Evidence map›Paper›PMID 29199510›Full record

ReviewSmall GTPases2020

Regulation of RhoA GTPase and novel target proteins for ROCK.

Eun-Kyoung Choi, Jae-Gyu Kim, Hee-Jun Kim, Jung-Yoon Cho, Hwalrim Jeong, Yohan Park, Rokibul Islam, Cuong Kim Cap, Jae-Bong Park

Open access · bronzeAbstract readReview
In one paragraph

Review in Small GTPases, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

23 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Genes · 2024
    Article
  6. Article
  7. Augmentation of functional recovery viaJournal of orthopaedic translation · 2024
    Article
  8. Exercise Attenuate Diaphragm Atrophy in COPD Mice via Inhibiting the RhoA/ROCK Signaling.International journal of chronic obstructive pulmonary disease · 2024
    Article
  9. Article
  10. A low androgen state impairs erectile function by suppressingTranslational andrology and urology · 2023
    Article
  11. Article
  12. The Dual Function of RhoGDI2 in Immunity and Cancer.International journal of molecular sciences · 2023
    Review
  13. Review
  14. Cellular Conditions Responsible for Methylmercury-Mediated Neurotoxicity.International journal of molecular sciences · 2022
    Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Review
  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

9 authors at 1 institution in 1 country.

Eun-Kyoung ChoiIlsong Institute of Life Science, Hallym University, Ahnyang, Gyeonggi-do, South Korea.
Jae-Gyu KimDepartment of Biochemistry, College of Medicine, Hallym University, Chuncheon, Kangwon-do, Republic of Korea.
Hee-Jun KimIlsong Institute of Life Science, Hallym University, Ahnyang, Gyeonggi-do, South Korea.
Jung-Yoon ChoDepartment of Biochemistry, College of Medicine, Hallym University, Chuncheon, Kangwon-do, Republic of Korea.
Hwalrim JeongDepartment of Paediatrics, Chuncheon Sacred Hospital, Hallym University, Chuncheon, Kangwon-do, Republic of Korea.
Yohan ParkDepartment of Biochemistry, College of Medicine, Hallym University, Chuncheon, Kangwon-do, Republic of Korea.
Rokibul IslamDepartment of Biochemistry, College of Medicine, Hallym University, Chuncheon, Kangwon-do, Republic of Korea.
Cuong Kim CapDepartment of Biochemistry, College of Medicine, Hallym University, Chuncheon, Kangwon-do, Republic of Korea.
Jae-Bong ParkDepartment of Biochemistry, College of Medicine, Hallym University, Chuncheon, Kangwon-do, Republic of Korea.
Hallym University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rho GTPases play significant roles in cellular function and their activity is regulated by guanine nucleotide exchange factors (GEFs) and GTPase activating proteins (GAPs), providing activation and inactivation of these GTPases, respectively. Active GTP-bound form of RhoA activates its effector proteins while the inactive GDP-bound form of RhoA exists in a RhoA-RhoGDI (guanine nucleotide dissociation inhibitor) complex in the cytosol. In particular, IκB kinase γ IKKγ/NF-κB essential modulator (NEMO) plays a role as a GDI displacement factor (GDF) for RhoA activation through binding to RhoA-RhoGDI complex. Meanwhile, prion protein inactivates RhoA despite RhoA/RhoGDI association. Novel target proteins for Rho-associated kinase (ROCK) such as glycogen synthase kinase (GSK)-3β and IKKβ are recently discovered. Here, we elaborate on a post-translationally modified version of RhoA, phosphorylated at Tyr42 and oxidized at Cys16/20. This form of RhoA dissociates from RhoA-RhoGDI complex and activates IKKβ on IKKγ/NEMO, thus providing possibly a critical role for tumourigenesis.

Indexed as

AnimalsHumansrhoA GTP-Binding Proteinrho-Associated KinasesrhoA GTP-Binding Proteinrho-Associated KinasescancerGDFpost-translational modificationprionRhoARhoGDIROCK

Identifiers

PMID29199510
PMCPMC7053945
OpenAlexW2772801538

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.