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

Network analysis of hydroxymethylbilane synthase dynamics.

Journal of molecular graphics & modelling - 1 Sept 2020

Chakrabarty Broto, Das Dibyajyoti, Bung Navneet, Roy Arijit, Bulusu Gopalakrishnan

Abstract excerpt

Hydroxymethylbilane synthase (HMBS) is one of the key enzymes of the heme biosynthetic pathway that catalyzes porphobilinogen to form the linear tetrapyrrole 1-hydroxymethylbilane through four intermediate steps. Mutations in the human HMBS (hHMBS) can lead to acute intermittent porphyria (AIP), a lethal metabolic disorder. The molecular basis of importance of the amino acid residues at the catalytic site of...

Read the complete abstract on PubMed

Topics

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

Share to Hydroxymethylbilane Synthase
Share to Molecular Dynamics Simulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Porphyria, Acute Intermittent

Share to Pyrroles

Source

Identifiers

PMID: 32619952
DOI: 10.1016/j.jmgm.2020.107641

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Network analysis of hydroxymethylbilane synthase dynamics.PMID 32619952Read ↗

Structural insights into E. coli porphobilinogen deaminase during synthesis and exit of 1-hydroxymethylbilane.Semantic proximity Read ↗

Systematically testing human HMBS missense variants to reveal mechanism and pathogenic variationSemantic proximity Read ↗

Synergistic Allosteric Mechanism of Fructose-1,6-bisphosphate and Serine for Pyruvate Kinase M2 via Dynamics Fluctuation Network Analysis.Semantic proximity Read ↗

One ring closer to a closure: the crystal structure of the ES3 hydroxymethylbilane synthase intermediate.Semantic proximity Read ↗

Two Novel Hydroxymethylbilane Synthase Splicing Mutations Predispose to Acute Intermittent Porphyria.Semantic proximity Read ↗

Network analysis to uncover the structural communication in GPCRs.Semantic proximity Read ↗

Conformational stability and activity analysis of two hydroxymethylbilane synthase mutants, K132N and V215E, with different phenotypic association with acute intermittent porphyria.Semantic proximity Read ↗

Understanding the Role of R266K Mutation in Cystathionine β-Synthase (CBS) Enzyme: An in Silico StudySemantic proximity Read ↗

HMBS gene mutations and hydroxymethylbilane synthase activity in acute intermittent porphyria: A systematic review.Semantic proximity Read ↗

Simulations of Pathogenic E1α Variants: Allostery and Impact on Pyruvate Dehydrogenase Complex-E1 Structure and Function.Semantic proximity Read ↗

Structural insight into acute intermittent porphyria.Semantic proximity Read ↗

Unveiling local and global conformational changes and allosteric communications in SOD1 systems using molecular dynamics simulation and network analyses.Semantic proximity Read ↗

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