ReviewEuropean biophysics journal : EBJ2012
Validation of macromolecular flexibility in solution by small-angle X-ray scattering (SAXS).
Review in European biophysics journal : EBJ, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
68 citing papers in PubMed.
- BilboMD: a web-accessible SAXS and AlphaFold-guided modeling pipeline.Nucleic acids research · 2026Article
- A Rahman Syndrome mutation in histone H1.4 disrupts chromatin compaction and phase separation.Nature communications · 2026Article
- Internal Dynamics of Pyrene-Labeled Polyols Studied Through the Lens of Pyrene Excimer Formation.Polymers · 2025Article
- Isoleucine Binding and Regulation ofBiochemistry · 2025Article
- Predicting RNA structure and dynamics with deep learning and solution scattering.Biophysical journal · 2025Article
- Predicting RNA Structure and Dynamics with Deep Learning and Solution Scattering.bioRxiv : the preprint server for biology · 2024Article
- Structural and Functional Biology of Mammalian ALOX Isoforms with Particular Emphasis on Enzyme Dimerization and Their Allosteric Properties.International journal of molecular sciences · 2024Review
- Altered Protein Dynamics and a More Reactive Catalytic Cysteine in a Neurodegeneration-associated UCHL1 Mutant.Journal of molecular biology · 2024Article
- Effects ofFrontiers in molecular biosciences · 2024Article
- Resolving domain positions of cellobiose dehydrogenase by small angle X-ray scattering.The FEBS journal · 2023Article
- The solution structure of the unbound IgG Fc receptor CD64 resembles its crystal structure: Implications for function.PloS one · 2023Article
- Interdomain Linkers Regulate Histidine Kinase Activity by Controlling Subunit Interactions.Biochemistry · 2022Article
- SAXS analysis of the intrinsic tenase complex bound to a lipid nanodisc highlights intermolecular contacts between factors VIIIa/IXa.Blood advances · 2022Article
- Untangling the Conformational Plasticity of V66M Human proBDNF Polymorphism as a Modifier of Psychiatric Disorder Susceptibility.International journal of molecular sciences · 2022Article
- Domain architecture and catalysis of the Staphylococcus aureus fatty acid kinase.The Journal of biological chemistry · 2022Article
- NaStructure (London, England : 1993) · 2021Article
- The role of SAXS and molecular simulations in 3D structure elucidation of a DNA aptamer against lung cancer.Molecular therapy. Nucleic acids · 2021Article
- X-ray scattering reveals disordered linkers and dynamic interfaces in complexes and mechanisms for DNA double-strand break repair impacting cell and cancer biology.Protein science : a publication of the Protein Society · 2021Review
- Visualizing functional dynamicity in the DNA-dependent protein kinase holoenzyme DNA-PK complex by integrating SAXS with cryo-EM.Progress in biophysics and molecular biology · 2021Article
- Albumin in patients with liver disease shows an altered conformation.Communications biology · 2021Article
8 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
Abstract
The dynamics of macromolecular conformations are critical to the action of cellular networks. Solution X-ray scattering studies, in combination with macromolecular X-ray crystallography (MX) and nuclear magnetic resonance (NMR), strive to determine complete and accurate states of macromolecules, providing novel insights describing allosteric mechanisms, supramolecular complexes, and dynamic molecular machines. This review addresses theoretical and practical concepts, concerns, and considerations for using these techniques in conjunction with computational methods to productively combine solution-scattering data with high-resolution structures. I discuss the principal means of direct identification of macromolecular flexibility from SAXS data followed by critical concerns about the methods used to calculate theoretical SAXS profiles from high-resolution structures. The SAXS profile is a direct interrogation of the thermodynamic ensemble and techniques such as, for example, minimal ensemble search (MES), enhance interpretation of SAXS experiments by describing the SAXS profiles as population-weighted thermodynamic ensembles. I discuss recent developments in computational techniques used for conformational sampling, and how these techniques provide a basis for assessing the level of the flexibility within a sample. Although these approaches sacrifice atomic detail, the knowledge gained from ensemble analysis is often appropriate for developing hypotheses and guiding biochemical experiments. Examples of the use of SAXS and combined approaches with X-ray crystallography, NMR, and computational methods to characterize dynamic assemblies are presented.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.