Evidence map›Paper›PMID 7619079›Full record

ArticleThe Biochemical journal1995

Specificity and VH sequence of two monoclonal antibodies against the N-terminus of dystrophin.

G E Morris, C Nguyen, Nguyen thi Man

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

2 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. 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.

G E MorrisMRIC Biotechnology Group, North East Wales Institute, Deeside, Clwyd, U.K.
C Nguyen
Nguyen thi Man
North East University · BD

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have used a random library of 15-mer peptides expressed on phage to show that two monoclonal antibodies (mAbs) require only the first three amino acids of dystrophin (Leu-Trp-Trp) for binding. Since the mAbs recognize dystrophin in frozen muscle sections, the results suggest that this hydrophobic N-terminus of dystrophin is accessible to antibody in situ. Quantitative binding studies suggested minor differences in specificity between the two mAbs, so the Ig heavy-chain variable region (VH) sequences of the two hybridomas were determined by RT-PCR and cDNA sequencing. After elimination of PCR errors, the two cDNA sequences were found to be identical except for five somatic mutations which resulted in three amino acid changes in the second hypervariable region (CDR2). The results suggest that the two hybridomas originated from the same lymphocyte clone in a germinal centre of the spleen, but underwent different point mutations and subtype switches during clonal expansion to form blast cells.

Indexed as

Amino Acid SequenceAnimalsAntibodies, MonoclonalAntibody SpecificityBase SequenceCell LineDNA, ComplementaryDystrophinImmunoglobulin Heavy ChainsImmunoglobulin Variable RegionMiceMolecular Sequence DataSequence Homology, Amino AcidAntibodies, MonoclonalDNA, ComplementaryDystrophinImmunoglobulin Heavy ChainsImmunoglobulin Variable Region

Identifiers

PMID7619079
PMCPMC1135841
OpenAlexW299056724

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.