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Novel protein–protein interactions of TPPII, p53, and SIRT7

Overview of attention for article published in Molecular and Cellular Biochemistry, July 2015
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  • Good Attention Score compared to outputs of the same age (73rd percentile)
  • High Attention Score compared to outputs of the same age and source (92nd percentile)

Mentioned by

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1 blog

Citations

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24 Mendeley
Title
Novel protein–protein interactions of TPPII, p53, and SIRT7
Published in
Molecular and Cellular Biochemistry, July 2015
DOI 10.1007/s11010-015-2507-y
Pubmed ID
Authors

Jarmila Nahálková

Abstract

Novel protein-protein interactions of TPPII, SIRT7, and p53 were detected by co-immunoprecipitation using both HeLa cell lysates and the cytoplasmic fraction prepared by fractionation of mouse liver tissue. The interactions were further verified in vivo by in situ proximity ligation assay (PLA) within control HEK293 cells transformed with empty vector, highactTPPII HEK293 cells over-expressing murine TPPII displaying high specific enzymatic activity and in lowactTPPII HEK293 cells over-expressing human TPPII having low specific activity of the enzyme. Besides an abundant cytoplasmic localization of TPPII-p53 interaction signal, the nuclear interactions were also demonstrated. The cytoplasmic interactions were likewise detected between TPPII and SIRT7 in control HEK293 and lowactTPPII HEK293 cells. The interactions of SIRT7 with p53 were confirmed in three HEK293 cell transformants as well. The cytoplasmic occurrence of SIRT7 protein was demonstrated by immunofluorescence, when both nucleolar and cytoplasmic signals were identified within HEK293 cells and primary human fibroblasts. The unique cytoplasmic localization of SIRT7 protein was discussed based on an epitope specificity of N-terminus specific SIRT7 antibodies utilized in the present study compared with C-terminus specific antibodies previously used for nuclear detection of SIRT7 by other authors. The epitope sequence of N-terminal antibodies is occurring in all three splicing variants of SIRT7 compared to the epitope of C-terminal antibody, which is specific exclusively to the splicing variant 1. The cytoplasmic localization of p53 detected by immunofluorescence supported the results from its interactions with TPPII and SIRT7 observed by in situ PLA within model cells. Novel interactions of TPPII, p53, and SIRT7 presented in this study might contribute to the knowledge of the regulatory effects of these proteins on apoptotic pathways and to the understanding mechanisms of aging and lifespan regulation.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 24 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 24 100%

Demographic breakdown

Readers by professional status Count As %
Student > Bachelor 6 25%
Researcher 3 13%
Student > Master 3 13%
Student > Ph. D. Student 2 8%
Other 1 4%
Other 4 17%
Unknown 5 21%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 6 25%
Agricultural and Biological Sciences 3 13%
Psychology 2 8%
Environmental Science 1 4%
Nursing and Health Professions 1 4%
Other 6 25%
Unknown 5 21%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 5. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 05 October 2015.
All research outputs
#5,891,195
of 22,829,683 outputs
Outputs from Molecular and Cellular Biochemistry
#315
of 2,304 outputs
Outputs of similar age
#67,376
of 262,637 outputs
Outputs of similar age from Molecular and Cellular Biochemistry
#3
of 41 outputs
Altmetric has tracked 22,829,683 research outputs across all sources so far. This one has received more attention than most of these and is in the 73rd percentile.
So far Altmetric has tracked 2,304 research outputs from this source. They receive a mean Attention Score of 3.9. This one has done well, scoring higher than 86% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 262,637 tracked outputs that were published within six weeks on either side of this one in any source. This one has gotten more attention than average, scoring higher than 73% of its contemporaries.
We're also able to compare this research output to 41 others from the same source and published within six weeks on either side of this one. This one has done particularly well, scoring higher than 92% of its contemporaries.