Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Angiotensin-converting enzyme 2 ectodomain shedding cleavage-site identification: determinants and constraints.

Biochemistry - 14 Jun 2011

Lai Zon W, Hanchapola Iresha, Steer David L, Smith A Ian

Abstract excerpt

ADAM17, also known as tumor necrosis factor α-converting enzyme, is involved in the ectodomain shedding of many integral membrane proteins. We have previously reported that ADAM17 is able to mediate the cleavage secretion of the ectodomain of human angiotensin-converting enzyme 2 (ACE2), a functional receptor for the severe acute respiratory syndrome coronavirus. In this study, we demonstrate that purified...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to ADAM Proteins
Share to ADAM17 Protein
Share to Angiotensin-Converting Enzyme 2

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Arginine

Share to CHO Cells

Share to Cricetulus

Share to Peptidyl-Dipeptidase A

Share to Serine

Source

Identifiers

PMID: 21563828
DOI: 10.1021/bi200525y

Genes

ADAM17
ACE2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Angiotensin-converting enzyme 2 ectodomain shedding cleavage-site identification: determinants and constraints.PMID 21563828Read ↗

Extracellular Juxtamembrane Segment of ADAM17 Interacts with Membranes and Is Essential for Its Shedding Activity.Semantic proximity Read ↗

Defining the boundaries of the testis angiotensin I-converting enzyme ectodomain.Semantic proximity Read ↗

The shedding protease ADAM17: Physiology and pathophysiologySemantic proximity Read ↗

ADAM17 is the main sheddase for the generation of human triggering receptor expressed in myeloid cells (hTREM2) ectodomain and cleaves TREM2 after histidine 157Semantic proximity Read ↗

Molecular switch in human diseases-disintegrin and metalloproteinases, ADAM17Semantic proximity Read ↗

Enhancing Interleukin-6 and Interleukin-11 receptor cleavage.Semantic proximity Read ↗

Substrate-selective protein ectodomain shedding by ADAM17 and iRhom2 depends on their juxtamembrane and transmembrane domains.Semantic proximity Read ↗

Strategies to Target ADAM17 in Disease: From Its Discovery to the iRhom RevolutionSemantic proximity Read ↗

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

Tumor necrosis factor-alpha converting enzyme.Semantic proximity Read ↗

Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands.Semantic proximity Read ↗

An angiotensin I-converting enzyme mutation (Y465D) causes a dramatic increase in blood ACE via accelerated ACE shedding.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.