ArticleActa crystallographica. Section F, Structural biology and crystallization communications2009
Structure of the thioredoxin-fold domain of human phosducin-like protein 2.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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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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.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- A structural vista of phosducin-like PhLP2A-chaperonin TRiC cooperation during the ATP-driven folding cycle.Nature communications · 2024Article
- The evolutionarily conserved PhLP3 is essential for sperm development in Drosophila melanogaster.PloS one · 2024Article
- Snapshots of actin and tubulin folding inside the TRiC chaperonin.Nature structural & molecular biology · 2022Article
- Combined RNA/tissue profiling identifies novel Cancer/testis genes.Molecular oncology · 2021Article
- Characterization of a protozoan Phosducin-like protein-3 (PhLP-3) reveals conserved redox activity.PloS one · 2018Article
- Identification of five genetic variants as novel determinants of type 2 diabetes mellitus in Japanese by exome-wide association studies.Oncotarget · 2017Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human phosducin-like protein 2 (hPDCL2) has been identified as belonging to subgroup II of the phosducin (Pdc) family. The members of this family share an N-terminal helix domain and a C-terminal thioredoxin-fold (Trx-fold) domain. The X-ray crystal structure of the Trx-fold domain of hPDCL2 was solved at 2.70 A resolution and resembled the Trx-fold domain of rat phosducin. Comparative structural analysis revealed the structural basis of their putative functional divergence.
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