Evidence map›Paper›PMID 26651858›Full record

ArticlemAbs2016

Discovery and characterization of hydroxylysine in recombinant monoclonal antibodies.

Qing Xie, Benjamin Moore, Richard L Beardsley

Open access · goldAbstract read
In one paragraph

Article in mAbs, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.5field-weighted citation impact, top 33% 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

6 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. 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

3 authors at 1 institution in 1 country.

Qing Xie
Benjamin Moore
Richard L Beardsleya Protein Analytical Chemistry Department , Genentech, 1 DNA Way, 94080, South San Francisco , CA , USA.
Analytical Services · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tryptic peptide mapping analysis of a Chinese hamster ovary (CHO)-expressed, recombinant IgG1 monoclonal antibody revealed a previously unreported +16 Da modification. Through a combination of MS(n) experiments, and preparation and analysis of known synthetic peptides, the possibility of a sequence variant (Ala to Ser) was ruled out and the presence of hydroxylysine was confirmed. Post-translational hydroxylation of lysine was found in a consensus sequence (XKG) known to be the site of modification in other proteins such as collagen, and was therefore presumed to result from the activity of the CHO homolog of the lysyl hydroxylase complex. Although this consensus sequence was present in several locations in the antibody sequence, only a single site on the heavy-chain Fab was found to be modified.

Indexed as

AnimalsAntibodies, Monoclonal, HumanizedCHO CellsCricetinaeCricetulusHydroxylysineImmunoglobulin GRecombinant ProteinsAntibodies, Monoclonal, HumanizedHydroxylysineImmunoglobulin GRecombinant ProteinshydroxylationHydroxylysineLC-MSlysyl hydroxylasemass spectrometrypost-translational modificationrecombinant monoclonal antibody

Identifiers

PMID26651858
PMCPMC4966620
OpenAlexW2207646307

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.