Evidence map›Paper›PMID 30849700›Full record

ReviewCurrent opinion in biotechnology2019

Why recombinant antibodies - benefits and applications.

Koli Basu, Evan M Green, Yifan Cheng, Charles S Craik

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
6.1field-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

39 citing papers in PubMed, 81 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Precise and Stable Labeling of Quantum Dots with Engineered Antibodies.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  7. Article
  8. Antibody Reveals Conformational Latch Controlling Herpesvirus Proteases.bioRxiv : the preprint server for biology · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

4 authors at 2 institutions in 1 country.

Koli BasuDepartment of Pharmaceutical Chemistry, University of California, San Francisco, United States.
Evan M GreenDepartment of Biochemistry and Biophysics, University of California, San Francisco, United States.
Yifan ChengDepartment of Biochemistry and Biophysics, University of California, San Francisco, United States; Howard Hughes Medical Institute, University of California, San Francisco, United States.
Charles S CraikDepartment of Pharmaceutical Chemistry, University of California, San Francisco, United States.
University of California, San Francisco · USHoward Hughes Medical Institute · US

Funding

X-ray Screening and Rapid Structure DeterminationP50GM082250 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KROGAN, NEVAN J · 2007 to 2018
$48.8M
Structure, States and Transition in ABC Transporters pp360-431P01GM111126 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SALI, ANDREJ · 2015 to 2019
$9.8M
Renewable antibodies to secreted proteins and single and multi-pass cell surfaceP41CA196276 · NCI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MARKS, JAMES D. · 2014 to 2018
$5.8M
Howard Hughes Medical InstituteNCI NIH HHS P41 CA196276NIGMS NIH HHS P01 GM111126NIGMS NIH HHS P50 GM082250
6 · The paper itself

Abstract

Antibodies (Abs) are ubiquitous reagents for biological and biochemical research and are rapidly expanding into new therapeutic areas. They are one of the most important probes for determining how proteins function under normal and pathophysiological conditions. Abs are required for the quantification of targets, detection of temporal and spatial patterns of protein expression in cells and tissues, and identification of interacting partners and their biological activities. Their remarkable specificity and unique binding properties can facilitate three-dimensional structure determination using X-ray crystallography and electron cryomicroscopy. While hybridoma technology that involves animal immunization is often productive, many antigen targets do not generate useful Abs. This is particularly true if unique states of the target or critical non-immunogenic target sequences need to be recognized by the Abs. By using the methods of recombinant antibody generation, identification, and engineering, these 'hybridoma-refractory' antigens can be readily targeted. Specific, reproducible, and renewable recombinant Abs are proving to be invaluable reagents in applications ranging from biological discovery to structure determination of challenging macromolecules.

Indexed as

AnimalsAntibodiesImmunizationRecombinant ProteinsAntibodiesRecombinant Proteins

Identifiers

PMID30849700
PMCPMC6728236
OpenAlexW2947780489

What OpenQuestion holds

Textmetadata
LicenceTDM
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.