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

Mapping of the active site of glutamate carboxypeptidase II by site‐directed mutagenesis

21 Aug 2007

Abstract excerpt

Human glutamate carboxypeptidase II [GCPII (EC 3.4.17.21)] is recognized as a promising pharmacological target for the treatment and imaging of various pathologies, including neurological disorders and prostate cancer. Recently reported crystal structures of GCPII provide structural insight into the organization of the substrate binding cavity and highlight residues implicated in substrate/inhibitor binding in...

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 Peptidase Inhibition and Analysis
Share to Receptor Mechanisms and Signaling

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 17714508
DOI: 10.1111/j.1742-4658.2007.06021.x

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

Mapping of the active site of glutamate carboxypeptidase II by site‐directed mutagenesisPMID 17714508Read ↗

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 ↗

In silico approaches to identify the potential inhibitors of glutamate carboxypeptidase II (GCPII) for neuroprotection.Semantic proximity Read ↗

Structural and biochemical characterization of the folyl‐poly‐γ‐<scp>l</scp>‐glutamate hydrolyzing activity of human glutamate carboxypeptidase <scp>II</scp>Semantic proximity Read ↗

Substrate specificity, inhibition and enzymological analysis of recombinant human glutamate carboxypeptidase IISemantic proximity Read ↗

Paradoxical role of C1561T glutamate carboxypeptidase II (GCPII) genetic polymorphism in altering disease susceptibility.Semantic proximity Read ↗

GCPII Variants, Paralogs and OrthologsSemantic proximity Read ↗

Clinical utility of genetic variants of glutamate carboxypeptidase II in predicting breast cancer and prostate cancer risk.Semantic proximity Read ↗

A novel allosteric site employs a conserved inhibition mechanism in human kidney-type glutaminase.Semantic proximity Read ↗

Selective reduction in glutaminase activity of l‑Asparaginase by asparagine 248 to serine mutation: A combined computational and experimental effort in blood cancer treatment.Semantic proximity Read ↗

Structural basis for the active site inhibition mechanism of human kidney-type glutaminase (KGA).Semantic proximity Read ↗

Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation.Semantic proximity Read ↗

β-Glucocerebrosidase Modulators Promote Dimerization of β-Glucocerebrosidase and Reveal an Allosteric Binding Site.Semantic proximity Read ↗

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