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Meprins, membrane-bound and secreted astacin metalloproteinases

Molecular aspects of medicine, 2008-10, Vol.29 (5), p.309-328

2008

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Human Intestinal Maltase–Glucoamylase: Crystal Structure of the N-Terminal Catalytic Subunit and Basis of Inhibition and Substrate Specificity

Journal of molecular biology, 2008-01, Vol.375 (3), p.782-792

2008

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

Proceedings of the National Academy of Sciences - PNAS, 2012-10, Vol.109 (40), p.16131-16136

2012

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Processing of Procollagen III by Meprins: New Players in Extracellular Matrix Assembly?

Journal of investigative dermatology, 2010-12, Vol.130 (12), p.2727-2735

2010

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

Biochemical journal, 2004-03, Vol.378 (Pt 2), p.383-389

2004

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

The Journal of biological chemistry, 2008-11, Vol.283 (46), p.31736-31744

2008

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Enhanced activity of meprin-α, a pro-migratory and pro-angiogenic protease, in colorectal cancer

PloS one, 2011-11, Vol.6 (11), p.e26450-e26450

2011

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Special issue: Metzincin metalloproteinases

Molecular aspects of medicine, 2008-10, Vol.29 (5), p.255-257

2008

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

Mucosal immunology, 2009-05, Vol.2 (3), p.220-231

2009

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

The Journal of biological chemistry, 2005-12, Vol.280 (52), p.42636-42643

2005

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

Journal of pediatric gastroenterology and nutrition, 2007-07, Vol.45 (1), p.32-43

2007

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

Kidney international, 2006-01, Vol.69 (2), p.358-368

2006

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

FEBS letters, 2007-05, Vol.581 (13), p.2381-2388

2007

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Metalloprotease meprin beta in rat kidney: glomerular localization and differential expression in glomerulonephritis

PloS one, 2008-05, Vol.3 (5), p.e2278-e2278

2008

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Inhibition of recombinant human maltase glucoamylase by salacinol and derivatives

The FEBS journal, 2006-06, Vol.273 (12), p.2673-2683

2006

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

The Journal of biological chemistry, 2012-10, Vol.287 (42), p.35201-35211

2012

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

Biological chemistry, 2003-05, Vol.384 (5), p.825-831

2003

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The astacin family of metalloendopeptidases

The Journal of biological chemistry, 1991-11, Vol.266 (32), p.21381-21385

1991

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

Cancer research (Chicago, Ill.), 1999-03, Vol.59 (5), p.1127-1133

1999

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The Metalloprotease Meprinβ Processes E-Cadherin and Weakens Intercellular Adhesion

PloS one, 2008-05, Vol.3 (5), p.e2153

2008

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Activation of human meprin-alpha in a cell culture model of colorectal cancer is triggered by the plasminogen-activating system

The Journal of biological chemistry, 2002-10, Vol.277 (43), p.40650-40658

2002

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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

Journal of investigative dermatology, 2007-05, Vol.127 (5), p.1115-1125

2007

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Luminal Starch Substrate Brake on Maltase-Glucoamylase Activity Is Located within the Glucoamylase Subunit

The Journal of nutrition, 2008-04, Vol.138 (4), p.685-692

2008

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

Biological chemistry, 2016-05, Vol.397 (9), p.857

2016

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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

Biochemical journal, 2003-02, Vol.369 (Pt 3), p.659-665

2003

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Meprins, membrane-bound and secreted astacin metalloproteinases

Human Intestinal Maltase–Glucoamylase: Crystal Structure of the N-Terminal Catalytic Subunit and Basis of Inhibition and Substrate Specificity

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

Processing of Procollagen III by Meprins: New Players in Extracellular Matrix Assembly?

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

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

Enhanced activity of meprin-α, a pro-migratory and pro-angiogenic protease, in colorectal cancer

Special issue: Metzincin metalloproteinases

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

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

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

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

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

Metalloprotease meprin beta in rat kidney: glomerular localization and differential expression in glomerulonephritis

Inhibition of recombinant human maltase glucoamylase by salacinol and derivatives

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

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

The astacin family of metalloendopeptidases

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

The Metalloprotease Meprinβ Processes E-Cadherin and Weakens Intercellular Adhesion

Activation of human meprin-alpha in a cell culture model of colorectal cancer is triggered by the plasminogen-activating system

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

Luminal Starch Substrate Brake on Maltase-Glucoamylase Activity Is Located within the Glucoamylase Subunit

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

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

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