ArticleThe EMBO journal2001
Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
54 citing papers in PubMed, 117 citations in OpenAlex.
- Binding of Bacillus subtilis dynamin-like protein DynA to the bacterial membrane is essential for effective phage defense.The FEBS journal · 2026Article
- Protein Architecture and Composition in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Conformational Rearrangement of Fission DSPs.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Molecular mechanisms of mitochondrial dynamics.Nature reviews. Molecular cell biology · 2025Review
- Structural basis for regulated assembly of the mitochondrial fission GTPase Drp1.Nature communications · 2024Article
- The Chemical Inhibitors of Endocytosis: From Mechanisms to Potential Clinical Applications.Cells · 2023Review
- Cellular and structural insight into dynamin function during endocytic vesicle formation: a tale of 50 years of investigation.Bioscience reports · 2022Review
- Role of Clathrin and Dynamin in Clathrin Mediated Endocytosis/Synaptic Vesicle Recycling and Implications in Neurological Diseases.Frontiers in cellular neuroscience · 2021Review
- Review
- Affinity Purification and Functional Characterization of Dynamin-Related Protein 1.Methods in molecular biology (Clifton, N.J.) · 2020Article
- The structural biology of the dynamin-related proteins: New insights into a diverse, multitalented family.Traffic (Copenhagen, Denmark) · 2019Review
- Deciphering the three-domain architecture in schlafens and the structures and roles of human schlafen12 and serpinB12 in transcriptional regulation.Journal of molecular graphics & modelling · 2019Article
- Structural Insights into the Mechanism of Dynamin Superfamily Proteins.Trends in cell biology · 2019Review
- T4 lysozyme-facilitated crystallization of the human molybdenum cofactor-dependent enzyme mARC.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Mitochondrial dynamics: The dynamin superfamily and execution by collusion.Seminars in cell & developmental biology · 2018Review
- Article
- Invited review: Mechanisms of GTP hydrolysis and conformational transitions in the dynamin superfamily.Biopolymers · 2016Review
- Distinct Splice Variants of Dynamin-related Protein 1 Differentially Utilize Mitochondrial Fission Factor as an Effector of Cooperative GTPase Activity.The Journal of biological chemistry · 2016Article
- Evolutionary Analyses Suggest a Function of MxB Immunity Proteins Beyond Lentivirus Restriction.PLoS pathogens · 2015Article
- Synthesis of Dynole 34-2, Dynole 2-24 and Dyngo 4a for investigating dynamin GTPase.Nature protocols · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dynamins form a family of multidomain GTPases involved in endocytosis, vesicle trafficking and maintenance of mitochondrial morphology. In contrast to the classical switch GTPases, a force-generating function has been suggested for dynamins. Here we report the 2.3 A crystal structure of the nucleotide-free and GDP-bound GTPase domain of Dictyostelium discoideum dynamin A. The GTPase domain is the most highly conserved region among dynamins. The globular structure contains the G-protein core fold, which is extended from a six-stranded beta-sheet to an eight-stranded one by a 55 amino acid insertion. This topologically unique insertion distinguishes dynamins from other subfamilies of GTP-binding proteins. An additional N-terminal helix interacts with the C-terminal helix of the GTPase domain, forming a hydrophobic groove, which could be occupied by C-terminal parts of dynamin not present in our construct. The lack of major conformational changes between the nucleotide-free and the GDP-bound state suggests that mechanochemical rearrangements in dynamin occur during GTP binding, GTP hydrolysis or phosphate release and are not linked to loss of GDP.
Indexed as
Identifiers
What OpenQuestion holds
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.