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

The effects of amino-acid mutations on specific interactions between urokinase-type plasminogen activator and its receptor: Ab initio molecular orbital calculations.

Journal of molecular graphics & modelling - 1 Aug 2011

Tsuji Shingo, Kasumi Tomoyo, Nagase Keisuke, Yoshikawa Eri, Kobayashi Hiroshi, Kurita Noriyuki

Abstract excerpt

During cancer invasion, the binding of urokinase-type plasminogen activator (uPA) to its receptor (uPAR) on the surface of a cancer cell is considered a trigger for invasion. Here, we present a stable structure of the solvated complex formed between uPA and uPAR (uPA-uPAR) and investigate the specific interactions between uPA and uPAR by ab initio fragment molecular orbital (FMO) calculations. The result...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Neoplasms

Share to Protein Interaction Domains and Motifs

Share to Receptors, Urokinase Plasminogen Activator

Share to Static Electricity

Share to Urokinase-Type Plasminogen Activator

Source

Identifiers

PMID: 21605990
DOI: 10.1016/j.jmgm.2011.04.003

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

The effects of amino-acid mutations on specific interactions between urokinase-type plasminogen activator and its receptor: Ab initio molecular orbital calculations.PMID 21605990Read ↗

Ab initio molecular simulations for proposing novel peptide inhibitors blocking the ligand-binding pocket of urokinase receptor.Semantic proximity Read ↗

Fragment Molecular Orbital Based Interaction Analyses on Complexes Between RBD Variants and ACE2Semantic proximity Read ↗

A novel approach to study multi-domain motions in JAK1's activation mechanism based on energy landscape.Semantic proximity Read ↗

Structural basis for recognition of urokinase-type plasminogen activator by plasminogen activator inhibitor-1.Semantic proximity Read ↗

Elucidating Electronic Structure Variations in Nucleic Acid-Protein Complexes Involved in Transcription Regulation Using a Tight-Binding ApproachSemantic proximity Read ↗

Interaction Analysis on the SARS-CoV-2 Spike Protein Receptor Binding Domain Using Visualization of the Interfacial Electrostatic ComplementaritySemantic proximity Read ↗

Structure of Human Urokinase Plasminogen Activator in Complex with Its ReceptorSemantic proximity Read ↗

Structural Basis of Interaction between Urokinase-type Plasminogen Activator and its ReceptorSemantic proximity Read ↗

Reliable Prediction of the Protein-Ligand Binding Affinity Using a Charge Penetration Corrected AMOEBA Force Field: A Case Study of Drug Resistance Mutations in Abl Kinase.Semantic proximity Read ↗

Water-mediated network in the resistance mechanism of fosfomycin.Semantic proximity Read ↗

Estimation of the Binding Free Energy of AC1NX476 to HIV-1 Protease Wild Type and Mutations Using Free Energy Perturbation Method.Semantic proximity Read ↗

Role of the key mutation in the selective binding of avian and human influenza hemagglutinin to sialosides revealed by quantum-mechanical calculations.Semantic proximity Read ↗

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