Evidence map›Paper›PMID 31739603›Full record

ReviewInternational journal of molecular sciences2019

The Hypervariable Region of K-Ras4B Governs Molecular Recognition and Function.

Hazem Abdelkarim, Avik Banerjee, Patrick Grudzien, Nicholas Leschinsky, Mahmoud Abushaer, Vadim Gaponenko

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 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
1.1field-weighted citation impact, top 22% 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, 19 citations in OpenAlex.

  1. Review
  2. Review
  3. Structural modifications and kinetic effects ofFrontiers in molecular biosciences · 2024
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. 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 1 institution in 1 country.

Hazem AbdelkarimDepartment of Biochemistry and Molecular Genetics, College of Medicine, University of Illinois at Chicago (UIC), Chicago, IL 60607, USA.
Avik BanerjeeDepartment of Chemistry, University of Illinois at Chicago (UIC), Chicago, IL 60612, USA.
Patrick GrudzienDepartment of Biochemistry and Molecular Genetics, College of Medicine, University of Illinois at Chicago (UIC), Chicago, IL 60607, USA.
Nicholas LeschinskyDepartment of Biochemistry and Molecular Genetics, College of Medicine, University of Illinois at Chicago (UIC), Chicago, IL 60607, USA.
Mahmoud AbushaerDepartment of Biochemistry and Molecular Genetics, College of Medicine, University of Illinois at Chicago (UIC), Chicago, IL 60607, USA.
Vadim GaponenkoDepartment of Biochemistry and Molecular Genetics, College of Medicine, University of Illinois at Chicago (UIC), Chicago, IL 60607, USA.
University of Illinois Chicago · US

Funding

Regulation of tyrosine kinase signaling through interaction with membrane lipidsR01CA188427 · NCI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI GAPONENKO, VADIM V, TYNER, ANGELA L · 2015 to 2019
$2.1M
American Cancer Society 132722-PF-18-196-01-DMCNCI NIH HHS R01CA188427U.S. Department of Defense W81XWH- 38817-10509
6 · The paper itself

Abstract

The flexible C-terminal hypervariable region distinguishes K-Ras4B, an important proto-oncogenic GTPase, from other Ras GTPases. This unique lysine-rich portion of the protein harbors sites for post-translational modification, including cysteine prenylation, carboxymethylation, phosphorylation, and likely many others. The functions of the hypervariable region are diverse, ranging from anchoring K-Ras4B at the plasma membrane to sampling potentially auto-inhibitory binding sites in its GTPase domain and participating in isoform-specific protein-protein interactions and signaling. Despite much research, there are still many questions about the hypervariable region of K-Ras4B. For example, mechanistic details of its interaction with plasma membrane lipids and with the GTPase domain require further clarification. The roles of the hypervariable region in K-Ras4B-specific protein-protein interactions and signaling are incompletely defined. It is also unclear why post-translational modifications frequently found in protein polylysine domains, such as acetylation, glycation, and carbamoylation, have not been observed in K-Ras4B. Expanding knowledge of the hypervariable region will likely drive the development of novel highly-efficient and selective inhibitors of K-Ras4B that are urgently needed by cancer patients.

Indexed as

Genetic VariationAmino Acid SequenceAnimalsCell MembraneHumansProtein BindingProtein Interaction Domains and MotifsProtein IsoformsProtein Processing, Post-TranslationalProto-Oncogene Proteins p21(ras)Signal TransductionStructure-Activity RelationshipKRAS protein, humanProtein IsoformsProto-Oncogene Proteins p21(ras)autoinhibitionGTPaseshypervariable regionK-Ras4Bmembrane binding motifsposttranslational modificationsprotein–protein interactions

Identifiers

PMID31739603
PMCPMC6888304
OpenAlexW2983417838

What OpenQuestion holds

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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.