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

Phosphinic Peptides as Tool Compounds for the Study of Pharmacologically Relevant Zn-Metalloproteases

28 Nov 2022

Abstract excerpt

Phosphinic peptides constitute an important class of bioactive compounds that have found a wide range of applications in the field of biology and pharmacology of Zn-metalloproteases, the largest family of proteases in humans. They are designed to mimic the structure of natural substrates during their proteolysis, thus acting as mechanism-based, transition state analogue inhibitors. A combination of electrostatic...

Read the complete abstract on PubMed

Topics

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

Share to Chemical Synthesis and Analysis
Share to Oral and gingival health research
Share to Peptidase Inhibition and Analysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 36524013
DOI: 10.1021/acsptsci.2c00183

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Phosphinic Peptides as Tool Compounds for the Study of Pharmacologically Relevant Zn-MetalloproteasesPMID 36524013Read ↗

Therapeutic Peptides Targeting PPI in Clinical Development: Overview, Mechanism of Action and PerspectivesSemantic proximity Read ↗

Protease propeptide structures, mechanisms of activation, and functions.Semantic proximity Read ↗

Glutamate Carboxypeptidase II: An Overview of Structural Studies and Their Importance for Structure-Based Drug Design and Deciphering the Reaction Mechanism of the EnzymeSemantic proximity Read ↗

Peptide Deformylase: A New Target in Antibacterial, Antimalarial and Anticancer Drug DiscoverySemantic proximity Read ↗

Tailoring Peptidomimetics for Targeting Protein–Protein InteractionsSemantic proximity Read ↗

Protease inhibitors: A panacea?Semantic proximity Read ↗

Mutation in the substrate-binding site of aminopeptidase B confers new enzymatic properties.Semantic proximity Read ↗

The neprilysin (NEP) family of zinc metalloendopeptidases: Genomics and functionSemantic proximity Read ↗

Structure of human cytosolic X-prolyl aminopeptidase: a double Mn(II)-dependent dimeric enzyme with a novel three-domain subunit.Semantic proximity Read ↗

Structure-function analyses of human kallikrein-related peptidase 2 establish the 99-loop as master regulator of activity.Semantic proximity Read ↗

Mutation in the Pro-Peptide Region of a Cysteine Protease Leads to Altered Activity and Specificity-A Structural and Biochemical Approach.Semantic proximity Read ↗

Dynamically chiral phosphonic acid-type metallo-β-lactamase inhibitorsSemantic proximity Read ↗

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