Evidence map›Paper›PMID 8404852›Full record

ArticleThe EMBO journal1993

Phosphorylation of KSP motifs in the C-terminal region of titin in differentiating myoblasts.

M Gautel, K Leonard, S Labeit

Abstract read
In one paragraph

Article in The EMBO journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

28 citing papers in PubMed, 113 citations in OpenAlex.

  1. Article
  2. Article
  3. Alterations in cytoskeletal and CaFrontiers in cardiovascular medicine · 2023
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Review
  13. Conformation-regulated mechanosensory control via titin domains in cardiac muscle.Pflugers Archiv : European journal of physiology · 2011
    Review
  14. Review
  15. Titin-based mechanosensing and signaling: role in diaphragm atrophy during unloading?American journal of physiology. Lung cellular and molecular physiology · 2011
    Review
  16. Article
  17. Review
  18. Studies on titin PEVK peptides and their interaction.Archives of biochemistry and biophysics · 2006
    Article
  19. Article
  20. Review
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

3 authors.

M GautelEuropean Molecular Biology Laboratory, Biological Structures Division, Heidelberg.
K Leonard
S Labeit

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Titin is a giant structural protein of striated muscle (M(r) approximately 3000 kDa) and single molecules span sarcomeres from the M- to Z-lines. We have cloned and sequenced the C-terminal region of the titin molecule, which is an integral part of M-lines and forms intimate contacts with the 165 and 190 kDa M-line proteins. In contrast to the regular motif patterns of the A-band portion of titin, the 5.7 kb of titin sequences from the M-line show a complex structure of immunoglobulin-C2 repeats, separated by unique interdomain insertion sequences. As a striking feature, one interdomain insertion comprises four KSP repeats analogous to the multi-phosphorylation repeats of neurofilament subunits H and M. In vitro phosphorylation assays with expressed titin KSP sequences detect high levels of titin KSP phosphorylating kinases in developing but not in differentiated muscle. Since this kinase activity can be depleted from myocyte extracts by antibodies against cdc2 kinase and p13suc1 beads, the titin KSP kinase is structurally related to cdc2 kinase. We suggest that titin C-terminal phosphorylation by SP-specific kinases is regulated during differentiation, and that this may control the assembly of M-line proteins into regular structures during myogenesis.

Indexed as

Amino Acid SequenceAnimalsBase SequenceCell DifferentiationCells, CulturedCloning, MolecularConnectinHumansMiceMolecular Sequence DataMuscle ProteinsMusclesMutagenesis, Site-DirectedMyocardiumPhosphorylationProtein KinasesConnectinMuscle ProteinsProtein KinasesTTN protein, human

Identifiers

PMID8404852
PMCPMC413666
OpenAlexW1827310380

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.