Ectodomain shedding of the Notch ligand Jagged1 is mediated by ADAM17, but is not a lipid-raft-associated event

Notch signaling: Emerging molecular targets for cancer therapy

(2010) Ling Yin et al.   BIOCHEMICAL PHARMACOLOGY

Targeting ADAM10 to lipid rafts in neuroblastoma SH-SY5Y cells impairs amyloidogenic processing of the amyloid precursor protein

(2009) Benjamin Harris et al.   BRAIN RESEARCH

Role of ADAMs in the Ectodomain Shedding and Conformational Conversion of the Prion Protein

(2009) David R. Taylor 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

A Notch updated

(2009) An-Chi Tien et al.   JOURNAL OF CELL BIOLOGY

A disintegrin and metalloproteinase (ADAM)-mediated ectodomain shedding of ADAM10

(2009) Edward Parkin et al.   JOURNAL OF NEUROCHEMISTRY

Selective Use of ADAM10 and ADAM17 in Activation of Notch1 Signaling

(2009) E. C. Bozkulak et al.   MOLECULAR AND CELLULAR BIOLOGY

Soluble Forms of the Notch Ligands Delta1 and Jagged1 Promote in Vivo Tumorigenicity in NIH3T3 Fibroblasts with Distinct Phenotypes

(2008) Sumithra Urs et al.   AMERICAN JOURNAL OF PATHOLOGY

Lipid rafts, cholesterol, and the brain

(2008) Zeljka Korade et al.   NEUROPHARMACOLOGY

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

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