A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions

Extracellular Juxtamembrane Segment of ADAM17 Interacts with Membranes and Is Essential for Its Shedding Activity

(2015) Stefan Düsterhöft et al.   BIOCHEMISTRY

Loss of ADAM17 is associated with severe multiorgan dysfunction

(2015) Robert H.J. Bandsma et al.   HUMAN PATHOLOGY

Notch1 Autoactivation via Transcriptional Regulation of Furin, Which Sustains Notch1 Signaling by Processing Notch1-Activating Proteases ADAM10 and Membrane Type 1 Matrix Metalloproteinase

(2015) Hong Qiu et al.   MOLECULAR AND CELLULAR BIOLOGY

A systematic study of modulation of ADAM-mediated ectodomain shedding by site-specific O-glycosylation

(2015) Christoffer K. Goth et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

iRhoms 1 and 2 are essential upstream regulators of ADAM17-dependent EGFR signaling

(2015) Xue Li et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

The alpha secretase ADAM10: A metalloprotease with multiple functions in the brain

(2015) Paul Saftig et al.   PROGRESS IN NEUROBIOLOGY

Deletions in the cytoplasmic domain of iRhom1 and iRhom2 promote shedding of the TNF receptor by the protease ADAM17

(2015) Sathish K. Maney et al.   Science Signaling

Cytokine secretion and NK cell activity in human ADAM17 deficiency

(2015) Pinchas Tsukerman et al.   Oncotarget

Deletions in the cytoplasmic domain of iRhom1 and iRhom2 promote shedding of the TNF receptor by the protease ADAM17

(2015) Sathish K. Maney et al.   Science Signaling

ADAM17 at the interface between inflammation and autoimmunity

(2014) Sabrina Lisi et al.   IMMUNOLOGY LETTERS

ADAM Metallopeptidase Domain 33 (ADAM33): A Promising Target for Asthma

(2014) Priya Tripathi et al.   MEDIATORS OF INFLAMMATION

Regulated Proteolysis of NOTCH2 and NOTCH3 Receptors by ADAM10 and Presenilins

(2014) A. J. Groot et al.   MOLECULAR AND CELLULAR BIOLOGY

Mammalian iRhoms have distinct physiological functions including an essential role in TACE regulation

(2013) Yonka Christova et al.   EMBO REPORTS

iRhom2 controls the substrate selectivity of stimulated ADAM17-dependent ectodomain shedding

(2013) T. Maretzky et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Ectodomain shedding and ADAMs in development

(2012) S. Weber et al.   DEVELOPMENT

Role of ADAM-15 in wound healing and melanoma development

(2012) Alexander Schönefuß et al.   EXPERIMENTAL DERMATOLOGY

Phylogenetic and molecular evolution of the ADAM (A Disintegrin And Metalloprotease) gene family from Xenopus tropicalis, to Mus musculus, Rattus norvegicus, and Homo sapiens

(2012) Jiaoyue Long et al.   GENE

Discovery of Novel Inhibitors of a Disintegrin and Metalloprotease 17 (ADAM17) Using Glycosylated and Non-glycosylated Substrates

(2012) Dmitriy Minond et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Epidermal ADAM17 maintains the skin barrier by regulating EGFR ligand–dependent terminal keratinocyte differentiation

(2012) Claus-Werner Franzke et al.   JOURNAL OF EXPERIMENTAL MEDICINE

Stromal Fibroblast–Specific Expression of ADAM-9 Modulates Proliferation and Apoptosis in Melanoma Cells In Vitro and In Vivo

(2012) Anna N. Abety et al.   JOURNAL OF INVESTIGATIVE DERMATOLOGY

Amyloid Precursor Protein Processing and Alzheimer's Disease

(2011) Richard J. O'Brien et al.   Annual Review of Neuroscience

Snake venom metalloproteinases: Structure, function and relevance to the mammalian ADAM/ADAMTS family proteins

(2011) Soichi Takeda et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

Deletion of Adam10 in endothelial cells leads to defects in organ-specific vascular structures

(2011) K. Glomski et al.   BLOOD

The disintegrin/metalloproteinase Adam10 is essential for epidermal integrity and Notch-mediated signaling

(2011) S. Weber et al.   DEVELOPMENT

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

(2011) Marcia L. Moss et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Regulated intramembrane proteolysis - lessons from amyloid precursor protein processing

(2011) Stefan F. Lichtenthaler et al.   JOURNAL OF NEUROCHEMISTRY

Inflammatory Skin and Bowel Disease Linked toADAM17Deletion

(2011) Diana C. Blaydon et al.   NEW ENGLAND JOURNAL OF MEDICINE

The tissue inhibitors of metalloproteinases (TIMPs): An ancient family with structural and functional diversity

(2010) Keith Brew et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH

Pathological Neovascularization Is Reduced by Inactivation of ADAM17 in Endothelial Cells but Not in Pericytes

(2010) Gisela Weskamp et al.   CIRCULATION RESEARCH

The “A Disintegrin And Metalloproteases” ADAM10 and ADAM17: Novel drug targets with therapeutic potential?

(2010) Paul Saftig et al.   EUROPEAN JOURNAL OF CELL BIOLOGY

Accelerated Wound Repair in ADAM-9 Knockout Animals

(2010) Cornelia Mauch et al.   JOURNAL OF INVESTIGATIVE DERMATOLOGY

The Disintegrin/Metalloproteinase ADAM10 Is Essential for the Establishment of the Brain Cortex

(2010) E. Jorissen et al.   JOURNAL OF NEUROSCIENCE

ADAM-15 Disintegrin-Like Domain Structure and Function

(2010) Dong Lu et al.   Toxins

Loss of the Metalloprotease ADAM9 Leads to Cone-Rod Dystrophy in Humans and Retinal Degeneration in Mice

(2009) David A. Parry et al.   AMERICAN JOURNAL OF HUMAN GENETICS

Disruption of ADAM3 Impairs the Migration of Sperm into Oviduct in Mouse1

(2009) Ryo Yamaguchi et al.   BIOLOGY OF REPRODUCTION

Structural Characterization of the Ectodomain of a Disintegrin and Metalloproteinase-22 (ADAM22), a Neural Adhesion Receptor Instead of Metalloproteinase

(2009) Heli Liu et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

ADAM10, the Rate-limiting Protease of Regulated Intramembrane Proteolysis of Notch and Other Proteins, Is Processed by ADAMS-9, ADAMS-15, and the γ-Secretase

(2009) Thomas Tousseyn et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Metalloprotease ADAM10 Is Required for Notch1 Site 2 Cleavage

(2009) Geert van Tetering et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

EGFR ligands and their signaling scissors, ADAMs, as new molecular targets for anticancer treatments

(2009) Hiromi Kataoka   JOURNAL OF DERMATOLOGICAL SCIENCE

Structures of two elapid snake venom metalloproteases with distinct activities highlight the disulfide patterns in the D domain of ADAMalysin family proteins

(2009) Hong-Hsiang Guan et al.   JOURNAL OF STRUCTURAL BIOLOGY

ADAM9 Is Involved in Pathological Retinal Neovascularization

(2009) V. Guaiquil et al.   MOLECULAR AND CELLULAR BIOLOGY

Nuclear signalling by tumour-associated antigen EpCAM

(2009) Dorothea Maetzel et al.   NATURE CELL BIOLOGY

The ADAM metalloproteinases

(2008) D EDWARDS et al.   MOLECULAR ASPECTS OF MEDICINE

Three-dimensional domain architecture of the ADAM family proteinases

(2008) Soichi Takeda   SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY

The “A Disintegrin And Metalloprotease” (ADAM) family of sheddases: Physiological and cellular functions

(2008) Karina Reiss et al.   SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY