Evidence map›Paper›PMID 24100038›Full record

ArticleThe Journal of biological chemistry2013

The inhibitory effects of a rhamnogalacturonan I (RG-I) domain from ginseng pectin on galectin-3 and its structure-activity relationship.

Xiaoge Gao, Yuan Zhi, Lin Sun, Xiaoxia Peng, Tao Zhang, Huiting Xue, Guihua Tai, Yifa Zhou

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed, 1 pooled it
2.8field-weighted citation impact, top 10% 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

43 citing papers in PubMed, 1 synthesis or guideline pooled it, 158 citations in OpenAlex.

  1. Pooled it
  2. International journal of molecular sciences · 2026
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  18. An Overview of Antitumour Activity of Polysaccharides.Molecules (Basel, Switzerland) · 2022
    Review
  19. Article
  20. 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

8 authors at 1 institution in 1 country.

Xiaoge GaoSchool of Life Sciences, Northeast Normal University, Changchun 130024, China.
Yuan ZhiSchool of Life Sciences, Northeast Normal University, Changchun 130024, China.
Lin SunSchool of Life Sciences, Northeast Normal University, Changchun 130024, China.
Xiaoxia PengSchool of Life Sciences, Northeast Normal University, Changchun 130024, China.
Tao ZhangSchool of Life Sciences, Northeast Normal University, Changchun 130024, China.
Huiting XueSchool of Life Sciences, Northeast Normal University, Changchun 130024, China.
Guihua TaiSchool of Life Sciences, Northeast Normal University, Changchun 130024, China. Electronic address: taigh477@nenu.edu.cn.
Yifa ZhouSchool of Life Sciences, Northeast Normal University, Changchun 130024, China. Electronic address: zhouyf383@nenu.edu.cn.
Northeast Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pectin has been shown to inhibit the actions of galectin-3, a β-galactoside-binding protein associated with cancer progression. The structural features of pectin involved in this activity remain unclear. We investigated the effects of different ginseng pectins on galectin-3 action. The rhamnogalacturonan I-rich pectin fragment, RG-I-4, potently inhibited galectin-3-mediated hemagglutination, cancer cell adhesion and homotypic aggregation, and binding of galectin-3 to T-cells. RG-I-4 specifically bound to the carbohydrate recognition domain of galectin-3 with a dissociation constant of 22.2 nm, which was determined by surface plasmon resonance analysis. The structure-activity relationship of RG-I-4 was investigated by modifying the structure through various enzymatic and chemical methods followed by activity tests. The results showed that (a) galactan side chains were essential to the activity of RG-I-4, whereas arabinan side chains positively or negatively regulated the activity depending on their location within the RG-I-4 molecule. (b) The activity of galactan chain was proportional to its length up to 4 Gal residues and largely unchanged thereafter. (c) The majority of galactan side chains in RG-I-4 were short with low activities. (d) The high activity of RG-I-4 resulted from the cooperative action of these side chains. (e) The backbone of the molecule was very important to RG-I-4 activity, possibly by maintaining a structural conformation of the whole molecule. (f) The isolated backbone could bind galectin-3, which was insensitive to lactose treatment. The novel discovery that the side chains and backbone play distinct roles in regulating RG-I-4 activity is valuable for producing highly active pectin-based galectin-3 inhibitors.

Indexed as

PectinsBlood ProteinsCarbohydrate ConformationCell AdhesionGalectin 3GalectinsHumansJurkat CellsNeoplasm ProteinsNeoplasmsPanaxStructure-Activity RelationshipBlood ProteinsGalectin 3GalectinsLGALS3 protein, humanNeoplasm ProteinsPectinsrhamnogalacturonan ICarbohydrate-binding ProteinCarbohydrate StructureGalectinGalectin-3 InhibitorsGinseng PectinOligosaccharidePolysaccharideRhamnogalacturonan IStructure-Activity Relationship

Identifiers

PMID24100038
PMCPMC3837135
OpenAlexW1967913284

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.