Evidence map›Paper›PMID 10926853›Full record

ArticleThe Biochemical journal2000

Fine mapping of the alpha-actinin binding site within cysteine-rich protein.

B D Harper, M C Beckerle, P Pomiès

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

13 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Review
  3. Characterization of an MLP Homologue fromPathogens (Basel, Switzerland) · 2020
    Article
  4. Article
  5. Building Blocks of Functioning Brain: Cytoskeletal Dynamics in Neuronal Development.International review of cell and molecular biology · 2016
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Muscle LIM protein in heart failure.Experimental and clinical cardiology · 2002
    Article
  13. 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

3 authors at 1 institution in 1 country.

B D HarperDepartment of Biology and Huntsman Cancer Institute, University of Utah, Salt Lake City, UT 84112-5550, USA.
M C Beckerle
P Pomiès
Huntsman Cancer Institute · US

Funding

Structure and function of muscleR01HL060591 · NHLBI · UNIVERSITY OF UTAH · PI BECKERLE, MARY C. · 1998 to 2005
$2.0M
NHLBI NIH HHS HL60591
6 · The paper itself

Abstract

The cysteine-rich proteins (CRPs) are a family of highly conserved LIM (an acronym derived from the three gene products lin-11, isl-1 and mec-3) domain proteins that have been implicated in muscle differentiation. All CRP family members characterized so far have been shown to interact with the filamentous actin cross-linker alpha-actinin. The region of CRP required for this interaction has previously been broadly mapped to the molecule's N-terminal half. Here we report that the alpha-actinin-binding region of CRP, which we have mapped by using a combination of blot overlay and Western immunoblot techniques, is confined to an 18-residue sequence occurring within the protein's N-terminal glycine-rich repeat. A site-directed mutagenesis analysis of the binding region has revealed the critical importance of a single lysine residue (lysine 65 in human CRP1). Alterations at this site lead to a 10-fold decrease in alpha-actinin binding in comparison with wild-type CRP. The critical lysine residue localizes within a short alpha-helix, raising the possibility that mutagenesis-induced alterations in alpha-actinin-binding capacity might be attributed to the disruption of a key structural element.

Indexed as

Nuclear ProteinsActininAmino Acid SequenceBinding SitesCysteineGlycineLIM Domain ProteinsMolecular Sequence DataMuscle ProteinsProtein ConformationSequence Homology, Amino AcidActininCsrp1 protein, mouseCysteineGlycineLIM Domain ProteinsMuscle ProteinsNuclear Proteins

Identifiers

PMID10926853
PMCPMC1221251
OpenAlexW1968387777

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.