ArticleProtein & cell2010
Crystal structures of NAC domains of human nascent polypeptide-associated complex (NAC) and its αNAC subunit.
Article in Protein & cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed.
- A molecular switch in NAC prevents mitochondrial protein mistargeting by SRP.Nature communications · 2026Article
- Mechanistic Insights into Protein Biogenesis and Maturation on the Ribosome.Journal of molecular biology · 2025Review
- Screening and functional characterization of salt-tolerant NAC gene family members inFrontiers in plant science · 2025Article
- Genome-Wide Identification and Expression Analysis ofPlants (Basel, Switzerland) · 2024Article
- NAC and Zuotin/Hsp70 chaperone systems coexist at the ribosome tunnel exit in vivo.Nucleic acids research · 2024Article
- Chp1 is a dedicated chaperone at the ribosome that safeguards eEF1A biogenesis.Nature communications · 2024Article
- Matrine Targets BTF3 to Inhibit the Growth of Canine Mammary Tumor Cells.International journal of molecular sciences · 2023Article
- Article
- Mechanism of signal sequence handover from NAC to SRP on ribosomes during ER-protein targeting.Science (New York, N.Y.) · 2022Article
- Fidelity of Cotranslational Protein Targeting to the Endoplasmic Reticulum.International journal of molecular sciences · 2021Review
- A ribosome-associated chaperone enables substrate triage in a cotranslational protein targeting complex.Nature communications · 2020Article
- TTC5 mediates autoregulation of tubulin via mRNA degradation.Science (New York, N.Y.) · 2020Article
- Chaperone Interactions at the Ribosome.Cold Spring Harbor perspectives in biology · 2019Review
- Dephosphorylation of the transcriptional cofactor NACA by the PP1A phosphatase enhances cJUN transcriptional activity and osteoblast differentiation.The Journal of biological chemistry · 2019Article
- Dual Role of Ribosome-Binding Domain of NAC as a Potent Suppressor of Protein Aggregation and Aging-Related Proteinopathies.Molecular cell · 2019Article
- Conformational flexibility within the nascent polypeptide-associated complex enables its interactions with structurally diverse client proteins.The Journal of biological chemistry · 2018Article
- Functional Dissection of the Nascent Polypeptide-Associated Complex in Saccharomyces cerevisiae.PloS one · 2015Article
- Cytokine effects induced by the human autoallergen α-NAC.The Journal of investigative dermatology · 2014Article
- NAC functions as a modulator of SRP during the early steps of protein targeting to the endoplasmic reticulum.Molecular biology of the cell · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nascent polypeptide associated complex (NAC) and its two isolated subunits, αNAC and βNAC, play important roles in nascent peptide targeting. We determined a 1.9 Å resolution crystal structure of the interaction core of NAC heterodimer and a 2.4 Å resolution crystal structure of αNAC NAC domain homodimer. These structures provide detailed information of NAC heterodimerization and αNAC homodimerization. We found that the NAC domains of αNAC and βNAC share very similar folding despite of their relative low identity of amino acid sequences. Furthermore, different electric charge distributions of the two subunits at the NAC interface provide an explanation to the observation that the heterodimer of NAC complex is more stable than the single subunit homodimer. In addition, we successfully built a βNAC NAC domain homodimer model based on homologous modeling, suggesting that NAC domain dimerization is a general property of the NAC family. These 3D structures allow further studies on structure-function relationship of NAC.
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.