P100, a transcriptional coactivator, is a human homologue of staphylococcal nuclease

Ponting, Chris P.

doi:10.1002/pro.5560060224

Cited by 45 publications

(31 citation statements)

References 42 publications

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“…15 Bioinformatical analysis suggests that-at the primary sequence level-the Tudor domain is inserted into the Cterminal SN domain (SN5). 21,22 The existence of such an extended Tudor domain (TSN) was confirmed by structural studies of human Tudor-SN. 23 The study provided biochemical evidence for an interaction between the TSN domain and several snRNPs.…”

Section: Introductionmentioning

confidence: 75%

Structure and Ligand Binding of the Extended Tudor Domain of D. melanogaster Tudor-SN

Friberg

Corsini

Mourão

et al. 2009

Journal of Molecular Biology

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Section: Introductionmentioning

confidence: 75%

Structure and Ligand Binding of the Extended Tudor Domain of D. melanogaster Tudor-SN

Friberg

Corsini

Mourão

et al. 2009

Journal of Molecular Biology

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“…4SNc-Tudor domain protein (also known as p100) has been previously thought to function as a transcription co-factor associated with pathogenic invasion (Ponting 1997). Recent studies show that it is a key component linking RNA interference and editing (Yang et al 2007).…”

Section: Discussionmentioning

confidence: 97%

Comparative proteomics analysis of cardiac muscle samples from pufferfishTakifugu rubripesexposed to excessive fluoride: Initial molecular response to fluorosis

Lü

Zheng

et al. 2009

Toxicology Mechanisms and Methods

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Comparative proteomics was performed to identify proteins in the cardiac muscle of Takifugu rubripes in initial response to excessive fluoride. Sixteen fish were randomly divided into a control group and an experimental group. The control group was raised in softwater alone (F(-) = 0.4 mg/L), and the experimental group was raised in the same water with sodium fluoride at a high concentration of 35 mg/L. After 3 days, proteins were extracted from the fish cardiac muscle and then were subjected to 2D PAGE analysis. The matrix assisted laser desorption ionization time of flight mass spectrometry (Maldi TOF MS) was applied to identify the proteins that were differentially expressed from the two groups of fish. Average of 318 and 275 proteins detected in the control and the experimental group, respectively, 167 spots were matched and 21 highly differentially expressed proteins were further analyzed by Maldi TOF-TOF MS, and 15 were identified by MASCOT. These 15 proteins include Telomerase reverse transcriptase, 4SNc-Tudor domain protein, protein disulfide isomerase ER-60, Tuba1 protein, mitogen-activated protein kinase 10, and SMC4 protein. Consistent with their previously known functions, these identified proteins seem to be involved in apoptosis and other functions associated with fluorosis. These results will contribute to our understanding for the effects of fluoride exposure on the physiological and biochemical functions of takifugu, and the toxicological mechanism of fluoride causing fluorosis in both fish and human.

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“…4SNc-Tudor domain protein is also known as p100 and nuclear factor kappa B2 (NF-κB2). It has been previously thought to function as a transcription cofactor associated with pathogenic invasion [24]. Recent studies show that it is a key component linking RNA interference and editing [25].…”

Section: Discussionmentioning

confidence: 99%

Proteomics analysis of liver samples from puffer fish Takifugu rubripes exposed to excessive fluoride: An insight into molecular response to fluorosis

Lü

Zheng

Liu

et al. 2010

J Biochem & Molecular Tox

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Comparative proteomics was performed to identify proteins in the liver of Takifugu rubripes in response to excessive fluoride exposure. Sixteen fish were randomly divided into a control group and an experimental group. The control group was raised in soft water alone (F(-) = 0.4 mg/L), and the experimental group was raised in the same water with sodium fluoride at a high concentration of 35 mg/L. After 3 days, proteins were extracted from the fish livers and then subjected to two-dimensional polyacrylamide gel electrophoresis analysis. The matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS) was applied to identify the proteins that were differentially expressed from the two groups of fish. Among an average of 816 and 918 proteins detected in the control and treated groups, respectively, 16 proteins were upregulated and 35 were downregulated (P < 0.01) in the fluoride-treated group as compared with those in the control group. Twenty-four highly differentially expressed proteins were further analyzed by MALDI-TOF/TOF-MS, and eight were identified by Mascot. These eight proteins include disulfide isomerase ER-60, 4SNc-Tudor domain protein, SMC3 protein, Cyclin D1, and mitogen-activated protein kinase 10, as well as three unknown proteins. Consistent with their previously known functions, these identified proteins seem to be involved in apoptosis and other functions associated with fluorosis. These results will greatly contribute to our understanding of the effects of fluoride exposure on the physiological and biochemical functions of Takifugu and the toxicological mechanism of fluoride causing fluorosis in both fish and human.

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P100, a transcriptional coactivator, is a human homologue of staphylococcal nuclease

Cited by 45 publications

References 42 publications

Structure and Ligand Binding of the Extended Tudor Domain of D. melanogaster Tudor-SN

Structure and Ligand Binding of the Extended Tudor Domain of D. melanogaster Tudor-SN

Comparative proteomics analysis of cardiac muscle samples from pufferfishTakifugu rubripesexposed to excessive fluoride: Initial molecular response to fluorosis

Proteomics analysis of liver samples from puffer fish Takifugu rubripes exposed to excessive fluoride: An insight into molecular response to fluorosis

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