Evidence map›Paper›PMID 18695987›Full record

ArticleGlycoconjugate journal2009

Systematic synthesis and inhibitory activity of haloacetamidyl oligosaccharide derivatives toward cytoplasmic peptide:N-glycanase.

Ayako Miyazaki, Ichiro Matsuo, Shinya Hagihara, Ayako Kakegawa, Tadashi Suzuki, Yukishige Ito

Abstract read
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In one paragraph

Article in Glycoconjugate journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

4 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
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  4. 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

6 authors at 3 institutions in 2 countries.

Ayako MiyazakiThe Institute of Physical and Chemical Research, Wako, Saitama, Japan.
Ichiro Matsuo
Shinya Hagihara
Ayako Kakegawa
Tadashi Suzuki
Yukishige Ito
RIKEN · JPJapan Science and Technology Agency · JPSaitama University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A series of glycosyl haloacetamides were synthesized as potential inhibitors of cytoplasmic peptide:N-glycanase (PNGase), an enzyme that removes N-glycans from misfolded glycoproteins. Chloro-, bromo-, and iodoacetamidyl chitobiose and chitotetraose derivatives exhibited a significant inhibitory activity. No inhibitory activity was observed with of fluoroacetamididyl derivatives. Moreover, N-acetylglucosamine derivatives, beta-chloropropionamidyl chitobiose, and chloroacetamidyl cellooligosaccharide derivatives did not show any activity. These results underscore the importance of the N-acetyl groups of chitobiose for PNGase recognition. In addition, reactivity and position of the leaving group at the reducing end are also important factors.

Indexed as

AcetamidesCytoplasmDisaccharidesEnzyme InhibitorsModels, MolecularOligosaccharidesPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidasePeptidesAcetamideschitobioseDisaccharidesEnzyme InhibitorsOligosaccharidesPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidasePeptides

Identifiers

PMID18695987
OpenAlexW1978504078

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.