Evidence map›Paper›PMID 11876299›Full record

ArticleMolecular biotechnology2002

MALDI/MS-based epitope mapping of antigens bound to immobilized antibodies.

Carol E Parker, Kenneth B Tomer

Abstract read
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In one paragraph

Article in Molecular biotechnology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. 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

2 authors.

Carol E ParkerLaboratory of Molecular Biophysics, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709, USA. parkerc@niehs.nih.gov
Kenneth B Tomer

Funding

EPITOPE MAPPING OF HIV PROTEINS USING PROTEOLYTIC FOOT PRINTING AND MSZ01ES050151 · NIEHS · ENVIRONMENTAL HEALTH SCIENCES · PI TOMER, KENNETH · 1996 to 2002
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Receptor Ligand Interactions Relevant to HIV InfectionZ01ES050152 · NIEHS · ENVIRONMENTAL HEALTH SCIENCES · PI TOMER, KENNETH · 1996 to 2002
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6 · The paper itself

Abstract

Proteolytic digestion of proteins bound to immobilized antibodies, combined with matrix assisted laser desorption (MALDI) mass spectrometric identification of the affinity-bound peptides, can be a powerful technique for epitope determination. Binding of the protein to the antibody is done while the protein is in its native, folded state. A purified protein is not required for this procedure, because only proteins containing the antigenic determinant will bind to the antibody in the initial step. The method makes use of the resistance of the antibody to enzymatic digestion. Enzymatic cleavage products of the antigenic protein not containing the epitope are washed off the beads, leaving the epitope-containing fragments affinity bound to the immobilized antibody. Dissociation of the antigen-antibody complex prior to mass spectrometric analysis is unnecessary because the affinity-bound peptides are released by the MALDI matrix crystallization process, although the antibody remains covalently attached to the sepharose beads. This epitope-mapping protocol has been used in the determination of both continuous and discontinuous epitopes on both glycosylated and unglycosylated proteins.

Indexed as

Amino Acid SequenceAnimalsAntibodiesAntigensEpitope MappingHumansMolecular Sequence DataSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationAntibodiesAntigens

Identifiers

PMID11876299

What OpenQuestion holds

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Registered trials

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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.