Evidence map›Paper›PMID 9451007›Full record

ArticleThe EMBO journal1998

A helix-turn-helix structure unit in human centromere protein B (CENP-B).

J Iwahara, T Kigawa, K Kitagawa, H Masumoto, T Okazaki, S Yokoyama

Abstract read
In one paragraph

Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
6.2field-weighted citation impact, top 4% 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

16 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Non-B-Form DNA Is Enriched at Centromeres.Molecular biology and evolution · 2018
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. CENP-B box and pJalpha sequence distribution in human alpha satellite higher-order repeats (HOR).Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2006
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. 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

6 authors at 1 institution in 1 country.

J IwaharaDepartment of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Bunkyo-ku, Tokyo 113.
T Kigawa
K Kitagawa
H Masumoto
T Okazaki
S Yokoyama
The University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

CENP-B has been suggested to organize arrays of centromere satellite DNA into a higher order structure which then directs centromere formation and kinetochore assembly in mammalian chromosomes. The N-terminal portion of CENP-B is a 15 kDa DNA binding domain (DBD) consisting of two repeating units, RP1 and RP2. The DBD specifically binds to the CENP-B box sequence (17 bp) in centromere DNA. We determined the solution structure of human CENP-B DBD RP1 by multi-dimensional 1H, 13C and 15N NMR methods. The CENP-B DBD RP1 structure consists of four helices and has a helix-turn-helix structure. The overall folding is similar to those of some other eukaryotic DBDs, although significant sequence homology with these proteins was not found. The DBD of yeast RAP1, a telomere binding protein, is most similar to CENP-B DBD RP1. We studied the interaction between CENP-B DBD RP1 and the CENP-B box by the use of NMR chemical shift perturbation. The results suggest that CENP-B DBD RP1 interacts with one of the essential regions of the CENP-B box DNA, mainly at the N-terminal basic region, the N-terminal portion of helix 2 and helix 3.

Indexed as

AutoantigensAmino Acid SequenceBase CompositionBinding SitesCentromere Protein BChromosomal Proteins, Non-HistoneDNA-Binding ProteinsHelix-Turn-Helix MotifsHumansMacromolecular SubstancesMagnetic Resonance SpectroscopyModels, BiologicalMolecular Sequence DataProtein Structure, TertiarySequence Homology, Amino AcidSolutionsAutoantigensCENPB protein, humanCentromere Protein BChromosomal Proteins, Non-HistoneDNA-Binding ProteinsMacromolecular SubstancesSolutions

Identifiers

PMID9451007
PMCPMC1170431
OpenAlexW2026453837

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.