Evidence map›Paper›PMID 19722279›Full record

ArticleProtein science : a publication of the Protein Society2009

Structure and interaction of ubiquitin-associated domain of human Fas-associated factor 1.

Jinsue Song, Joon Kyu Park, Jae-Jin Lee, Yun-Seok Choi, Kyoung-Seok Ryu, Jae-Hong Kim, Eunhee Kim, Kong-Joo Lee, Young-Ho Jeon, Eunice Eunkyeong Kim

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
0.7field-weighted citation impact, top 30% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
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  8. CBioMed research international · 2019
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  9. Article
  10. The AAA+ ATPase p97, a cellular multitool.The Biochemical journal · 2017
    Review
  11. Review
  12. Article
  13. UBXD Proteins: A Family of Proteins with Diverse Functions in Cancer.International journal of molecular sciences · 2016
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Protein domain definition should allow for conditional disorder.Protein science : a publication of the Protein Society · 2013
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 5 institutions in 1 country.

Jinsue SongMagnetic Resonance Team, Korea Basic Science Institute, 804-1 Yangchung-Ri, Ochang, Chungbuk, Korea.
Joon Kyu Park
Jae-Jin Lee
Yun-Seok Choi
Kyoung-Seok Ryu
Jae-Hong Kim
Eunhee Kim
Kong-Joo Lee
Young-Ho Jeon
Eunice Eunkyeong Kim
Korea Basic Science Institute · KREwha Womans University · KRKorea University · KRChungnam National University · KRKorea Institute of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fas-associated factor (FAF)-1 is a multidomain protein that was first identified as a member of the Fas death-inducing signaling complex, but later found to be involved in various biological processes. Although the exact mechanisms are not clear, FAF1 seems to play an important role in cancer, asbestos-induced mesotheliomas, and Parkinson's disease. It interacts with polyubiquitinated proteins, Hsp70, and p97/VCP (valosin-containing protein), in addition to the proteins of the Fas-signaling pathway. We have determined the crystal structure of the ubiquitin-associated domain of human FAF1 (hFAF1-UBA) and examined its interaction with ubiquitin and ubiquitin-like proteins using nuclear magnetic resonance. hFAF1-UBA revealed a canonical three-helical bundle that selectively binds to mono- and di-ubiquitin (Lys48-linked), but not to SUMO-1 (small ubiquitin-related modifier 1) or NEDD8 (neural precursor cell expressed, developmentally down-regulated 8). The interaction between hFAF1-UBA and di-ubiquitin involves hydrophobic interaction accompanied by a transition in the di-ubiquitin conformation. These results provide structural insight into the mechanism of polyubiquitin recognition by hFAF1-UBA.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceApoptosis Regulatory ProteinsBinding SitesCell LineCrystallography, X-RayHumansModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularProtein BindingProtein Structure, TertiarySequence AlignmentUbiquitinUbiquitinsAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsFAF1 protein, humanUBD protein, humanUbiquitinUbiquitins

Identifiers

PMID19722279
PMCPMC2788281
OpenAlexW2098677951

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.