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

Insights into the Allosteric Effect of SENP1 Q597A Mutation on the Hydrolytic Reaction of SUMO1 via an Integrated Computational Study.

Molecules (Basel, Switzerland) - 28 Jun 2022

Ji Mingfei, Chai Zongtao, Chen Jie, Li Gang, Li Qiang, Li Miao, Ding Yelei, Lu Shaoyong, Ju Guanqun, Hou Jianquan

Abstract excerpt

Small ubiquitin-related modifier (SUMO)-specific protease 1 (SENP1) is a cysteine protease that catalyzes the cleavage of the C-terminus of SUMO1 for the processing of SUMO precursors and deSUMOylation of target proteins. SENP1 is considered to be a promising target for the treatment of hepatocellular carcinoma (HCC) and prostate cancer. SENP1 Gln597 is located at the unstructured loop connecting the helices α4...

Read the complete abstract on PubMed

Topics

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

Share to Carcinoma, Hepatocellular
Share to Cysteine Endopeptidases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Liver Neoplasms

Share to Mutation

Share to Peptide Hydrolases

Share to SUMO-1 Protein

Source

Open in PubMed Open full text

Identifiers

PMID: 35807394
DOI: 10.3390/molecules27134149
PMCID: PMC9268427

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Insights into the Allosteric Effect of SENP1 Q597A Mutation on the Hydrolytic Reaction of SUMO1 via an Integrated Computational Study.PMID 35807394Read ↗

Systematic Analysis of the Genetic Variability That Impacts SUMO Conjugation and Their Involvement in Human Diseases.Semantic proximity Read ↗

Engineering pre-SUMO4 as efficient substrate of SENP2.Semantic proximity Read ↗

Molecular dynamics investigation of single nucleotide polymorphism-driven variations in GSTP1 phosphorylation and substrate interaction.Semantic proximity Read ↗

Mapping increased flexibility and conformational divergence via N-terminal helix-to-coil transition in USP12 mutant Y49N: a comprehensive in-detail normal mode simulation study.Semantic proximity Read ↗

Computational studies on the functional and structural impact of pathogenic mutations in enzymes.Semantic proximity Read ↗

Structure of the human SENP7 catalytic domain and poly-SUMO deconjugation activities for SENP6 and SENP7.Semantic proximity Read ↗

Structural and Dynamic Characterizations Highlight the Deleterious Role of SULT1A1 R213H Polymorphism in Substrate Binding.Semantic proximity Read ↗

Impacts of Cancer-associated Mutations on the Structure-Activity Relationship of BAP1.Semantic proximity Read ↗

Integrative computational simulations and functional assays decode allosteric dysregulation in a pathogenic SIRT6 variant.Semantic proximity Read ↗

Molecular Dynamics Simulations and Dynamic Network Analysis Reveal the Allosteric Unbinding of Monobody to H-Ras Triggered by R135K Mutation.Semantic proximity Read ↗

Domain alternation and active site remodeling are conserved structural features of ubiquitin E1.Semantic proximity Read ↗

The intrinsically disordered N-terminus of SUMO1 is an intramolecular inhibitor of SUMO1 interactionsSemantic proximity Read ↗

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