Evidence map›Paper›PMID 28320404›Full record

ArticleMalaria journal2017

Tryptophan-rich domains of Plasmodium falciparum SURFIN

Xiaotong Zhu, Yang He, Yifan Liang, Osamu Kaneko, Liwang Cui, Yaming Cao

Open access · goldAbstract read
In one paragraph

Article in Malaria journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

8 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Host Cytoskeleton Remodeling throughout the Blood Stages of Plasmodium falciparum.Microbiology and molecular biology reviews : MMBR · 2019
    Review
  5. Article
  6. Article
  7. Article
  8. 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

6 authors at 4 institutions in 3 countries.

Xiaotong ZhuDepartment of Immunology, College of Basic Medical Science, China Medical University, Shenyang, 110122, Liaoning, China.
Yang HeDepartment of Immunology, College of Basic Medical Science, China Medical University, Shenyang, 110122, Liaoning, China.
Yifan Liang98K 73B Seven-year Programme 127306, China Medical University, Shenyang, 110001, Liaoning, China.
Osamu KanekoDepartment of Protozoology, Institute of Tropical Medicine (NEKKEN), Nagasaki University, 1-12-4 Sakamoto, Nagasaki, 852-8523, Japan.
Liwang CuiDepartment of Immunology, College of Basic Medical Science, China Medical University, Shenyang, 110122, Liaoning, China. luc2@psu.edu.
Yaming CaoDepartment of Immunology, College of Basic Medical Science, China Medical University, Shenyang, 110122, Liaoning, China. ymcao@mail.cmu.edu.cn.
China Medical University · CNNagasaki University · JPPennsylvania State University · USShenyang Medical College · CN

Funding

Southeast Asia Malaria Research CenterU19AI089672 · NIAID · UNIVERSITY OF SOUTH FLORIDA · PI CUI, LIWANG · 2010 to 2023
$28.9M
NIAID NIH HHS U19 AI089672
6 · The paper itself

Abstract

backgroundPlasmodium falciparum dramatically alters the morphology and properties of the infected red blood cells (iRBCs). A large group of exported proteins participate in these parasite-host interactions occurring at the iRBC membrane skeleton. SURFIN

methodsTwo transfected lines expressing recombinant SURFINs (NTC-GFP and NTC-4.2WRD2-GFP) of the 3D7 sequence were generated by transfection in P. falciparum. In vitro binding assays were performed by using recombinant WRDs of SURFIN

resultsThe recombinant SURFINs (NTC-4.2WRD2-GFP), in which the second WRD from SURFIN

conclusionsBecause PfEMP1 and Pf332 also bind to actin and/or spectrin, the authors propose that the interaction between WRD and RBC membrane skeleton might be a common feature of WRD-containing proteins and may be important for the translocation of these proteins from Maurer's clefts to the iRBC surface. The findings suggest a conserved mechanism of host-parasite interactions and targeting this interaction may disrupt the iRBC surface exposure of Plasmodium virulence-related proteins.

Indexed as

ErythrocytesHumansMembrane ProteinsPlasmodium falciparumPlasmodium vivaxProtozoan ProteinsTryptophanMembrane ProteinsProtozoan ProteinsSURFIN 4.2 protein, Plasmodium falciparumTryptophanF-actinRBC membrane skeletonSpectrinSURFINTryptophan-rich domain

Identifiers

PMID28320404
PMCPMC5359885
OpenAlexW2603529815

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.