Evidence map›Paper›PMID 11448986›Full record

ReviewThe Journal of cell biology2001

Fishing out proteins that bind to titin.

J W Sanger, J M Sanger

Open access · bronzeAbstract readCommentReview
In one paragraph

Review in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

19 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Titin mutations: the fall of Goliath.Heart failure reviews · 2015
    Review
  7. Biophysical characterization of naturally occurring titin M10 mutations.Protein science : a publication of the Protein Society · 2015
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Mechanotransduction in skeletal muscle.Frontiers in bioscience : a journal and virtual library · 2007
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. How to build a myofibril.Journal of muscle research and cell motility · 2005
    Article
  19. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

J W SangerDepartment of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA. sangerj@mail.med.upenn.edu
J M Sanger
University of Pennsylvania · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Another giant protein has been detected in cross-striated muscle cells. Given the name obscurin, it was discovered in a yeast two-hybrid screen in which the bait was a small region of titin that is localized near the Z-band. Obscurin is about 720 kD, similar in molecular weight to nebulin, but present at about one tenth the level (Young et al., 2001). Like titin, obscurin contains multiple immunoglobulin-like domains linked in tandem, but in contrast to titin it contains just two fibronectin-like domains. It also contains sequences that suggest obscurin may have roles in signal transduction. During embryonic development, its localization changes from the Z-band to the M-band. With these intriguing properties, obscurin may not remain obscure for long.

Indexed as

AnimalsConnectinFibronectinsImmunoglobulinsModels, BiologicalMuscle ProteinsMuscle, SkeletalMyocardiumProtein BindingProtein KinasesProtein Structure, TertiarySignal TransductionTwo-Hybrid System TechniquesConnectinFibronectinsImmunoglobulinsMuscle ProteinsProtein Kinases

Identifiers

PMID11448986
PMCPMC2196855
OpenAlexW2112605964

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.