Evidence map›Paper›PMID 22869111›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2012

Structure of human Rack1 protein at a resolution of 2.45 Å.

David Ruiz Carrillo, Ramya Chandrasekaran, Martina Nilsson, Tobias Cornvik, Chong Wai Liew, Suet Mien Tan, Julien Lescar

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
–field-weighted citation impact
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

35 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. RACK1 promotesiScience · 2023
    Article
  12. Role of pyroptosis in inflammation and cancer.Cellular & molecular immunology · 2022
    Review
  13. Article
  14. Article
  15. Article
  16. RACK1 on and off the ribosome.RNA (New York, N.Y.) · 2019
    Article
  17. Article
  18. Capturing the Asc1p/Molecular & cellular proteomics : MCP · 2017
    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

7 authors.

David Ruiz CarrilloSchool of Biological Sciences, Nanyang Technological University, Singapore.
Ramya Chandrasekaran
Martina Nilsson
Tobias Cornvik
Chong Wai Liew
Suet Mien Tan
Julien Lescar

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The crystal structure of human receptor for activated C-kinase 1 (hRack1) protein is reported at 2.45 Å resolution. The crystals belongs to space group P4(1)2(1)2, with three molecules per asymmetric unit. The hRack1 structure features a sevenfold β-propeller, with each blade housing a sequence motif that contains a strictly conserved Trp, the indole group of which is embedded between adjacent blades. In blades 1-5 the imidazole group of a His residue is wedged between the side chains of a Ser residue and an Asp residue through two hydrogen bonds. The hRack1 crystal structure forms a starting basis for understanding the remarkable scaffolding properties of this protein.

Indexed as

Amino Acid SequenceCrystallography, X-RayGTP-Binding ProteinsHumansModels, MolecularMolecular Sequence DataNeoplasm ProteinsProtein Structure, QuaternaryProtein Structure, TertiaryReceptors, Cell SurfaceReceptors for Activated C KinaseSequence AlignmentSequence Homology, Amino AcidStructural Homology, ProteinGTP-Binding ProteinsNeoplasm ProteinsRACK1 protein, humanReceptors, Cell SurfaceReceptors for Activated C Kinase

Identifiers

PMID22869111
PMCPMC3412762

What OpenQuestion holds

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Registered trials

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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.