Evidence map›Paper›PMID 27763506›Full record

ArticleToxins2016

Improvement of the Pharmacological Properties of Maize RIP by Cysteine-Specific PEGylation.

Ka-Yee Au, Wei-Wei Shi, Shuai Qian, Zhong Zuo, Pang-Chui Shaw

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Toxins, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 36% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Review
  2. 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.

Ka-Yee AuCentre for Protein Science and Crystallography, School of Life Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong, China. aaky73@yahoo.com.hk.
Wei-Wei ShiCentre for Protein Science and Crystallography, School of Life Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong, China. Shiww@cuhk.edu.hk.
Shuai QianSchool of Pharmacy, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong, China. silence_qs@163.com.
Zhong ZuoSchool of Pharmacy, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong, China. joanzuo@cuhk.edu.hk.
Pang-Chui ShawCentre for Protein Science and Crystallography, School of Life Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong, China. pcshaw@cuhk.edu.hk.
Chinese University of Hong Kong · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To improve the pharmacological properties of maize ribosome-inactivating protein (maize RIP) for targeting HIV-infected cells, the previously engineered TAT-fused active form of maize RIP (MOD) was further engineered for cysteine-directed PEGylation. In this work, two potential antigenic sites, namely Lys-78 and Lys-264, were identified. They were mutated to cysteine residue and conjugated with PEG

Indexed as

Zea maysAnimalsCell LineCysteineHalf-LifeHumansImmunoglobulin EImmunoglobulin GMice, Inbred C57BLMutationPlant ProteinsPolyethylene GlycolsRats, Sprague-DawleyRibosome Inactivating ProteinsCysteineImmunoglobulin EImmunoglobulin GPlant ProteinsPolyethylene GlycolsRibosome Inactivating Proteinsantibody inductionantigenicitycirculation half-lifeMODPEGylationpharmacokinetics study

Identifiers

PMID27763506
PMCPMC5086658
OpenAlexW2534132645

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.