M. Moss

发表

Fluorescence displacement method for the determination of receptor-ligand binding constants.

J. Kofron, P. Kuzmič, D. Rich, 1992, Analytical biochemistry.

Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α

M. Lambert, W. Rocque, S. Jin, 1997, Nature.

Metalloprotease-Disintegrin MDC9: Intracellular Maturation and Catalytic Activity*

G. Weskamp, C. Blobel, H. Erdjument-Bromage, 1999, The Journal of Biological Chemistry.

Identification of candidate substrates for ectodomain shedding by the metalloprotease-disintegrin ADAM8

Z. Guan, D. Wildeboer, S. Lichtenthaler, 2006, Biological chemistry.

Mechanism of time-dependent inhibition of 5 alpha-reductases by delta 1-4-azasteroids: toward perfection of rates of time-dependent inhibition by using ligand-binding energies.

S. Frye, R. Mook, M. Moss, 1995, Biochemistry.

Inhibition of human steroid 5alpha reductases type I and II by 6-aza-steroids: structural determinants of one-step vs two-step mechanism.

J. D. Stuart, S. Frye, P. Kuzmič, 1996 .

Inhibition of human steroid 5alpha reductases type I and II by 6-aza-steroids: structural determinants of one-step vs two-step mechanism.

J. D. Stuart, S. Frye, P. Kuzmič, 1996, Biochemistry.

The isolated N-terminal domains of TIMP-1 and TIMP-3 are insufficient for ADAM10 inhibition.

G. Murphy, S. Atkinson, M. Moss, 2008, The Biochemical journal.

Targeting autocrine HB-EGF signaling with specific ADAM12 inhibition using recombinant ADAM12 prodomain

Miles A. Miller, Aaron S. Meyer, D. Lauffenburger, 2015, Scientific Reports.

Fluorescent substrates useful as high-throughput screening tools for ADAM9.

P. Dempsey, Jason Williams, M. Moss, 2010, Combinatorial chemistry & high throughput screening.

Structural features and biochemical properties of TNF-α converting enzyme (TACE)

W. Rocque, S. Jin, M. Milla, 1997, Journal of Neuroimmunology.

Fluorescent substrates for the proteinases ADAM17, ADAM10, ADAM8, and ADAM12 useful for high-throughput inhibitor screening.

M. Moss, F. Rasmussen, 2007, Analytical biochemistry.

Ectodomain Shedding of the Neural Recognition Molecule CHL1 by the Metalloprotease-disintegrin ADAM8 Promotes Neurite Outgrowth and Suppresses Neuronal Cell Death*

M. Schachner, D. Wildeboer, Melanie Richter, 2004, Journal of Biological Chemistry.

Activation of lysine 2,3-aminomutase by S-adenosylmethionine.

P. Frey, M. Moss, 1990, The Journal of biological chemistry.

ADAM8 as a drug target in Pancreatic Cancer

Miles A. Miller, D. Lauffenburger, Randal R Ketchem, 2015, Nature Communications.

The role of S-adenosylmethionine in the lysine 2,3-aminomutase reaction.

P. Frey, M. Moss, Perry A. Frey, 1987, The Journal of biological chemistry.

Use of a multiple-enzyme/multiple-reagent assay system to quantify activity levels in samples containing mixtures of matrix metalloproteinases.

C. López-Otín, M. Vitek, G. Murphy, 2004, Biochemistry.

Cleavage of cell surface proteins by thrombin.

D. Cunningham, M. Moss, 1981, Journal of supramolecular structure and cellular biochemistry.

The tumor necrosis factor-alpha converting enzyme (TACE): a unique metalloproteinase with highly defined substrate selectivity.

M. Milla, G. Waitt, K. Blackburn, 2002, Biochemistry.

ADAM10 as a therapeutic target for cancer and inflammation.

P. Dempsey, H. Crawford, L. Adam, 2009, Current pharmaceutical design.

Lysine 2,3-aminomutase. Support for a mechanism of hydrogen transfer involving S-adenosylmethionine.

P. Frey, M. Moss, J. Baraniak, 1989, The Journal of biological chemistry.

Remarks on an Enzymatic Amplification System for Use in Point of CareDiagnostics

M. Moss, 2015 .

Inhibition of Tumor Necrosis Factor-( TNF-) Production and Arthritis in the Rat by GW 3333 , a Dual Inhibitor of TNF-- Converting Enzyme and Matrix Metalloproteinases

T. Brodie, M. Milla, T. Tippin, 2001 .

Screening And Design Of Tumor Necrosis Factor-: Converting Enzyme Inhibitors

M. Lambert, T. Tippin, R. Wiethe, 2000 .

A high throughput assay for the TNF converting enzyme

M. A. Leesnitzer, J. Becherer, M. Moss, 2000 .

TNFα converting enzyme

M. Lambert, S. Frye, M. Vitek, 1999 .

Multiple metalloproteinases process protransforming growth factor-alpha (proTGF-alpha).

C. Hinkle, M. Milla, M. Moss, 2003, Biochemistry.

N-hydroxyformamide peptidomimetics as TACE/matrix metalloprotease inhibitors: oral activity via P1' isobutyl substitution.

J. Warner, M. Lambert, T. Tippin, 2001, Bioorganic & medicinal chemistry letters.

17 beta-(N-tert-butylcarbamoyl)-4-aza-5 alpha-androstan-1-en-3-one is an active site-directed slow time-dependent inhibitor of human steroid 5 alpha-reductase 1.

J. D. Stuart, T. Kost, R. Mook, 1994, Biochemistry.

Nuclear processing of the 3'-terminal nucleotides of pre-U1 RNA in Xenopus laevis oocytes

H. Yang, E. Lund, J. Dahlberg, 1992, Molecular and cellular biology.

Structural features and biochemical properties of TNF-alpha converting enzyme (TACE).

W. Rocque, M. Milla, F. Schoenen, 1997, Journal of neuroimmunology.

Differentiation of secreted and membrane-type matrix metalloproteinase activities based on substitutions and interruptions of triple-helical sequences.

K. Brew, C. Overall, G. Fields, 2007, Biochemistry.

Design of Selective and Soluble Inhibitors of Tumor Necrosis Factor-α Converting Enzyme (TACE)+

M. Lambert, A. Musso, M. A. Leesnitzer, 2001 .

The ADAM10 Prodomain Is a Specific Inhibitor of ADAM10 Proteolytic Activity and Inhibits Cellular Shedding Events*

P. Dempsey, D. Wildeboer, P. Zhou, 2007, Journal of Biological Chemistry.

6-Azasteroids: Potent Dual Inhibitors of Human Type 1 and 2 Steroid 5. alpha.-Reductase.

M. K. James, S. Frye, T. Tippin, 1994 .

Recent Advances in ADAM17 Research: A Promising Target for Cancer and Inflammation

M. Moss, Dmitry Minond, 2017, Mediators of inflammation.

A Disintegrin and Metalloproteinase-10 (ADAM-10) Mediates DN30 Antibody-induced Shedding of the Met Surface Receptor*

A. Krüger, P. Comoglio, C. Boccaccio, 2010, The Journal of Biological Chemistry.

Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α

M. Lambert, W. Rocque, S. Jin, 1997, Nature.

Endotoxin induces rapid metalloproteinase‐mediated shedding followed by up‐regulation of the monocyte hemoglobin scavenger receptor CD163

P. Wallace, A. Givan, P. Guyre, 2002, Journal of leukocyte biology.

Tumor Necrosis Factor-α (TNF-α) Regulates Shedding of TNF-α Receptor 1 by the Metalloprotease-Disintegrin ADAM8: Evidence for a Protease-Regulated Feedback Loop in Neuroprotection

H. Jockusch, D. Wildeboer, Andrea Rittger, 2010, The Journal of Neuroscience.

ADAM 8 as a drug target in pancreatic cancer

Miles A. Miller, D. Lauffenburger, Randal R Ketchem, 2015 .

Inhibition of Tumor Necrosis Factor-α (TNF-α) Production and Arthritis in the Rat by GW3333, a Dual Inhibitor of TNF-α-Converting Enzyme and Matrix Metalloproteinases

Michael H. Rabinowitz, T. Brodie, M. Milla, 2001 .

Metastasis-associated C4.4A, a GPI-anchored protein cleaved by ADAM10 and ADAM17

J. Arribas, F. Canals, N. Colomé, 2008, Biological chemistry.

Substrate Specificity of Human Collagenase 3 Assessed Using a Phage-displayed Peptide Library*

M. Weiner, M. Lambert, G. Pahel, 2000, The Journal of Biological Chemistry.

Proteolytic Activity Matrix Analysis (PrAMA) for simultaneous determination of multiple protease activities.

Douglas A Lauffenburger, Linda G Griffith, Andreas Herrlich, 2011, Integrative biology : quantitative biosciences from nano to macro.

Therapeutic benefits from targeting of ADAM family members.

J. Bartsch, M. Moss, 2004, Biochemistry.

Photoaffinity labeling of specific alpha-thrombin binding sites on Chinese hamster lung cells.

H. Wiley, J. Fenton, D. Cunningham, 1983, The Journal of biological chemistry.

EphrinA/EphA‐induced ectodomain shedding of neural cell adhesion molecule regulates growth cone repulsion through ADAM10 metalloprotease

P. Maness, M. Moss, L. H. Brennaman, 2014, Journal of neurochemistry.

CD30 on extracellular vesicles from malignant Hodgkin cells supports damaging of CD30 ligand-expressing bystander cells with Brentuximab-Vedotin, in vitro

M. Hallek, M. von Bergwelt-Baildon, A. Trad, 2016, Oncotarget.

Drug Insight: tumor necrosis factor-converting enzyme as a pharmaceutical target for rheumatoid arthritis

Raphael Nudelman, Marcia L Moss, Liora Sklair-Tavron, 2008, Nature Clinical Practice Rheumatology.

The Knockout Punch for HER2 Positive Breast Cancer: Addition of an ADAM10 Inhibitor to the Combination Therapy of Trastuzamab and Lapatinib

M. Moss, 2016 .

ADAM9 Inhibition Increases Membrane Activity of ADAM10 and Controls α-Secretase Processing of Amyloid Precursor Protein*

Miles A. Miller, D. Lauffenburger, B. de Strooper, 2011, The Journal of Biological Chemistry.

Fluorescent substrates for ADAM15 useful for assaying and high throughput screening.

Miles A. Miller, N. Vujanović, T. Yoneyama, 2016, Analytical biochemistry.

Species Specificity of ADAM10 and ADAM17 Proteins in Interleukin-6 (IL-6) Trans-signaling and Novel Role of ADAM10 in Inducible IL-6 Receptor Shedding*

J. Scheller, A. Chalaris, S. Rose-John, 2011, The Journal of Biological Chemistry.

The Low Affinity IgE Receptor (CD23) Is Cleaved by the Metalloproteinase ADAM10*

P. Lipsky, Z. Werb, G. A. Lemieux, 2007, Journal of Biological Chemistry.

Specific Sequence Elements Are Required for the Expression of Functional Tumor Necrosis Factor-α-converting Enzyme (TACE)*

M. Lambert, M. Milla, W. C. Clay, 1999, The Journal of Biological Chemistry.

The Role of S‐Adenosylmethionine as a Poor Man's Adenosylcobalamin in the Reaction of Lysine 2,3‐Aminomutase

G. H. Reed, Christopher H. Chang, P. Frey, 2007 .

Development of flow cytometry assays for measuring cell-membrane enzyme activity on individual cells

Michelle A. Garlin, Miles A. Miller, M. Gorry, 2020, Journal of Cancer.

ADAM10 Sheddase Activity is a Potential Lung-Cancer Biomarker

Miles A. Miller, D. Lauffenburger, L. Griffith, 2018, Journal of Cancer.

Modification of proteolytic activity matrix analysis (PrAMA) to measure ADAM10 and ADAM17 sheddase activities in cell and tissue lysates

Miles A. Miller, D. Lauffenburger, L. Griffith, 2017, Journal of Cancer.

Shedding of membrane proteins by ADAM family proteases.

M. Lambert, M. Moss, 2002, Essays in biochemistry.

Multiple Metalloproteinases Process Protransforming Growth Factor-α (ProTGF-α)†

C. Hinkle, M. Milla, M. Moss, 2003 .

ADAM10 as a target for anti-cancer therapy.

P. Dempsey, Wenbo Yan, A. Stoeck, 2008, Current pharmaceutical biotechnology.

An improved fluorescent substrate for assaying soluble and membrane-associated ADAM family member activities.

H. Hansen, N. Vujanović, T. Yoneyama, 2016, Analytical biochemistry.

Substrate specificity and novel selective inhibitors of TNF-alpha converting enzyme (TACE) from two-dimensional substrate mapping.

M. Lambert, D. Kassel, R. Wiethe, 2005, Combinatorial chemistry & high throughput screening.

Potential of fluorescent metalloproteinase substrates for cancer detection.

D. Zurakowski, M. Moses, S. Pories, 2011, Clinical biochemistry.

Inhibition of tumor necrosis factor-alpha (TNF-alpha) production and arthritis in the rat by GW3333, a dual inhibitor of TNF-alpha-converting enzyme and matrix metalloproteinases.

T. Brodie, M. Milla, T. Tippin, 2001, The Journal of pharmacology and experimental therapeutics.

TACE and other ADAM proteases as targets for drug discovery.

M. Lambert, J. White, M L. Moss, 2001, Drug discovery today.

A colorimetric-based amplification system for proteinases including MMP2 and ADAM8.

S. Rakow, G. Koller, J. Bartsch, 2015, Analytical biochemistry.