Evidence map›Paper›PMID 35528656›Full record

ArticleRSC advances2019

Interaction of carbohydrate binding module 20 with starch substrates.

Son Tung Ngo, Phuong Duy Tran-Le, Giap T Ho, Loan Q Le, Le Minh Bui, Bao Khanh Vu, Huong Thi Thu Phung, Hoang-Dung Nguyen, Thanh-Sang Vo, Van V Vu

Open access · goldAbstract read
In one paragraph

Article in RSC advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed, 23 citations in OpenAlex.

  1. Biochemical and structural characterization of AmyY fromApplied and environmental microbiology · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Novel Design of an α-Amylase with an N-Terminal CBM20 inMolecules (Basel, Switzerland) · 2023
    Article
  8. Article
  9. 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

10 authors at 3 institutions in 2 countries.

Son Tung NgoLaboratory of Theoretical and Computational Biophysics, Ton Duc Thang University Ho Chi Minh City Vietnam ngosontung@tdtu.edu.vn.ORCID https://orcid.org/0000-0003-1034-1768
Phuong Duy Tran-LeNTT Hi-Tech Institute, Nguyen Tat Thanh University Ho Chi Minh City Vietnam vanvu@ntt.edu.vn.
Giap T HoNTT Hi-Tech Institute, Nguyen Tat Thanh University Ho Chi Minh City Vietnam vanvu@ntt.edu.vn.
Loan Q LeInstitute of Tropical Biology, Vietnam Academy of Science and Technology Ho Chi Minh City Vietnam.ORCID https://orcid.org/0000-0003-2376-5164
Le Minh BuiNTT Hi-Tech Institute, Nguyen Tat Thanh University Ho Chi Minh City Vietnam vanvu@ntt.edu.vn.
Bao Khanh VuNTT Hi-Tech Institute, Nguyen Tat Thanh University Ho Chi Minh City Vietnam vanvu@ntt.edu.vn.
Huong Thi Thu PhungNTT Hi-Tech Institute, Nguyen Tat Thanh University Ho Chi Minh City Vietnam vanvu@ntt.edu.vn.
Hoang-Dung NguyenNTT Hi-Tech Institute, Nguyen Tat Thanh University Ho Chi Minh City Vietnam vanvu@ntt.edu.vn.
Thanh-Sang VoNTT Hi-Tech Institute, Nguyen Tat Thanh University Ho Chi Minh City Vietnam vanvu@ntt.edu.vn.ORCID https://orcid.org/0000-0002-6726-3257
Van V VuNTT Hi-Tech Institute, Nguyen Tat Thanh University Ho Chi Minh City Vietnam vanvu@ntt.edu.vn.ORCID https://orcid.org/0000-0003-0009-6703
Trường ĐH Nguyễn Tất Thành · VNTon Duc Thang University · VNVietnam Academy of Science and Technology · VN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

CBM20s are starch-binding domains found in many amylolytic enzymes, including glucoamylase, alpha-amylase, beta-amylases, and a new family of starch-active polysaccharide monooxygenases (AA13 PMOs). Previous studies of CBM20-substrate interaction only concerned relatively small or soluble amylose molecules, while amylolytic enzymes often work on extended chains of insoluble starch molecules. In this study, we utilized molecular simulation techniques to gain further insights into the interaction of CBM20 with substrates of various sizes

Identifiers

PMID35528656
PMCPMC9069913
OpenAlexW2967443278

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.