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

Multiple Timescale Dynamic Analysis of Functionally-Impairing Mutations in Human Ileal Bile Acid-Binding Protein.

International journal of molecular sciences - 26 Sept 2022

Horváth Gergő, Balterer Bence, Micsonai András, Kardos József, Toke Orsolya

Abstract excerpt

Human ileal bile acid-binding protein (hI-BABP) has a key role in the enterohepatic circulation of bile salts. Its two internal binding sites exhibit positive cooperativity accompanied by a site-selectivity of glycocholate (GCA) and glycochenodeoxycholate (GCDA), the two most abundant bile salts in humans. To improve our understanding of the role of dynamics in ligand binding, we introduced functionally impairing...

Read the complete abstract on PubMed

Topics

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

Share to Bile Acids and Salts
Share to Carrier Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ligands

Share to Membrane Glycoproteins

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 36232642
DOI: 10.3390/ijms231911346
PMCID: PMC9569817

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

Multiple Timescale Dynamic Analysis of Functionally-Impairing Mutations in Human Ileal Bile Acid-Binding Protein.PMID 36232642Read ↗

Towards the elucidation of molecular determinants of cooperativity in the liver bile acid binding protein.Semantic proximity Read ↗

Bile acid interactions with rabbit ileal lipid binding protein and an engineered helixless variant reveal novel ligand binding properties of a versatile beta-clam shell protein scaffold.Semantic proximity Read ↗

Engineering a compact non-native state of intestinal fatty acid-binding protein.Semantic proximity Read ↗

Dynamic coupling of residues within proteins as a mechanistic foundation of many enigmatic pathogenic missense variantsSemantic proximity Read ↗

Mechanisms of intramolecular communication in a hyperthermophilic acylaminoacyl peptidase: a molecular dynamics investigation.Semantic proximity Read ↗

Dynamic coupling of residues within proteins as a mechanistic foundation of many enigmatic pathogenic missense variants.Semantic proximity Read ↗

Pathogenic mechanism of the K141E mutation in HSPB8: Insights from smFRET and simulations.Semantic proximity Read ↗

Molecular differences between human liver fatty acid binding protein and its T94A variant in their unbound and lipid-bound states.Semantic proximity Read ↗

Molecular Dynamics Insights into the Binding Interactions of Semaglutide with Human Serum AlbuminSemantic proximity Read ↗

Structural insight into sodium-dependent bile acid transport by members of the SLC10 familySemantic proximity Read ↗

Binding of Cholesterol to the N-Terminal Domain of the NPC1L1 Transporter: Analysis of the Epimerization-Related Binding Selectivity and Loop Mutations.Semantic proximity Read ↗

HdeB chaperone activity is coupled to its intrinsic dynamic properties.Semantic proximity Read ↗

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