ArticleJournal of molecular biology2009
Topology is the principal determinant in the folding of a complex all-alpha Greek key death domain from human FADD.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed, 28 citations in OpenAlex.
- Slowest-first protein translation scheme: Structural asymmetry and co-translational folding.Biophysical journal · 2021Article
- Insights into the structure and RNA-binding specificity of Caenorhabditis elegans Dicer-related helicase 3 (DRH-3).Nucleic acids research · 2021Article
- Network Connectivity, Centrality and Fragmentation in the Greek-Key Protein Topology.The protein journal · 2019Article
- Structure of the C-terminal domain of TRADD reveals a novel fold in the death domain superfamily.Scientific reports · 2017Article
- Structural insights of homotypic interaction domains in the ligand-receptor signal transduction of tumor necrosis factor (TNF).BMB reports · 2016Review
- The response of Greek key proteins to changes in connectivity depends on the nature of their secondary structure.Journal of molecular biology · 2015Article
- Structures of the NLRP14 pyrin domain reveal a conformational switch mechanism regulating its molecular interactions.Acta crystallographica. Section D, Biological crystallography · 2014Article
- The loop hypothesis: contribution of early formed specific non-local interactions to the determination of protein folding pathways.Biophysical reviews · 2013Review
- Take home lessons from studies of related proteins.Current opinion in structural biology · 2013Review
- Molecular basis of NF-κB signaling.Annual review of biophysics · 2013Review
- Helical assembly in the death domain (DD) superfamily.Current opinion in structural biology · 2012Review
- Folding of an all-helical Greek-key protein monitored by quenched-flow hydrogen-deuterium exchange and NMR spectroscopy.European biophysics journal : EBJ · 2012Article
- What lessons can be learned from studying the folding of homologous proteins?Methods (San Diego, Calif.) · 2010Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In order to elucidate the relative importance of secondary structure and topology in determining folding mechanism, we have carried out a phi-value analysis of the death domain (DD) from human FADD. FADD DD is a 100 amino acid domain consisting of six anti-parallel alpha helices arranged in a Greek key structure. We asked how does the folding of this domain compare with that of (a) other all-alpha-helical proteins and (b) other Greek key proteins? Is the folding pathway determined mainly by secondary structure or is topology the principal determinant? Our Phi-value analysis reveals a striking resemblance to the all-beta Greek key immunoglobulin-like domains. Both fold via diffuse transition states and, importantly, long-range interactions between the four central elements of secondary structure are established in the transition state. The elements of secondary structure that are less tightly associated with the central core are less well packed in both cases. Topology appears to be the dominant factor in determining the pathway of folding in all Greek key domains.
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.