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Quantitation of human metallothionein isoforms in cells, tissues, and cerebrospinal fluid by mass spectrometry

EPSCoR Research Infrastructure Improvement Program AND Program Evaluation

[No authors listed]
GSID: PyvTA2Uo0eUJ
JB Shabb, WW Muhonen, AA Mehus - Methods in Enzymology, 2017 - Elsevier

Metallothioneins (MTs) are a family of small, highly conserved, cysteine-rich metal-binding proteins that are important for zinc and copper homeostasis, protection against oxidative stress, and buffering against toxic heavy metals. Individual human MT isoforms are candidate biomarkers for heavy...

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Shabb, J. B., Muhonen, W. W., & Mehus, A. A. (2017). Quantitation of human metallothionein isoforms in cells, tissues, and cerebrospinal fluid by mass spectrometry. In Methods in Enzymology (Vol. 586, pp. 413-431). Academic Press.
Shabb, J. B., W. W. Muhonen, and A. A. Mehus. "Quantitation of human metallothionein isoforms in cells, tissues, and cerebrospinal fluid by mass spectrometry." Methods in Enzymology. Vol. 586. Academic Press, 2017. 413-431.
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UDL in apprenticeships and career training programs that serve youth with untapped talent

Stem career programs

Castine EE.
GSID: kzv9kNlnbkMJ
SC Johnston, EE Castine - Transforming Higher Education …, 2019 - taylorfrancis.com

A greater focus on providing high quality career training programs could help address high levels of youth unemployment, inequitable access to well-paying jobs, under developed talent within the youth population, and labor shortages across numerous industries worldwide (Symonds, Schwartz,...

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Johnston, S. C., & Castine, E. E. (2019). UDL in apprenticeships and career training programs that serve youth with untapped talent. In Transforming Higher Education Through Universal Design for Learning (pp. 131-158). Routledge.
Johnston, Sam Catherine, and Eleanor Ellie Castine. "UDL in apprenticeships and career training programs that serve youth with untapped talent." Transforming Higher Education Through Universal Design for Learning. Routledge, 2019. 131-158.
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Predicting antimicrobial and other cysteine-rich peptides in 1267 plant transcriptomes

pipeline programs

Shelenkov A.
GSID: f2Wzp6bCm0AJ
A Shelenkov, A Slavokhotova, T Odintsova - Antibiotics, 2020 - mdpi.com

Antimicrobial peptides (AMPs) are a key component of innate immunity in various organisms including bacteria, insects, mammals, and plants. Their mode of action decreases the …

A network biology approach evaluating the anticancer effects of bortezomib identifies SPARC as a therapeutic target in adult T-cell leukemia cells.

Advances and applications in bioinformatics and chemistry : AABC

Ohyashiki JH, Hamamura R, Kobayashi C, Zhang Y, Ohyashiki K.
PMID: 21918608
Adv Appl Bioinform Chem. 2008;1:85-98. doi: 10.2147/aabc.s4133. Epub 2008 Oct 30.

There is a need to identify the regulatory gene interaction of anticancer drugs on target cancer cells. Whole genome expression profiling offers promise in this regard, but can be complicated by the challenge of identifying the genes affected by...

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Ohyashiki JH, Hamamura R, Kobayashi C, et al. A network biology approach evaluating the anticancer effects of bortezomib identifies SPARC as a therapeutic target in adult T-cell leukemia cells. Adv Appl Bioinform Chem. 2008;1:85-98doi: 10.2147/aabc.s4133.
Ohyashiki, J. H., Hamamura, R., Kobayashi, C., Zhang, Y., & Ohyashiki, K. (2008). A network biology approach evaluating the anticancer effects of bortezomib identifies SPARC as a therapeutic target in adult T-cell leukemia cells. Advances and applications in bioinformatics and chemistry : AABC, 185-98. https://doi.org/10.2147/aabc.s4133
Ohyashiki, Junko H, et al. "A network biology approach evaluating the anticancer effects of bortezomib identifies SPARC as a therapeutic target in adult T-cell leukemia cells." Advances and applications in bioinformatics and chemistry : AABC vol. 1 (2008): 85-98. doi: https://doi.org/10.2147/aabc.s4133
Ohyashiki JH, Hamamura R, Kobayashi C, Zhang Y, Ohyashiki K. A network biology approach evaluating the anticancer effects of bortezomib identifies SPARC as a therapeutic target in adult T-cell leukemia cells. Adv Appl Bioinform Chem. 2008;1:85-98. doi: 10.2147/aabc.s4133. Epub 2008 Oct 30. PMID: 21918608; PMCID: PMC3169936.
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Amino acids inhibit kynurenic acid formation via suppression of kynurenine uptake or kynurenic acid synthesis in rat brain in vitro.

SpringerPlus

Sekine A, Okamoto M, Kanatani Y, Sano M, Shibata K, Fukuwatari T.
PMID: 25674503
Springerplus. 2015 Feb 01;4:48. doi: 10.1186/s40064-015-0826-9. eCollection 2015.

The tryptophan metabolite, kynurenic acid (KYNA), is a preferential antagonist of the α7 nicotinic acetylcholine receptor at endogenous brain concentrations. Recent studies have suggested that increase of brain KYNA levels is involved in psychiatric disorders such as schizophrenia and...

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Sekine A, Okamoto M, Kanatani Y, et al. Amino acids inhibit kynurenic acid formation via suppression of kynurenine uptake or kynurenic acid synthesis in rat brain in vitro. Springerplus. 2015;4:48doi: 10.1186/s40064-015-0826-9.
Sekine, A., Okamoto, M., Kanatani, Y., Sano, M., Shibata, K., & Fukuwatari, T. (2015). Amino acids inhibit kynurenic acid formation via suppression of kynurenine uptake or kynurenic acid synthesis in rat brain in vitro. SpringerPlus, 448. https://doi.org/10.1186/s40064-015-0826-9
Sekine, Airi, et al. "Amino acids inhibit kynurenic acid formation via suppression of kynurenine uptake or kynurenic acid synthesis in rat brain in vitro." SpringerPlus vol. 4 (2015): 48. doi: https://doi.org/10.1186/s40064-015-0826-9
Sekine A, Okamoto M, Kanatani Y, Sano M, Shibata K, Fukuwatari T. Amino acids inhibit kynurenic acid formation via suppression of kynurenine uptake or kynurenic acid synthesis in rat brain in vitro. Springerplus. 2015 Feb 01;4:48. doi: 10.1186/s40064-015-0826-9. eCollection 2015. PMID: 25674503; PMCID: PMC4318830.
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Secreted protein acidic and rich in cysteine (SPARC) induces cell migration and epithelial mesenchymal transition through WNK1/snail in non-small cell lung cancer.

Oncotarget

Hung JY, Yen MC, Jian SF, Wu CY, Chang WA, Liu KT, Hsu YL, Chong IW, Kuo PL.
PMID: 28969021
Oncotarget. 2017 Jul 22;8(38):63691-63702. doi: 10.18632/oncotarget.19475. eCollection 2017 Sep 08.

The extracellular matrix is a component of physiological microenvironment and a regulator of cellular processes such as migration and proliferation. Secreted Protein Acidic and Rich in Cysteine (SPARC/osteonectin) is an extracellular matrix-associated glycoprotein involved in the regulation of cell...

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Hung JY, Yen MC, Jian SF, et al. Secreted protein acidic and rich in cysteine (SPARC) induces cell migration and epithelial mesenchymal transition through WNK1/snail in non-small cell lung cancer. Oncotarget. 2017;8(38):63691-63702doi: 10.18632/oncotarget.19475.
Hung, J. Y., Yen, M. C., Jian, S. F., Wu, C. Y., Chang, W. A., Liu, K. T., Hsu, Y. L., Chong, I. W., & Kuo, P. L. (2017). Secreted protein acidic and rich in cysteine (SPARC) induces cell migration and epithelial mesenchymal transition through WNK1/snail in non-small cell lung cancer. Oncotarget, 8(38), 63691-63702. https://doi.org/10.18632/oncotarget.19475
Hung, Jen-Yu, et al. "Secreted protein acidic and rich in cysteine (SPARC) induces cell migration and epithelial mesenchymal transition through WNK1/snail in non-small cell lung cancer." Oncotarget vol. 8,38 (2017): 63691-63702. doi: https://doi.org/10.18632/oncotarget.19475
Hung JY, Yen MC, Jian SF, Wu CY, Chang WA, Liu KT, Hsu YL, Chong IW, Kuo PL. Secreted protein acidic and rich in cysteine (SPARC) induces cell migration and epithelial mesenchymal transition through WNK1/snail in non-small cell lung cancer. Oncotarget. 2017 Jul 22;8(38):63691-63702. doi: 10.18632/oncotarget.19475. eCollection 2017 Sep 08. PMID: 28969021; PMCID: PMC5609953.
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Albendazole induces oxidative stress and DNA damage in the parasitic protozoan Giardia duodenalis.

Frontiers in microbiology

Martínez-Espinosa R, Argüello-García R, Saavedra E, Ortega-Pierres G.
PMID: 26300866
Front Microbiol. 2015 Aug 06;6:800. doi: 10.3389/fmicb.2015.00800. eCollection 2015.

The control of Giardia duodenalis infections is carried out mainly by drugs, among these albendazole (ABZ) is commonly used. Although the cytotoxic effect of ABZ usually involves binding to β-tubulin, it has been suggested that oxidative stress may also...

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Martínez-Espinosa R, Argüello-García R, Saavedra E, et al. Albendazole induces oxidative stress and DNA damage in the parasitic protozoan Giardia duodenalis. Front Microbiol. 2015;6:800doi: 10.3389/fmicb.2015.00800.
Martínez-Espinosa, R., Argüello-García, R., Saavedra, E., & Ortega-Pierres, G. (2015). Albendazole induces oxidative stress and DNA damage in the parasitic protozoan Giardia duodenalis. Frontiers in microbiology, 6800. https://doi.org/10.3389/fmicb.2015.00800
Martínez-Espinosa, Rodrigo, et al. "Albendazole induces oxidative stress and DNA damage in the parasitic protozoan Giardia duodenalis." Frontiers in microbiology vol. 6 (2015): 800. doi: https://doi.org/10.3389/fmicb.2015.00800
Martínez-Espinosa R, Argüello-García R, Saavedra E, Ortega-Pierres G. Albendazole induces oxidative stress and DNA damage in the parasitic protozoan Giardia duodenalis. Front Microbiol. 2015 Aug 06;6:800. doi: 10.3389/fmicb.2015.00800. eCollection 2015. PMID: 26300866; PMCID: PMC4526806.
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Mapping of the local environmental changes in proteins by cysteine scanning.

Biophysics (Nagoya-shi, Japan)

Yamazaki Y, Nagata T, Terakita A, Kandori H, Shichida Y, Imamoto Y.
PMID: 27493492
Biophysics (Nagoya-shi). 2014 Jan 16;10:1-7. doi: 10.2142/biophysics.10.1. eCollection 2014.

Protein conformational changes, which regulate the activity of proteins, are induced by the alternation of intramolecular interactions. Therefore, the detection of the local environmental changes around the key amino acid residues is essential to understand the activation mechanisms of...

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Yamazaki Y, Nagata T, Terakita A, et al. Mapping of the local environmental changes in proteins by cysteine scanning. Biophysics (Nagoya-shi). 2014;10:1-7doi: 10.2142/biophysics.10.1.
Yamazaki, Y., Nagata, T., Terakita, A., Kandori, H., Shichida, Y., & Imamoto, Y. (2014). Mapping of the local environmental changes in proteins by cysteine scanning. Biophysics (Nagoya-shi, Japan), 101-7. https://doi.org/10.2142/biophysics.10.1
Yamazaki, Yoichi, et al. "Mapping of the local environmental changes in proteins by cysteine scanning." Biophysics (Nagoya-shi, Japan) vol. 10 (2014): 1-7. doi: https://doi.org/10.2142/biophysics.10.1
Yamazaki Y, Nagata T, Terakita A, Kandori H, Shichida Y, Imamoto Y. Mapping of the local environmental changes in proteins by cysteine scanning. Biophysics (Nagoya-shi). 2014 Jan 16;10:1-7. doi: 10.2142/biophysics.10.1. eCollection 2014. PMID: 27493492; PMCID: PMC4629666.
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Decreased calpain 6 expression is associated with tumorigenesis and poor prognosis in HNSCC.

Oncology letters

Xiang Y, Li F, Wang L, Zheng A, Zuo J, Li M, Wang Y, Xu Y, Chen C, Chen S, Xiao B, Tao Z.
PMID: 28454386
Oncol Lett. 2017 Apr;13(4):2237-2243. doi: 10.3892/ol.2017.5687. Epub 2017 Feb 07.

Calpains are a family of intracellular cysteine proteases involved in various biological processes. Previously, the family was identified to have abnormal expression in several types of malignant tumor. Calpain 6 was less well known; however, it was recently identified...

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Xiang Y, Li F, Wang L, et al. Decreased calpain 6 expression is associated with tumorigenesis and poor prognosis in HNSCC. Oncol Lett. 2017;13(4):2237-2243doi: 10.3892/ol.2017.5687.
Xiang, Y., Li, F., Wang, L., Zheng, A., Zuo, J., Li, M., Wang, Y., Xu, Y., Chen, C., Chen, S., Xiao, B., & Tao, Z. (2017). Decreased calpain 6 expression is associated with tumorigenesis and poor prognosis in HNSCC. Oncology letters, 13(4), 2237-2243. https://doi.org/10.3892/ol.2017.5687
Xiang, Yinzhou, et al. "Decreased calpain 6 expression is associated with tumorigenesis and poor prognosis in HNSCC." Oncology letters vol. 13,4 (2017): 2237-2243. doi: https://doi.org/10.3892/ol.2017.5687
Xiang Y, Li F, Wang L, Zheng A, Zuo J, Li M, Wang Y, Xu Y, Chen C, Chen S, Xiao B, Tao Z. Decreased calpain 6 expression is associated with tumorigenesis and poor prognosis in HNSCC. Oncol Lett. 2017 Apr;13(4):2237-2243. doi: 10.3892/ol.2017.5687. Epub 2017 Feb 07. PMID: 28454386; PMCID: PMC5403261.
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Plant Cell Wall-Penetrable, Redox-Responsive Silica Nanoprobe for the Imaging of Starvation-Induced Vesicle Trafficking.

Analytical chemistry

Huang XC, Inoue-Aono Y, Moriyasu Y, Hsieh PY, Tu WM, Hsiao SC, Jane WN, Hsu HY.
PMID: 27673337
Anal Chem. 2016 Oct 18;88(20):10231-10236. doi: 10.1021/acs.analchem.6b02920. Epub 2016 Oct 06.

Autophagy is a self-protection process against reactive oxygen species (ROS). The intracellular level of ROS increased when cells were cultured under nutrient starvation. Antioxidants such as glutathione and ascorbic acid play an important role in ROS removal. However, the...

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Huang XC, Inoue-Aono Y, Moriyasu Y, et al. Plant Cell Wall-Penetrable, Redox-Responsive Silica Nanoprobe for the Imaging of Starvation-Induced Vesicle Trafficking. Anal Chem. 2016;88(20):10231-10236doi: 10.1021/acs.analchem.6b02920.
Huang, X. C., Inoue-Aono, Y., Moriyasu, Y., Hsieh, P. Y., Tu, W. M., Hsiao, S. C., Jane, W. N., & Hsu, H. Y. (2016). Plant Cell Wall-Penetrable, Redox-Responsive Silica Nanoprobe for the Imaging of Starvation-Induced Vesicle Trafficking. Analytical chemistry, 88(20), 10231-10236. https://doi.org/10.1021/acs.analchem.6b02920
Huang, Xin-Chun, et al. "Plant Cell Wall-Penetrable, Redox-Responsive Silica Nanoprobe for the Imaging of Starvation-Induced Vesicle Trafficking." Analytical chemistry vol. 88,20 (2016): 10231-10236. doi: https://doi.org/10.1021/acs.analchem.6b02920
Huang XC, Inoue-Aono Y, Moriyasu Y, Hsieh PY, Tu WM, Hsiao SC, Jane WN, Hsu HY. Plant Cell Wall-Penetrable, Redox-Responsive Silica Nanoprobe for the Imaging of Starvation-Induced Vesicle Trafficking. Anal Chem. 2016 Oct 18;88(20):10231-10236. doi: 10.1021/acs.analchem.6b02920. Epub 2016 Oct 06. PMID: 27673337.
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Correction: Combined Treatment with Troglitazone and Lovastatin Inhibited Epidermal Growth Factor-Induced Migration through the Downregulation of Cysteine-Rich Protein 61 in Human Anaplastic Thyroid Cancer Cells.

PloS one

Chin LH, Hsu SP, Zhong WB, Liang YC.
PMID: 28481927
PLoS One. 2017 May 08;12(5):e0177545. doi: 10.1371/journal.pone.0177545. eCollection 2017.

[This corrects the article DOI: 10.1371/journal.pone.0118674.].

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Chin LH, Hsu SP, Zhong WB, et al. Correction: Combined Treatment with Troglitazone and Lovastatin Inhibited Epidermal Growth Factor-Induced Migration through the Downregulation of Cysteine-Rich Protein 61 in Human Anaplastic Thyroid Cancer Cells. PLoS One. 2017;12(5):e0177545doi: 10.1371/journal.pone.0177545.
Chin, L. H., Hsu, S. P., Zhong, W. B., & Liang, Y. C. (2017). Correction: Combined Treatment with Troglitazone and Lovastatin Inhibited Epidermal Growth Factor-Induced Migration through the Downregulation of Cysteine-Rich Protein 61 in Human Anaplastic Thyroid Cancer Cells. PloS one, 12(5), e0177545. https://doi.org/10.1371/journal.pone.0177545
Chin, Li-Han, et al. "Correction: Combined Treatment with Troglitazone and Lovastatin Inhibited Epidermal Growth Factor-Induced Migration through the Downregulation of Cysteine-Rich Protein 61 in Human Anaplastic Thyroid Cancer Cells." PloS one vol. 12,5 (2017): e0177545. doi: https://doi.org/10.1371/journal.pone.0177545
Chin LH, Hsu SP, Zhong WB, Liang YC. Correction: Combined Treatment with Troglitazone and Lovastatin Inhibited Epidermal Growth Factor-Induced Migration through the Downregulation of Cysteine-Rich Protein 61 in Human Anaplastic Thyroid Cancer Cells. PLoS One. 2017 May 08;12(5):e0177545. doi: 10.1371/journal.pone.0177545. eCollection 2017. PMID: 28481927; PMCID: PMC5421810.
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Disulfide bond formation of thiols by using carbon nanotubes.

Nanoscale

Hirano A, Kameda T, Sakuraba S, Wada M, Tanaka T, Kataura H.
PMID: 28422249
Nanoscale. 2017 May 04;9(17):5389-5393. doi: 10.1039/c7nr01001j.

Clarification of the interactions between carbon nanotubes (CNTs) and proteinogenic amino acids is a key approach to understanding CNT-protein interactions. Previous studies have addressed the mechanism of the physical adsorption of amino acids onto CNTs. However, little is known...

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Hirano A, Kameda T, Sakuraba S, et al. Disulfide bond formation of thiols by using carbon nanotubes. Nanoscale. 2017;9(17):5389-5393doi: 10.1039/c7nr01001j.
Hirano, A., Kameda, T., Sakuraba, S., Wada, M., Tanaka, T., & Kataura, H. (2017). Disulfide bond formation of thiols by using carbon nanotubes. Nanoscale, 9(17), 5389-5393. https://doi.org/10.1039/c7nr01001j
Hirano, A, et al. "Disulfide bond formation of thiols by using carbon nanotubes." Nanoscale vol. 9,17 (2017): 5389-5393. doi: https://doi.org/10.1039/c7nr01001j
Hirano A, Kameda T, Sakuraba S, Wada M, Tanaka T, Kataura H. Disulfide bond formation of thiols by using carbon nanotubes. Nanoscale. 2017 May 04;9(17):5389-5393. doi: 10.1039/c7nr01001j. PMID: 28422249.
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Showing 1 to 12 of 7942 entries