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

Thermodynamic coupling of the tandem RRM domains of hnRNP A1 underlie its pleiotropic RNA binding functions.

Science advances - 12 Jul 2024

Levengood Jeffrey D, Potoyan Davit, Penumutchu Srinivasa, Kumar Abhishek, Zhou Qianzi, Wang Yiqing, Hansen Alexandar L, Kutluay Sebla, Roche Julien, Tolbert Blanton S

Abstract excerpt

The functional properties of RNA binding proteins (RBPs) require allosteric regulation through interdomain communication. Despite the importance of allostery to biological regulation, only a few studies have been conducted to describe the biophysical nature by which interdomain communication manifests in RBPs. Here, we show for hnRNP A1 that interdomain communication is vital for the unique stability of its...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Heterogeneous Nuclear Ribonucleoprotein A1

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Protein Binding

Share to Protein Domains

Share to Protein Stability

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 38985864
DOI: 10.1126/sciadv.adk6580
PMCID: PMC11235170

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

Thermodynamic coupling of the tandem RRM domains of hnRNP A1 underlie its pleiotropic RNA binding functions.PMID 38985864Read ↗

Small molecule binding to disordered proteinsSemantic proximity Read ↗

Stabilization and ATP-binding for tandem RRM domains of ALS-causing TDP-43 and hnRNPA1Semantic proximity Read ↗

Allosteric Dynamic Control of Binding.Semantic proximity Read ↗

Do intrinsically disordered proteins possess high specificity in protein-protein interactions?Semantic proximity Read ↗

An evolutionarily conserved tryptophan cage promotes folding of the extended RNA recognition motif in the hnRNPR-like protein familySemantic proximity Read ↗

An interdisciplinary study of the mechanical and dynamic properties of α-solenoid repeat proteinsSemantic proximity Read ↗

Multivalency enables unidirectional switch-like competition between intrinsically disordered proteins.Semantic proximity Read ↗

Liaison amid disorder: non-native interactions may underpin long-range coupling in proteins.Semantic proximity Read ↗

Molecular insights into the interaction between a disordered protein and a folded RNASemantic proximity Read ↗

Thermodynamic Architecture and Conformational Plasticity of GPCRsSemantic proximity Read ↗

HuR thermal stability is dependent on domain binding and upon phosphorylation.Semantic proximity Read ↗

Target Recognition in Tandem WW Domains: Complex Structures for Parallel and Antiparallel Ligand Orientation in h-FBP21 Tandem WWSemantic proximity Read ↗

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