8 research outputs found
Creation of a publication plan in the field of science and research
This thesis focuses on the topic of open data, especially in the field of science and research. The work is defined by six sub-targets and characterize the area of science and research in the Czech Republic and abroad, to characterize the issue of open data in the Czech Republic and in the world, describe the method of publication of data on the promotion of science and research in the Czech Republic and in the world, how to propose a procedure and create publications plan for TA CR, prepare a sample dataset, and then evaluate the procedure used. The work is divided into thematic blocks, which are based on these goals. It consists of an introduction, theoretical part, practical part and conclusion. The introductory section defines the objectives of work and research resources devoted to similar topics. The theoretical part describes the problems of science and the problem of open data in the Czech Republic and other countries, and also the process of creating publication plan according to the chosen methodology. The practical part contains according to the targets two parts, one is the analysis of open data of science and research and other preparation publication plan TA CR. The practical part ends with evaluation of procedure used with proposals for improvement. The conclusion contains a summary of the work and evaluate the goals achieved
Additional file 2: of Molecular characterization of irinotecan (SN-38) resistant human breast cancer cell lines
32 genes that are differentially expressed in both the MDA-MB-231 and the MCF7 model system. (XLSX 4123Â kb
TIMP‑1 Increases Expression and Phosphorylation of Proteins Associated with Drug Resistance in Breast Cancer Cells
Tissue inhibitor of metalloproteinase
1 (TIMP-1) is a protein with
a potential biological role in drug resistance. To elucidate the unknown
molecular mechanisms underlying the association between high TIMP-1
levels and increased chemotherapy resistance, we employed SILAC-based
quantitative mass spectrometry to analyze global proteome and phosphoproteome
differences of MCF-7 breast cancer cells expressing high or low levels
of TIMP-1. In TIMP-1 high expressing cells, 312 proteins and 452 phosphorylation
sites were up-regulated. Among these were the cancer drug targets
topoisomerase 1, 2A, and 2B, which may explain the resistance phenotype
to topoisomerase inhibitors that was observed in cells with high TIMP-1
levels. Pathway analysis showed an enrichment of proteins from functional
categories such as apoptosis, cell cycle, DNA repair, transcription
factors, drug targets and proteins associated with drug resistance
or sensitivity, and drug transportation. The NetworKIN algorithm predicted
the protein kinases CK2a, CDK1, PLK1, and ATM as likely candidates
involved in the hyperphosphorylation of the topoisomerases. Up-regulation
of protein and/or phosphorylation levels of topoisomerases in TIMP-1
high expressing cells may be part of the mechanisms by which TIMP-1
confers resistance to treatment with the widely used topoisomerase
inhibitors in breast and colorectal cancer
TIMP‑1 Increases Expression and Phosphorylation of Proteins Associated with Drug Resistance in Breast Cancer Cells
Tissue inhibitor of metalloproteinase
1 (TIMP-1) is a protein with
a potential biological role in drug resistance. To elucidate the unknown
molecular mechanisms underlying the association between high TIMP-1
levels and increased chemotherapy resistance, we employed SILAC-based
quantitative mass spectrometry to analyze global proteome and phosphoproteome
differences of MCF-7 breast cancer cells expressing high or low levels
of TIMP-1. In TIMP-1 high expressing cells, 312 proteins and 452 phosphorylation
sites were up-regulated. Among these were the cancer drug targets
topoisomerase 1, 2A, and 2B, which may explain the resistance phenotype
to topoisomerase inhibitors that was observed in cells with high TIMP-1
levels. Pathway analysis showed an enrichment of proteins from functional
categories such as apoptosis, cell cycle, DNA repair, transcription
factors, drug targets and proteins associated with drug resistance
or sensitivity, and drug transportation. The NetworKIN algorithm predicted
the protein kinases CK2a, CDK1, PLK1, and ATM as likely candidates
involved in the hyperphosphorylation of the topoisomerases. Up-regulation
of protein and/or phosphorylation levels of topoisomerases in TIMP-1
high expressing cells may be part of the mechanisms by which TIMP-1
confers resistance to treatment with the widely used topoisomerase
inhibitors in breast and colorectal cancer
TIMP‑1 Increases Expression and Phosphorylation of Proteins Associated with Drug Resistance in Breast Cancer Cells
Tissue inhibitor of metalloproteinase
1 (TIMP-1) is a protein with
a potential biological role in drug resistance. To elucidate the unknown
molecular mechanisms underlying the association between high TIMP-1
levels and increased chemotherapy resistance, we employed SILAC-based
quantitative mass spectrometry to analyze global proteome and phosphoproteome
differences of MCF-7 breast cancer cells expressing high or low levels
of TIMP-1. In TIMP-1 high expressing cells, 312 proteins and 452 phosphorylation
sites were up-regulated. Among these were the cancer drug targets
topoisomerase 1, 2A, and 2B, which may explain the resistance phenotype
to topoisomerase inhibitors that was observed in cells with high TIMP-1
levels. Pathway analysis showed an enrichment of proteins from functional
categories such as apoptosis, cell cycle, DNA repair, transcription
factors, drug targets and proteins associated with drug resistance
or sensitivity, and drug transportation. The NetworKIN algorithm predicted
the protein kinases CK2a, CDK1, PLK1, and ATM as likely candidates
involved in the hyperphosphorylation of the topoisomerases. Up-regulation
of protein and/or phosphorylation levels of topoisomerases in TIMP-1
high expressing cells may be part of the mechanisms by which TIMP-1
confers resistance to treatment with the widely used topoisomerase
inhibitors in breast and colorectal cancer
TIMP‑1 Increases Expression and Phosphorylation of Proteins Associated with Drug Resistance in Breast Cancer Cells
Tissue inhibitor of metalloproteinase
1 (TIMP-1) is a protein with
a potential biological role in drug resistance. To elucidate the unknown
molecular mechanisms underlying the association between high TIMP-1
levels and increased chemotherapy resistance, we employed SILAC-based
quantitative mass spectrometry to analyze global proteome and phosphoproteome
differences of MCF-7 breast cancer cells expressing high or low levels
of TIMP-1. In TIMP-1 high expressing cells, 312 proteins and 452 phosphorylation
sites were up-regulated. Among these were the cancer drug targets
topoisomerase 1, 2A, and 2B, which may explain the resistance phenotype
to topoisomerase inhibitors that was observed in cells with high TIMP-1
levels. Pathway analysis showed an enrichment of proteins from functional
categories such as apoptosis, cell cycle, DNA repair, transcription
factors, drug targets and proteins associated with drug resistance
or sensitivity, and drug transportation. The NetworKIN algorithm predicted
the protein kinases CK2a, CDK1, PLK1, and ATM as likely candidates
involved in the hyperphosphorylation of the topoisomerases. Up-regulation
of protein and/or phosphorylation levels of topoisomerases in TIMP-1
high expressing cells may be part of the mechanisms by which TIMP-1
confers resistance to treatment with the widely used topoisomerase
inhibitors in breast and colorectal cancer
TIMP‑1 Increases Expression and Phosphorylation of Proteins Associated with Drug Resistance in Breast Cancer Cells
Tissue inhibitor of metalloproteinase
1 (TIMP-1) is a protein with
a potential biological role in drug resistance. To elucidate the unknown
molecular mechanisms underlying the association between high TIMP-1
levels and increased chemotherapy resistance, we employed SILAC-based
quantitative mass spectrometry to analyze global proteome and phosphoproteome
differences of MCF-7 breast cancer cells expressing high or low levels
of TIMP-1. In TIMP-1 high expressing cells, 312 proteins and 452 phosphorylation
sites were up-regulated. Among these were the cancer drug targets
topoisomerase 1, 2A, and 2B, which may explain the resistance phenotype
to topoisomerase inhibitors that was observed in cells with high TIMP-1
levels. Pathway analysis showed an enrichment of proteins from functional
categories such as apoptosis, cell cycle, DNA repair, transcription
factors, drug targets and proteins associated with drug resistance
or sensitivity, and drug transportation. The NetworKIN algorithm predicted
the protein kinases CK2a, CDK1, PLK1, and ATM as likely candidates
involved in the hyperphosphorylation of the topoisomerases. Up-regulation
of protein and/or phosphorylation levels of topoisomerases in TIMP-1
high expressing cells may be part of the mechanisms by which TIMP-1
confers resistance to treatment with the widely used topoisomerase
inhibitors in breast and colorectal cancer
TIMP‑1 Increases Expression and Phosphorylation of Proteins Associated with Drug Resistance in Breast Cancer Cells
Tissue inhibitor of metalloproteinase
1 (TIMP-1) is a protein with
a potential biological role in drug resistance. To elucidate the unknown
molecular mechanisms underlying the association between high TIMP-1
levels and increased chemotherapy resistance, we employed SILAC-based
quantitative mass spectrometry to analyze global proteome and phosphoproteome
differences of MCF-7 breast cancer cells expressing high or low levels
of TIMP-1. In TIMP-1 high expressing cells, 312 proteins and 452 phosphorylation
sites were up-regulated. Among these were the cancer drug targets
topoisomerase 1, 2A, and 2B, which may explain the resistance phenotype
to topoisomerase inhibitors that was observed in cells with high TIMP-1
levels. Pathway analysis showed an enrichment of proteins from functional
categories such as apoptosis, cell cycle, DNA repair, transcription
factors, drug targets and proteins associated with drug resistance
or sensitivity, and drug transportation. The NetworKIN algorithm predicted
the protein kinases CK2a, CDK1, PLK1, and ATM as likely candidates
involved in the hyperphosphorylation of the topoisomerases. Up-regulation
of protein and/or phosphorylation levels of topoisomerases in TIMP-1
high expressing cells may be part of the mechanisms by which TIMP-1
confers resistance to treatment with the widely used topoisomerase
inhibitors in breast and colorectal cancer