Evidence map›Paper›PMID 20195383›Full record

ArticleAging2009

Oxidative modification and aggregation of creatine kinase from aged mouse skeletal muscle.

Jonathan E Nuss, James K Amaning, C Eric Bailey, James H DeFord, Vincent L Dimayuga, Jeffrey P Rabek, John Papaconstantinou

Open access · hybridAbstract read
In one paragraph

Article in Aging, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

29 citing papers in PubMed, 52 citations in OpenAlex.

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  19. Oxidative stress in aging: advances in proteomic approaches.Oxidative medicine and cellular longevity · 2014
    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

7 authors at 1 institution in 1 country.

Jonathan E NussDepartment of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555-0643, USA.
James K Amaning
C Eric Bailey
James H DeFord
Vincent L Dimayuga
Jeffrey P Rabek
John Papaconstantinou
The University of Texas Medical Branch at Galveston · US

Funding

UTMB OAIC Research Education Component (REC)P30AG024832 · NIA · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI JAMES S. GOODWIN, MD, MELISSA M. MORROW · 2005 to 2026
$26.7M
UPPER EXTREMITY TRAINING FOR CHRONIC STROKEP60AG012583 · NIA · UNIVERSITY OF MARYLAND BALTIMORE · PI GOLDBERG, ANDREW P · 1994 to 2005
$7.8M
OXIDATIVE STRESS,REPAIR OF OXIDIZED GUANINES IN AGED CELLSP01AG021830 · NIA · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI PAPACONSTANTINOU, JOHN NMN · 2004 to 2010
$6.4M
NIA NIH HHS 1P01 AG021830NIA NIH HHS P01 AG021830NIA NIH HHS P30 AG024832NIA NIH HHS P60 AG012583PHS HHS NIEHS T32-07254PHS HHS P60AAG12583
6 · The paper itself

Abstract

Creatine kinase catalyzes the reversible transfer of the gamma phosphate from ATP to creatine forming the high energy compound creatine phosphate. Muscle creatine kinase (CKm) activity maintains energetic homeostasis as variations in energy requirements dictate that ATP be readily available. Recent studies suggest that CKm activity is altered during aging. Proteomic analyses have shown that CKm is 3-nitrotyrosine (3-NT) modified and carbonylated in aged rodent skeletal muscle. However, it remains unknown if these modifications affect its structure and activity. To address this we characterized oxidatively modified CKm from the quadriceps of young, middle-aged, and aged mice. Our data indicate that 3-NT modified and carbonylated CKm are found predominantly in aged muscle and that it exists in high molecular weight oligomers and insoluble protein aggregates. CKm from middle-aged and aged mouse quadriceps also exhibits structural instability that may account for its reduction in function. These structural and functional changes correlate with the differential protein modifications. Interestingly, the majority of the age-related changes in enzyme activity and protein stability occurred by middle age. Our studies indicate that the age-associated oxidative and nitrative modification of CKm results in a decrease in its activity and may cause structural changes that promote oligomerization and aggregation.

Indexed as

AgingAnimalsCreatine KinaseGlycogen PhosphorylaseKineticsMaleMiceMice, Inbred C57BLMuscle, SkeletalOxidative StressProtein CarbonylationTyrosine3-nitrotyrosineCreatine KinaseGlycogen PhosphorylaseTyrosine3-nitrotyrosineagingcarbonylationCreatine kinasecreatine kinase kineticscreatine kinase structureskeletal muscle

Identifiers

PMID20195383
PMCPMC2830079
OpenAlexW2157796703

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.