ArticleStructure (London, England : 1993)2018
Conservation of Dynamics Associated with Biological Function in an Enzyme Superfamily.
Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Large Numbers of New Human Paralogs Discovered.bioRxiv : the preprint server for biology · 2025Article
- Sequence - dynamics - function relationships in protein tyrosine phosphatases.QRB discovery · 2024Article
- Loop dynamics and the evolution of enzyme activity.Nature reviews. Chemistry · 2023Review
- Conformational exchange divergence along the evolutionary pathway of eosinophil-associated ribonucleases.Structure (London, England : 1993) · 2023Article
- A multi-layered computational structural genomics approach enhances domain-specific interpretation of Kleefstra syndrome variants in EHMT1.Computational and structural biotechnology journal · 2023Article
- Identifying structural and dynamic changes during the Biliverdin Reductase B catalytic cycle.Frontiers in molecular biosciences · 2023Article
- Capture of activated dioxygen intermediates at the copper-active site of a lytic polysaccharide monooxygenase.Chemical science · 2022Article
- Insights into the importance of WPD-loop sequence for activity and structure in protein tyrosine phosphatases.Chemical science · 2022Article
- Conserved conformational dynamics determine enzyme activity.Science advances · 2022Article
- Mechanism of nucleotide discrimination by the translesion synthesis polymerase Rev1.Nature communications · 2022Article
- Enzyme dynamics: Looking beyond a single structure.ChemCatChem · 2020Article
- Allosteric pluripotency as revealed by protein kinase A.Science advances · 2020Article
- Insights into Structural and Dynamical Changes Experienced by Human RNase 6 upon Ligand Binding.Biochemistry · 2020Article
- Engineering Dynamic Surface Peptide Networks on ButyrylcholinesteraseChemical research in toxicology · 2019Article
- The Structural Dynamics of Engineered β-Lactamases Vary Broadly on Three Timescales yet Sustain Native Function.Scientific reports · 2019Article
- A Biophysical Perspective on Enzyme Catalysis.Biochemistry · 2019Article
- Nucleotide substrate binding characterization in human pancreatic-type ribonucleases.PloS one · 2019Article
- Evolutionary Trends in RNA Base Selectivity Within the RNase A Superfamily.Frontiers in pharmacology · 2019Article
- Differential Substrate Recognition by Maltose Binding Proteins Influenced by Structure and Dynamics.Biochemistry · 2018Article
- gRINN: a tool for calculation of residue interaction energies and protein energy network analysis of molecular dynamics simulations.Nucleic acids research · 2018Article
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7 authors.
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Abstract
Enzyme superfamily members that share common chemical and/or biological functions also share common features. While the role of structure is well characterized, the link between enzyme function and dynamics is not well understood. We present a systematic characterization of intrinsic dynamics of over 20 members of the pancreatic-type RNase superfamily, which share a common structural fold. This study is motivated by the fact that the range of chemical activity as well as molecular motions of RNase homologs spans over 10
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