Evidence map›Paper›PMID 8524873›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

Expression studies of catalytic antibodies.

H D Ulrich, P A Patten, P L Yang, F E Romesberg, P G Schultz

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
5.3field-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

15 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
  2. Article
  3. Protein dynamics and the diversity of an antibody response.The Journal of biological chemistry · 2012
    Article
  4. Article
  5. An aspartate and a water molecule mediate efficient acid-base catalysis in a tailored antibody pocket.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  6. Article
  7. Article
  8. Antibody evolution constrains conformational heterogeneity by tailoring protein dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  9. Protein dynamics and the immunological evolution of molecular recognition.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  10. Molecular mechanism of enantioselective proton transfer to carbon in catalytic antibody 14D9.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  11. Structural evidence for substrate strain in antibody catalysis.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  12. Flexibility and molecular recognition in the immune system.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  13. A phage display approach for rapid antibody humanization: designed combinatorial V gene libraries.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  14. Phage display of a catalytic antibody to optimize affinity for transition-state analog binding.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
  15. Insights into antibody catalysis: structure of an oxygenation catalyst at 1.9-angstrom resolution.Proceedings of the National Academy of Sciences of the United States of America · 1996
    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

5 authors at 1 institution in 1 country.

H D UlrichHoward Hughes Medical Institute, Department of Chemistry, University of California, Berkeley 94720, USA.
P A Patten
P L Yang
F E Romesberg
P G Schultz
Howard Hughes Medical Institute · US

Funding

PROBING THE STRUCTURE AND FUNCTION OF THE HIV 1 PROTEASEF32AI009136 · NIAID · UNIVERSITY OF CALIFORNIA BERKELEY · PI ROMESBERG, FLOYD E · 1994 to 1997
–
NIAID NIH HHS F32AI09136
6 · The paper itself

Abstract

We have examined the positive influence of human constant regions on the folding and bacterial expression of active soluble mouse immunoglobulin variable domains derived from a number of catalytic antibodies. Expression yields of eight hybridoma- and myeloma-derived chimeric Fab fragments are compared in both shake flasks and high density fermentations. In addition the usefulness of this system for the generation of in vivo expression libraries is examined by constructing and expressing combinations of heavy and light chain variable regions that were not selected as a pair during an immune response. A mutagenesis study of one of the recombinant catalytic Fab fragments reveals that single amino acid substitutions can have dramatic effects on the expression yield. This system should be generally applicable to the production of Fab fragments of catalytic and other hybridoma-derived antibodies for crystallographic and structure-function studies.

Indexed as

Amino Acid SequenceAnimalsAntibodies, CatalyticBase SequenceCloning, MolecularEscherichia coliGenes, ImmunoglobulinGenetic VectorsHumansHybridomasImmunoglobulin Fab FragmentsImmunoglobulin Heavy ChainsImmunoglobulin Light ChainsMiceMolecular Sequence DataPoint MutationAntibodies, CatalyticImmunoglobulin Fab FragmentsImmunoglobulin Heavy ChainsImmunoglobulin Light ChainsRecombinant Fusion ProteinsRecombinant Proteins

Identifiers

PMID8524873
PMCPMC40512
OpenAlexW2059568862

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.