Evidence map›Paper›PMID 8506279›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1993

The LIM motif defines a specific zinc-binding protein domain.

J W Michelsen, K L Schmeichel, M C Beckerle, D R Winge

Abstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing 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

48 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Evo-devo applied to sleep research: an approach whose time has come.Sleep advances : a journal of the Sleep Research Society · 2024
    Review
  7. The Roles of FHL3 in Cancer.Frontiers in oncology · 2022
    Review
  8. Article
  9. LIM domain proteins in cell mechanobiology.Cytoskeleton (Hoboken, N.J.) · 2021
    Review
  10. Effect ofTranslational cancer research · 2021
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. 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

4 authors.

J W MichelsenDepartment of Biology, University of Utah, Salt Lake City 84132.
K L Schmeichel
M C Beckerle
D R Winge

Funding

UTAH REGIONAL CANCER CENTERP30CA042014 · NCI · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Jared P Rutter · 1986 to 2026
$72.6M
METAL CHELATION IN PROTEINS WITH POLYMETALLIC CLUSTERSR37ES003817 · NIEHS · UNIVERSITY OF UTAH · PI WINGE, DENNIS R. · 1999 to 2008
$4.1M
METAL CHELATION IN PROTEINS WITH POLYMETALLIC CLUSTERSR01ES003817 · NIEHS · UNIVERSITY OF UTAH · PI WINGE, DENNIS R. · 1985 to 2013
$2.3M
MEMBRANE-CYTOSKELETON LINKAGES IN PLATELETSR01HL041553 · NHLBI · UNIVERSITY OF UTAH · PI BECKERLE, MARY C. · 1989 to 1997
–
NCI NIH HHS CA42014NHLBI NIH HHS HL41553NIEHS NIH HHS ES03817
6 · The paper itself

Abstract

The cysteine-rich protein (CRP) contains two copies of the LIM sequence motif, CX2CX17HX2CX2CX2CX17-CX2C, that was first identified in the homeodomain proteins Lin-11, Is1-1, and Mec-3. The abundance and spacing of the cysteine residues in the LIM motif are reminiscent of a metal-binding domain. We examined the metal-binding properties of CRP isolated from chicken smooth muscle (cCRP) and from a bacterial expression system and observed that cCRP is a specific Zn-binding metalloprotein. Four Zn(II) ions are maximally bound to cCRP, consistent with the idea that each LIM domain coordinates two metal ions. From spectroscopic studies of Co(II)- and 113Cd(II)-substituted cCRP, we determined that each metal ion is tetrahedrally coordinated with cysteinyl sulfurs dominating the ligand types. One metal site within each LIM motif has tetrathiolate (S4) coordination, the second site may either be S4 or S3N1. The LIM motif represents another example of a specific Zn-binding protein sequence.

Indexed as

Avian ProteinsMuscle ProteinsAmino Acid SequenceAnimalsApoproteinsChickensCloning, MolecularCobaltConsensus SequenceMagnetic Resonance SpectroscopyMetalloproteinsMolecular Sequence DataProto-Oncogene Proteins c-mycRecombinant ProteinsSequence AlignmentZincApoproteinsAvian ProteinsCobaltcysteine-rich protein, avianMetalloproteinsMuscle ProteinsProto-Oncogene Proteins c-mycRecombinant ProteinsZinc

Identifiers

PMID8506279
PMCPMC46519

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.