Evidence map›Paper›PMID 9671778›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

A phage display approach for rapid antibody humanization: designed combinatorial V gene libraries.

C Rader, D A Cheresh, C F Barbas

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
6.8field-weighted citation impact, top 3% 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

22 citing papers in PubMed, 95 citations in OpenAlex.

  1. Universal Baseline forbioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. CAR T cells targeting αAdvances in cell and gene therapy · 2018
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Augmented Binary Substitution: Single-pass CDR germ-lining and stabilization of therapeutic antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  12. Article
  13. Article
  14. Conversion of scFv peptide-binding specificity for crystal chaperone development.Protein engineering, design & selection : PEDS · 2011
    Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Using antibody catalysis to study the outcome of multiple evolutionary trials of a chemical task.Proceedings of the National Academy of Sciences of the United States of America · 2000
    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.

C RaderSkaggs Institute for Chemical Biology and Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
D A Cheresh
C F Barbas
Scripps Research Institute · US

Funding

IN VITRO EVOLUTION OF HUMAN ANTIHIV ANTIBODIESR01AI037470 · NIAID · SCRIPPS RESEARCH INSTITUTE · PI BARBAS, CARLOS F · 1995 to 2002
$1.1M
CHEMOKINE RECEPTOR ANTAGONISTS FOR HIV1 THERAPYR01AI041944 · NIAID · SCRIPPS RESEARCH INSTITUTE · PI BARBAS, CARLOS F · 1997 to 2000
$375k
NIAID NIH HHS AI 37470NIAID NIH HHS AI 41944
6 · The paper itself

Abstract

The development of a new strategy for antibody humanization is described. This strategy incorporates key recognition sequences from the parental rodent antibody into a phage display-based selection strategy. The original sequences of the third complementarity-determining regions (CDRs) of heavy and light chains, HCDR3 and LCDR3, were maintained and all other sequences were replaced by human sequences selected from phage-displayed antibody libraries. This approach was applied to the humanization of mouse mAb LM609 that is directed to human integrin alphav beta3 and has potential applicability in cancer therapy as an antiangiogenic agent. We demonstrate this approach (i) provides a rapid route for antibody humanization constraining the content of original mouse sequences in the final antibodies to the most hypervariable of the CDRs; (ii) generates several humanized versions with different sequences at the same time; (iii) results in affinities as high as or higher than the affinity of the original antibody; and (iv) retains the antigen and epitope specificity of the original antibody. The production of multiple humanized variants may present advantages in the selection of antibodies that are more readily expressed on a large scale and could be important in therapeutic regimens that call for long-term treatment with antibodies in which antiidiotypic responses might be avoided by administration of alternative antibodies.

Indexed as

Gene LibraryAmino Acid SequenceAnimalsAntibodiesBase SequenceBinding Sites, AntibodyCell LineCloning, MolecularDNA, ComplementaryDNA PrimersHumansImmunoglobulin Variable RegionMiceMolecular Sequence DataSequence Homology, Amino AcidAntibodiesDNA, ComplementaryDNA PrimersImmunoglobulin Variable Region

Identifiers

PMID9671778
PMCPMC21176
OpenAlexW2056110137

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.