Evidence map›Paper›PMID 30586935›Full record

ArticleMolecules (Basel, Switzerland)2018

Site-Directed Mutagenesis of a β-Glycoside Hydrolase from

Jing-Jing Chen, Xiao Liang, Tian-Jiao Chen, Jin-Ling Yang, Ping Zhu

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

3 citing papers in PubMed, 11 citations in OpenAlex.

  1. Review
  2. Article
  3. 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.

Jing-Jing ChenState Key Laboratory of Bioactive Substance and Function of Natural Medicines & NHC Key Laboratory of Biosynthesis of Natural Products, Institute of Materia Medica, Chinese Academy of Medical Sciences & Peking Union Medical College, 1 Xian Nong Tan Street, Beijing 100050, China. chenjingjing@imm.ac.cn.
Xiao LiangState Key Laboratory of Bioactive Substance and Function of Natural Medicines & NHC Key Laboratory of Biosynthesis of Natural Products, Institute of Materia Medica, Chinese Academy of Medical Sciences & Peking Union Medical College, 1 Xian Nong Tan Street, Beijing 100050, China. liangxiao@imm.ac.cn.
Tian-Jiao ChenState Key Laboratory of Bioactive Substance and Function of Natural Medicines & NHC Key Laboratory of Biosynthesis of Natural Products, Institute of Materia Medica, Chinese Academy of Medical Sciences & Peking Union Medical College, 1 Xian Nong Tan Street, Beijing 100050, China. chentianjiao@imm.ac.cn.
Jin-Ling YangState Key Laboratory of Bioactive Substance and Function of Natural Medicines & NHC Key Laboratory of Biosynthesis of Natural Products, Institute of Materia Medica, Chinese Academy of Medical Sciences & Peking Union Medical College, 1 Xian Nong Tan Street, Beijing 100050, China. yangjl@imm.ac.cn.
Ping ZhuState Key Laboratory of Bioactive Substance and Function of Natural Medicines & NHC Key Laboratory of Biosynthesis of Natural Products, Institute of Materia Medica, Chinese Academy of Medical Sciences & Peking Union Medical College, 1 Xian Nong Tan Street, Beijing 100050, China. zhuping@imm.ac.cn.ORCID 0000-0001-8537-2169
Chinese Academy of Medical Sciences & Peking Union Medical College · CN

Funding

CAMS Innovation Fund for Medical Sciences CIFMS-2017-I2M-2-004Fundamental Research Funds for the Central Universities 2017PT35001National Mega-project for Innovative Drugs 2018ZX09711001-006-001National Natural Science Foundation of China 81573325
6 · The paper itself

Abstract

The β-glycoside hydrolases (LXYL-P1-1 and LXYL-P1-2) from

Indexed as

Mutagenesis, Site-DirectedBiomassGlycoside HydrolasesKineticsMolecular Docking SimulationMutationRecombination, GeneticSaccharomyces cerevisiaeShiitake MushroomsSubstrate SpecificityTaxoidsXylosidases7-xylosyl-10-deacetyltaxolGlycoside HydrolasesTaxoidsXylosidasescatalytic efficiencymolecular dockingsite-directed mutagenesisβ-glucosidaseβ-xylosidase

Identifiers

PMID30586935
PMCPMC6337304
OpenAlexW2906485238

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.