Evidence map›Paper›PMID 30141104›Full record

ArticleMolecular biology reports2018

Identification and analysis of dominant negative mutants of RIP1 DD that disrupt RIPoptosome core formation.

Hyun Ji Ha, Hyun Ho Park

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular biology reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 92% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. 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

2 authors at 1 institution in 1 country.

Hyun Ji HaCollege of Pharmacy, Chung-Ang University, Seoul, 06974, South Korea.
Hyun Ho ParkCollege of Pharmacy, Chung-Ang University, Seoul, 06974, South Korea. xrayleox@cau.ac.kr.
Chung-Ang University · KR

Funding

the Basic Science Research Program through the National Research Foundation (NRF) of Ministry of Education, Science and Technology NRF-2017M3A9D8062960the Korea Healthcare Technology R&D project, Ministry of Health & Welfare HI17C0155
6 · The paper itself

Abstract

The RIPoptosome, composed of RIP1 and caspase-8, plays an important role in the regulation of apoptosis and necroptosis; however, the mechanism of complex formation by oligomerization and how the caspase-activating process and necroptosis are mediated by the formation of the RIPoptosome is not well-understood. This study revealed that the assembly mechanism of the RIPoptosome core is dependent on salt concentration and not on pH and time. In addition, we demonstrated that three RIP1 mutations, E626K, M637K, and S657K, have dominant negative effects. These dominant negative mutations in RIP1 may have potential applications in therapeutic intervention.

Indexed as

ApoptosisCaspase 8Cloning, MolecularDeath DomainFas-Associated Death Domain ProteinGenes, DominantHumansHydrogen-Ion ConcentrationInhibitor of Apoptosis ProteinsNecrosisReceptor-Interacting Protein Serine-Threonine KinasesRNA-Binding ProteinsSaltsSignal TransductionCaspase 8FADD protein, humanFas-Associated Death Domain ProteinInhibitor of Apoptosis ProteinsReceptor-Interacting Protein Serine-Threonine KinasesRNA-Binding ProteinsSaltsDominant negative mutantFADDNecroptosisRIP1RIPoptosome

Identifiers

PMID30141104
OpenAlexW2888734538

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.