Evidence map›Paper›PMID 1372440›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1992

Isolation and characterization of human cDNA clones encoding a high mobility group box protein that recognizes structural distortions to DNA caused by binding of the anticancer agent cisplatin.

S L Bruhn, P M Pil, J M Essigmann, D E Housman, S J Lippard

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
10.2field-weighted citation impact, top 1% 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

72 citing papers in PubMed, 251 citations in OpenAlex.

  1. Article
  2. Research Progress of LEF1 Gene in Malignant Tumors.Clinical Medicine Insights. Oncology · 2025
    Review
  3. Facilitates Chromatin Transcription in Breast and Other Cancers.Advances in experimental medicine and biology · 2024
    Review
  4. Review
  5. Structure and function of the histone chaperone FACT - Resolving FACTual issues.Biochimica et biophysica acta. Gene regulatory mechanisms · 2018
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. HMGB1 in health and disease.Molecular aspects of medicine · 2014
    Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. The sequence selectivity of DNA-targeted 9-aminoacridine cisplatin analogues in a telomere-containing DNA sequence.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011
    Article
  20. Article

12 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

S L BruhnDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge 02139.
P M Pil
J M Essigmann
D E Housman
S J Lippard
Massachusetts Institute of Technology · US

Funding

PATHOBIOLOGY OF B16 MELANOMA METASTASISR01CA032134 · NCI · NEW YORK MEDICAL COLLEGE · PI STACKPOLE, CHRISTOPHER W · 1985 to 1988
–
CELLULAR RESPONSE TO DNA DAMAGER35CA052127 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ESSIGMANN, JOHN M · 1990 to 1998
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NCI NIH HHS CA 32134NCI NIH HHS CA 52127
6 · The paper itself

Abstract

Human cDNA clones encoding a structure-specific recognition protein, SSRP1, that binds specifically to DNA modified with cisplatin have been isolated and characterized. The SSRP1 gene maps to human chromosome 11q12. The cDNA clones, obtained by using partial-length cDNAs described previously, predict an 81-kDa protein containing several highly charged domains and a stretch of 75 amino acids 47% identical to a portion of the high mobility group (HMG) protein HMG1. This HMG box most likely constitutes the structure recognition element for cisplatin-modified DNA, with the probable recognition motif being the local duplex unwinding and bending toward the major groove that occurs upon formation of intrastrand cis-[Pt(NH3)2]2+ d(GpG) and d(ApG) cross-links. Although the DNA recognition properties of members of the HMG-box family of proteins have been characterized with respect to their sequence specificity, the present work demonstrates that proteins with this domain can recognize particular DNA structures as well. The Pt-DNA SSRP described here is the human homolog of a recently identified mouse protein that binds to recombination signal sequences [Shirakata, M., Hüppi, K., Usuda, S., Okazaki, K., Yoshida, K. & Sakano, H. (1991) Mol. Cell. Biol. 11, 4528-4536]. These sequences have been postulated to form stem-loop structures, further implicating local bends and unwinding in DNA as a recognition target for HMG-box proteins. Expression analysis in a variety of tissues and cisplatin-resistant cell lines and the inability of cisplatin to induce the message in HeLa cells argue against a direct link between SSRP1 mRNA levels and the response of cells to the drug.

Indexed as

Transcriptional Elongation FactorsAmino Acid SequenceAnimalsBase SequenceBlotting, NorthernChromosomes, Human, Pair 11CisplatinCloning, MolecularDNADNA-Binding ProteinsEscherichia coliGene LibraryHeLa CellsHigh Mobility Group ProteinsHumansMolecular Sequence DataCisplatinDNADNA-Binding ProteinsHigh Mobility Group ProteinsRNASSRP1 protein, humanSsrp1 protein, mouseTranscriptional Elongation Factors

Identifiers

PMID1372440
PMCPMC48646
OpenAlexW2045630690

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.