Evidence map›Paper›PMID 22708568›Full record

ReviewEssays in biochemistry2012

Lysine post-translational modifications and the cytoskeleton.

Wendy D Zencheck, Hui Xiao, Louis M Weiss

Abstract readReview
In one paragraph

Review in Essays in biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. A secreted sirtuin fromScience advances · 2023
    Article
  3. Article
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  5. The cardioprotective role of sirtuins is mediated in part by regulating KAmerican journal of physiology. Cell physiology · 2023
    Article
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  8. Review
  9. Article
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  15. Review
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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

3 authors at 1 institution in 1 country.

Wendy D ZencheckDepartment of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, U.S.A.
Hui Xiao
Louis M Weiss
Albert Einstein College of Medicine · US

Funding

New Opportunistic Infections in AIDS MicrosporidosisR01AI031788 · NIAID · YESHIVA UNIVERSITY · PI WEISS, LOUIS M. · 1992 to 2011
$4.6M
Toxoplasma encephalitis in AIDS:Bradyzoite RegulationsR01AI039454 · NIAID · YESHIVA UNIVERSITY · PI WEISS, LOUIS M. · 1996 to 2009
$3.1M
Toxoplasma gondii: cyst wallR01AI095094 · NIAID · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI WEISS, LOUIS M. · 2012 to 2016
$2.1M
NIAID NIH HHS AI31788NIAID NIH HHS AI39454NIAID NIH HHS R01 AI031788NIAID NIH HHS R01 AI039454NIAID NIH HHS R01 AI095094
6 · The paper itself

Abstract

PTMs (post-translational modifications) of lysine residues have proven to be major regulators of gene expression, protein-protein interactions, and protein processing and degradation. This is of particular importance in regulating the cytoskeleton, an enormously complex system of proteins responsible for cell motility, intracellular trafficking, and maintenance of cell form and structure. The cytoskeleton is present in all cells, including eukaryotes and prokaryotes, and comprises structures such as flagella, cilia and lamellipodia which play critical roles in intracellular transport and cellular division. Cytoskeletal regulation relies on numerous multi-component assemblies. In this chapter, we focus on the regulation of the cytoskeleton by means of PTMs of lysine residues on the cytoskeletal subunits and their accessory proteins. We specifically address the three main classes of cytoskeletal proteins in eukaryotes that polymerize into filaments, including microfilaments (actin filaments), intermediate filaments and microtubules. We discuss the identification and biological importance of lysine acetylation, a regulator of all three filament types. We also review additional lysine modifications, such as ubiquitination and SUMOylation, and their role in protein regulation and processing.

Indexed as

Actin CytoskeletonAnimalsCytoskeletonHumansLysineProtein Processing, Post-TranslationalSumoylationUbiquitinationLysine

Identifiers

PMID22708568
PMCPMC3703749
OpenAlexW2020186556

What OpenQuestion holds

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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.