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

Mechanistic insights into temperature-dependent regulation of the simple cyanobacterial hsp17 RNA thermometer at base-pair resolution.

Nucleic acids research - 23 Jun 2015

Wagner Dominic, Rinnenthal Jörg, Narberhaus Franz, Schwalbe Harald

Abstract excerpt

The cyanobacterial hsp17 ribonucleicacid thermometer (RNAT) is one of the smallest naturally occurring RNAT. It forms a single hairpin with an internal 1×3-bulge separating the start codon in stem I from the ribosome binding site (RBS) in stem II. We investigated the temperature-dependent regulation of hsp17 by mapping individual base-pair stabilities from solvent exchange nuclear magnetic resonance (NMR)...

Read the complete abstract on PubMed

Topics

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

Share to Base Pairing
Share to Entropy
Share to Heat-Shock Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protons

Share to RNA, Bacterial

Share to RNA Folding

Share to Synechocystis

Source

Open in PubMed Open full text

Identifiers

PMID: 25940621
DOI: 10.1093/nar/gkv414
PMCID: PMC4477652

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

Mechanistic insights into temperature-dependent regulation of the simple cyanobacterial hsp17 RNA thermometer at base-pair resolution.PMID 25940621Read ↗

Temperature-controlled structural alterations of an RNA thermometer.Semantic proximity Read ↗

Comparative study on tertiary contacts and folding of RNase P RNAs from a psychrophilic, a mesophilic/radiation-resistant, and a thermophilic bacterium.Semantic proximity Read ↗

SHAPE analysis of the htrA RNA thermometer from Salmonella enterica.Semantic proximity Read ↗

Extreme temperature tolerance of a hyperthermophilic protein coupled to residual structure in the unfolded state.Semantic proximity Read ↗

Large favorable enthalpy changes drive specific RNA recognition by RNA recognition motif proteins.Semantic proximity Read ↗

Translational induction of heat shock transcription factor sigma32: evidence for a built-in RNA thermosensor.Semantic proximity Read ↗

Exploring the Dynamics and Mutational Landscape of Riboregulation with a Minimal Synthetic Circuit in Living Cells.Semantic proximity Read ↗

The thermostability of DNA-binding protein HU from mesophilic, thermophilic, and extreme thermophilic bacteria.Semantic proximity Read ↗

Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis.Semantic proximity Read ↗

Non-nearest neighbor effects on the thermodynamics of unfolding of a model mRNA pseudoknot.Semantic proximity Read ↗

T-rich DNA single strands bind to a preformed site on the bacterial cold shock protein Bs-CspB.Semantic proximity Read ↗

Thermally induced structural changes of intrinsically disordered small heat shock protein Hsp22.Semantic proximity Read ↗

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