch substrate "brake" on maltase-glucoamylase activity is located within the glucoamylase subunit.

G. Brayer, B. Hamaker, B. Nichols, 2008, The Journal of nutrition.

N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase: a metalloendopeptidase of the human intestinal microvillus membrane which degrades biologically active peptides.

H. Hauri, J. Fransen, H. Naim, 1988, Archives of biochemistry and biophysics.

Moderating carbohydrate digestion rate promotes metabolic flexibility in mice

N. Butte, B. Hamaker, B. Nichols, 2023, bioRxiv.

The maltase-glucoamylase gene: Common ancestry to sucrase-isomaltase with complementary starch digestion activities

D. Swallow, P. Sen, B. Nichols, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Meprinα Transactivates the Epidermal Growth Factor Receptor (EGFR) via Ligand Shedding, thereby Enhancing Colorectal Cancer Cell Proliferation and Migration*

E. Sterchi, C. Becker-Pauly, E. Bayha, 2012, The Journal of Biological Chemistry.

Transport to cell surface of intestinal sucrase-isomaltase is blocked in the Golgi apparatus in a patient with congenital sucrase-isomaltase deficiency.

H. Hauri, J. Roth, M. Lentze, 1985, Proceedings of the National Academy of Sciences of the United States of America.

Characteristics of maltase activity in amniotic fluid.

H. J. Sips, H. Hauri, E. Sterchi, 1985, Clinica chimica acta; international journal of clinical chemistry.

Proteolytic Enzymes

E. Sterchi, W. Stocker, 1999, Springer Lab Manual.

Contribution of mucosal maltase-glucoamylase activities to mouse small intestinal starch alpha-glucogenesis.

S. Wattler, M. Nehls, G. Brayer, 2007, The Journal of nutrition.

The Nature of Raw Starch Digestion

B. Hamaker, B. Nichols, D. Rose, 2012, Journal of pediatric gastroenterology and nutrition.

Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.

B. Nichols, D. Rose, E. Sterchi, 2008, Journal of molecular biology.

Biosynthesis of the human sucrase-isomaltase complex. Differential O-glycosylation of the sucrase subunit correlates with its position within the enzyme complex.

H. Naim, M. Lentze, E. Sterchi, 1988, The Journal of biological chemistry.

Biosynthesis and maturation of lactase-phlorizin hydrolase in the human small intestinal epithelial cells.

H. Naim, M. Lentze, E. Sterchi, 1987, The Biochemical journal.

Mucosal maltase-glucoamylase plays a crucial role in starch digestion and prandial glucose homeostasis of mice.

N. Butte, J. Marini, B. Hamaker, 2009, The Journal of nutrition.

Disaccharidase Activities in Dyspeptic Children: Biochemical and Molecular Investigations of Maltase-Glucoamylase Activity

D. Swallow, P. Sen, B. Nichols, 2002, Journal of pediatric gastroenterology and nutrition.

Human Small Intestinal Maltase-glucoamylase cDNA Cloning

B. Nichols, A. Quaroni, E. Sterchi, 1998, The Journal of Biological Chemistry.

Biochemical mechanisms in congenital enzyme deficiencies of the small intestine.

H. Hauri, J. Green, E. Sterchi, 1981, Clinics in gastroenterology.

Nonpolarized secretion of human meprin alpha in colorectal cancer generates an increased proteolytic potential in the stroma.

M. Büchler, C. Maurer, E. Sterchi, 1999, Cancer research.

Enhanced Activity of Meprin-α, a Pro-Migratory and Pro-Angiogenic Protease, in Colorectal Cancer

A. Noël, H. Friess, C. Maurer, 2011, PloS one.

MEP1A allele for meprin A metalloprotease is a susceptibility gene for inflammatory bowel disease

T. Ahmad, D. Jewell, F. Seibold, 2009, Mucosal Immunology.

Two α subunits and one β subunit of meprin zinc-endopeptidases are differentially expressed in the zebrafish Danio rerio

E. Sterchi, C. Becker-Pauly, D. Lottaz, 2007, Biological chemistry.

Letter to the Editor: The Distribution of Brush Border Peptidases along the Small Intestine of the Adult Human

E. Sterchi, 1981, Pediatric Research.

Human meprin alpha and beta homo-oligomers: cleavage of basement membrane proteins and sensitivity to metalloprotease inhibitors.

H. Krell, E. Sterchi, D. Lottaz, 2004, The Biochemical journal.

Non-pancreatic hydrolysis of N-benzoyl-l-tyrosyl-p-aminobenzoic acid (PABA-peptide) in the human small intestine.

M. Lentze, J. Green, E. Sterchi, 1982, Clinical science.

Phorbol 12-Myristate 13-Acetate-induced Ectodomain Shedding and Phosphorylation of the Human Meprinβ Metalloprotease*

B. Leuenberger, E. Sterchi, D. Hahn, 2003, Journal of Biological Chemistry.

Sample preparation of culture medium from Madin-Darby canine kidney cells.

E. Sterchi, D. Lottaz, Daniel Ambort, 2008, Methods in molecular biology.

The constitutive exocytotic pathway in microvillous atrophy.

H. Hauri, J. Fransen, E. Sterchi, 1993, Journal of pediatric gastroenterology and nutrition.

2 – Protein Structure and Function of Brush Border Enzymes in Clinical Mucosal Disorders

H. Naim, M. Lentze, E. Sterchi, 1990 .

Purification and biosynthesis of the brush-border hydrolases of the human small intestine

H. Hauri, H. Naim, M. Lentze, 1986 .

39. AN IN VITRO MODEL SYSTEM FOR STUDYING THE BIOSYNTHESIS OF BRUSH BORDER MEMBRANE (BBM) HYDROLASES IN COELIAC DISEASE (CD)

M. Lentze, E. Sterchi, H. Nairn, 1987, Pediatric Research.

Evidence of native starch degradation with human small intestinal maltase‐glucoamylase (recombinant)

B. Hamaker, B. Nichols, E. Sterchi, 2007, FEBS letters.

Endopeptidase activity of the small intestine

E. Sterchi, J. Woodley, 1978 .

Meprin mRNA in rat intestine during normal and glucocorticoid‐induced maturation: divergent patterns of expression of α and β subunits

S. Henning, E. Sterchi, D. Lottaz, 1999 .

Maturation of human intestinal lactase-phlorizin hydrolase: generation of the brush border form of the enzyme involves at least two proteolytic cleavage steps.

R. Jacob, H. Naim, E. Sterchi, 1996, European journal of biochemistry.

Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane

W. Bode, F. Gomis-Rüth, J. Arolas, 2012, Proceedings of the National Academy of Sciences.

Human meprin beta: O-linked glycans in the intervening region of the type I membrane protein protect the C-terminal region from proteolytic cleavage and diminish its secretion.

B. Leuenberger, E. Sterchi, D. Hahn, 2003, The Biochemical journal.

The digestion and absorption of dietary protein

A. Makin, E. Sterchi, J. Woodley, 1980 .

Immuno-electronmicroscopical localization of a microvillus membrane disaccharidase in the human small-intestinal epithelium with monoclonal antibodies.

H. Hauri, J. Fransen, E. Sterchi, 1985, European journal of cell biology.

Sucrase-Isomaltase Provide Evidence for the Existence of an Intracellular Sorting Signal in the Isomaltase Subunit

H. Hauri, J. Fransen, M. Lentze, 2002 .

Polarised expression of human intestinal N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase (human meprin) alpha and beta subunits in Madin-Darby canine kidney cells.

J. Fransen, H. Croes, E. Sterchi, 1997, European journal of biochemistry.

Differential regulation of metzincins in experimental chronic renal allograft rejection: potential markers and novel therapeutic targets.

R. Lindberg, C. V. Kooten, A. Kappeler, 2006, Kidney international.

The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin β and ADAM10

A. Chalaris, S. Rose-John, C. Overall, 2012, Cellular and Molecular Life Sciences.

Sucrase-isomaltase and cystic fibrosis

H. J. Sips, H. Hauri, H. Galjaard, 1985, Journal of Inherited Metabolic Disease.

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.

V. Magdolen, E. Sterchi, C. Becker-Pauly, 2007, Journal of Investigative Dermatology.

Differences in the activation mechanism between the alpha and beta subunits of human meprin.

J. Harris, E. Sterchi, W. Stöcker, 2003, Biological chemistry.

Nonpancreatic Hydrolysis of N‐Benzoyl‐L‐tyrosyl‐p‐aminobenzoic Acid (PABA Peptide) in the Rat Small Intestine

M. Lentze, J. Green, E. Sterchi, 1983, Journal of pediatric gastroenterology and nutrition.

N-Benzoyl-l-tyrosyl-p-aminobenzoic acid hydrolase β (human meprinβ)

B. Leuenberger, E. Sterchi, D. Hahn, 1999 .

A novel 2D‐based approach to the discovery of candidate substrates for the metalloendopeptidase meprin

M. Heller, B. Oneda, E. Sterchi, 2008, The FEBS journal.

INTESTINAL ENTEROPEPTIDASE DEFICIENCY ASSOCIATED WITH EXOCRINE PANCREATIC INSUFFICIENCY

M. Hermier, M. Lentze, J. Green, 1982, The Lancet.

Special issue: metzincin metalloproteinases.

E. Sterchi, 2008, Molecular aspects of medicine.

Human N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase (human meprin): genomic structure of the alpha and beta subunits.

A. Metspalu, E. Sterchi, D. Hahn, 2000, The Biochemical journal.

Secretion of human meprin from intestinal epithelial cells depends on differential expression of the alpha and beta subunits.

E. Sterchi, D. Lottaz, D. Hahn, 1999, European journal of biochemistry.

Meprins, membrane-bound and secreted astacin metalloproteinases.

E. Sterchi, W. Stöcker, J. Bond, 2008, Molecular aspects of medicine.

Contribution of villous atrophy to reduced intestinal maltase in infants with malnutrition.

B. Nichols, A. Quaroni, J. K. Fraley, 2000, Journal of pediatric gastroenterology and nutrition.

Expression and intracellular transport of microvillus membrane hydrolases in human intestinal epithelial cells

H. Hauri, J. Fransen, E. Sterchi, 1985, The Journal of cell biology.

Activation of the Epidermal Growth Factor Receptor (EGFR) by a Novel Metalloprotease Pathway*

N. McElvaney, C. Greene, S. O’Neill, 2008, Journal of Biological Chemistry.