Plasma Membrane Proteomics of Human Breast Cancer Cell Lines Identifies Potential Targets for Breast Cancer Diagnosis and Treatment
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{"title"=>"Plasma membrane proteomics of human breast cancer cell lines identifies potential targets for breast cancer diagnosis and treatment", "type"=>"journal", "authors"=>[{"first_name"=>"Yvonne S.", "last_name"=>"Ziegler", "scopus_author_id"=>"6603644826"}, {"first_name"=>"James J.", "last_name"=>"Moresco", "scopus_author_id"=>"6503994367"}, {"first_name"=>"Patricia G.", "last_name"=>"Tu", "scopus_author_id"=>"55427912100"}, {"first_name"=>"John R.", "last_name"=>"Yates", "scopus_author_id"=>"35352109200"}, {"first_name"=>"Ann M.", "last_name"=>"Nardulli", "scopus_author_id"=>"7004345515"}], "year"=>2014, "source"=>"PLoS ONE", "identifiers"=>{"scopus"=>"2-s2.0-84904297960", "sgr"=>"84904297960", "issn"=>"19326203", "doi"=>"10.1371/journal.pone.0102341", "pmid"=>"25029196", "pui"=>"373542282"}, "id"=>"6088378d-2530-376d-98f4-dc29ea271efe", "abstract"=>"The use of broad spectrum chemotherapeutic agents to treat breast cancer results in substantial and debilitating side effects, necessitating the development of targeted therapies to limit tumor proliferation and prevent metastasis. In recent years, the list of approved targeted therapies has expanded, and it includes both monoclonal antibodies and small molecule inhibitors that interfere with key proteins involved in the uncontrolled growth and migration of cancer cells. The targeting of plasma membrane proteins has been most successful to date, and this is reflected in the large representation of these proteins as targets of newer therapies. In view of these facts, experiments were designed to investigate the plasma membrane proteome of a variety of human breast cancer cell lines representing hormone-responsive, ErbB2 over-expressing and triple negative cell types, as well as a benign control. Plasma membranes were isolated by using an aqueous two-phase system, and the resulting proteins were subjected to mass spectrometry analysis. Overall, each of the cell lines expressed some unique proteins, and a number of proteins were expressed in multiple cell lines, but in patterns that did not always follow traditional clinical definitions of breast cancer type. From our data, it can be deduced that most cancer cells possess multiple strategies to promote uncontrolled growth, reflected in aberrant expression of tyrosine kinases, cellular adhesion molecules, and structural proteins. Our data set provides a very rich and complex picture of plasma membrane proteins present on breast cancer cells, and the sorting and categorizing of this data provides interesting insights into the biology, classification, and potential treatment of this prevalent and debilitating disease.", "link"=>"http://www.mendeley.com/research/plasma-membrane-proteomics-human-breast-cancer-cell-lines-identifies-potential-targets-breast-cancer", "reader_count"=>39, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>4, "Researcher"=>7, "Student > Ph. D. Student"=>10, "Student > Postgraduate"=>1, "Student > Master"=>6, "Other"=>2, "Student > Bachelor"=>7, "Lecturer"=>1, "Professor"=>1}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>4, "Researcher"=>7, "Student > Ph. D. Student"=>10, "Student > Postgraduate"=>1, "Student > Master"=>6, "Other"=>2, "Student > Bachelor"=>7, "Lecturer"=>1, "Professor"=>1}, "reader_count_by_subject_area"=>{"Unspecified"=>2, "Engineering"=>7, "Biochemistry, Genetics and Molecular Biology"=>8, "Agricultural and Biological Sciences"=>12, "Neuroscience"=>1, "Pharmacology, Toxicology and Pharmaceutical Science"=>1, "Physics and Astronomy"=>1, "Chemistry"=>4, "Computer Science"=>3}, "reader_count_by_subdiscipline"=>{"Engineering"=>{"Engineering"=>7}, "Neuroscience"=>{"Neuroscience"=>1}, "Chemistry"=>{"Chemistry"=>4}, "Physics and Astronomy"=>{"Physics and Astronomy"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>12}, "Computer Science"=>{"Computer Science"=>3}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>8}, "Unspecified"=>{"Unspecified"=>2}, "Pharmacology, Toxicology and Pharmaceutical Science"=>{"Pharmacology, Toxicology and Pharmaceutical Science"=>1}}, "reader_count_by_country"=>{"France"=>1, "Germany"=>1, "India"=>1}, "group_count"=>2}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1596595"], "description"=>"<p>Categories relevant to proliferation and metastasis were examined and spectral IDs for proteins in each category were summed for each cell line (<a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0102341#pone.0102341.s002\" target=\"_blank\">Tables S2</a>-<a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0102341#pone.0102341.s007\" target=\"_blank\">S7</a>). This allowed an overall comparison among the cell lines, confirming the more invasive phenotype of the TNBC cells and investigating some specific traits that could potentially be targetable by pharmaceuticals. The % of total spectral IDs was calculated to compensate for differences in the number of spectra obtained for each of the cell lines.</p>", "links"=>[], "tags"=>["Biochemistry", "proteomics", "cell biology", "Molecular cell biology", "molecular biology", "oncology", "Cancers and neoplasms", "Breast tumors", "breast cancer", "Basic cancer research", "Cancer detection and diagnosis", "Cancer treatment", "carcinogenesis", "chemistry", "Analytical chemistry", "mass spectrometry", "Electrospray ionization mass spectrometry"], "article_id"=>1107264, "categories"=>["Biological Sciences"], "users"=>["Yvonne S. Ziegler", "James J. Moresco", "Patricia G. Tu", "John R. Yates III", "Ann M. Nardulli"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0102341.t009", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Oncogenic_processes_/1107264", "title"=>"Oncogenic processes.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-07-16 02:54:46"}
  • {"files"=>["https://ndownloader.figshare.com/files/1596593"], "description"=>"<p>Parentheses indicate ambiguity in the protein identification.</p>", "links"=>[], "tags"=>["Biochemistry", "proteomics", "cell biology", "Molecular cell biology", "molecular biology", "oncology", "Cancers and neoplasms", "Breast tumors", "breast cancer", "Basic cancer research", "Cancer detection and diagnosis", "Cancer treatment", "carcinogenesis", "chemistry", "Analytical chemistry", "mass spectrometry", "Electrospray ionization mass spectrometry", "cytoskeleton", "proteins", "anchoring", "plasma"], "article_id"=>1107262, "categories"=>["Biological Sciences"], "users"=>["Yvonne S. Ziegler", "James J. Moresco", "Patricia G. Tu", "John R. Yates III", "Ann M. Nardulli"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0102341.t007", "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Cortical_cytoskeleton_8211_proteins_anchoring_the_cytoskeleton_to_the_plasma_membrane_/1107262", "title"=>"Cortical cytoskeleton – proteins anchoring the cytoskeleton to the plasma membrane.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-07-16 02:54:46"}
  • {"files"=>["https://ndownloader.figshare.com/files/1596590"], "description"=>"<p>Plasma membrane proteomes for each of the cell lines were compared and the number of shared proteins was examined to determine potential relationships. Bolded numbers reflect the total proteome for the indicated cell line. MDA-MB-231 is abbreviated as MB-231.</p>", "links"=>[], "tags"=>["Biochemistry", "proteomics", "cell biology", "Molecular cell biology", "molecular biology", "oncology", "Cancers and neoplasms", "Breast tumors", "breast cancer", "Basic cancer research", "Cancer detection and diagnosis", "Cancer treatment", "carcinogenesis", "chemistry", "Analytical chemistry", "mass spectrometry", "Electrospray ionization mass spectrometry"], "article_id"=>1107259, "categories"=>["Biological Sciences"], "users"=>["Yvonne S. Ziegler", "James J. Moresco", "Patricia G. Tu", "John R. Yates III", "Ann M. Nardulli"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0102341.t002", "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Intersection_of_the_protein_data_sets_/1107259", "title"=>"Intersection of the protein data sets.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-07-16 02:54:46"}
  • {"files"=>["https://ndownloader.figshare.com/files/1596589"], "description"=>"<p>Tyrosine kinases.</p>", "links"=>[], "tags"=>["Biochemistry", "proteomics", "cell biology", "Molecular cell biology", "molecular biology", "oncology", "Cancers and neoplasms", "Breast tumors", "breast cancer", "Basic cancer research", "Cancer detection and diagnosis", "Cancer treatment", "carcinogenesis", "chemistry", "Analytical chemistry", "mass spectrometry", "Electrospray ionization mass spectrometry"], "article_id"=>1107258, "categories"=>["Biological Sciences"], "users"=>["Yvonne S. Ziegler", "James J. Moresco", "Patricia G. Tu", "John R. Yates III", "Ann M. Nardulli"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0102341.t003", "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Tyrosine_kinases_/1107258", "title"=>"Tyrosine kinases.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-07-16 02:54:46"}
  • {"files"=>["https://ndownloader.figshare.com/files/1596584"], "description"=>"<p>RNA was isolated from each of the cell lines, cDNA was made, and RT-PCR was performed to determine whether the spectral ID numbers were correlated to transcript levels of selected genes. Spectral ID numbers are displayed above each graph and the gene symbol is below those numbers.</p>", "links"=>[], "tags"=>["Biochemistry", "proteomics", "cell biology", "Molecular cell biology", "molecular biology", "oncology", "Cancers and neoplasms", "Breast tumors", "breast cancer", "Basic cancer research", "Cancer detection and diagnosis", "Cancer treatment", "carcinogenesis", "chemistry", "Analytical chemistry", "mass spectrometry", "Electrospray ionization mass spectrometry", "demonstrates", "quantitative", "ms"], "article_id"=>1107253, "categories"=>["Biological Sciences"], "users"=>["Yvonne S. Ziegler", "James J. Moresco", "Patricia G. Tu", "John R. Yates III", "Ann M. Nardulli"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0102341.g004", "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_RT_PCR_demonstrates_the_quantitative_nature_of_the_MS_data_/1107253", "title"=>"RT-PCR demonstrates the quantitative nature of the MS data.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-07-16 02:54:46"}
  • {"files"=>["https://ndownloader.figshare.com/files/1596583"], "description"=>"<p>A. Relationships between the data sets can be visualized by clustering those that share similar expression profiles. B. Venn diagrams highlight the degree of similarity between DT22 and MDA-MB-231 (231) cells compared to DT22 and MCF-10A (10A) cells.</p>", "links"=>[], "tags"=>["Biochemistry", "proteomics", "cell biology", "Molecular cell biology", "molecular biology", "oncology", "Cancers and neoplasms", "Breast tumors", "breast cancer", "Basic cancer research", "Cancer detection and diagnosis", "Cancer treatment", "carcinogenesis", "chemistry", "Analytical chemistry", "mass spectrometry", "Electrospray ionization mass spectrometry", "pm", "proteomes", "shows", "similarities", "differences"], "article_id"=>1107252, "categories"=>["Biological Sciences"], "users"=>["Yvonne S. Ziegler", "James J. Moresco", "Patricia G. Tu", "John R. Yates III", "Ann M. Nardulli"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0102341.g003", "stats"=>{"downloads"=>0, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Comparison_of_PM_proteomes_shows_similarities_and_differences_among_the_cell_lines_/1107252", "title"=>"Comparison of PM proteomes shows similarities and differences among the cell lines.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-07-16 02:54:46"}
  • {"files"=>["https://ndownloader.figshare.com/files/1596597", "https://ndownloader.figshare.com/files/1596598", "https://ndownloader.figshare.com/files/1596599", "https://ndownloader.figshare.com/files/1596600", "https://ndownloader.figshare.com/files/1596601", "https://ndownloader.figshare.com/files/1596602", "https://ndownloader.figshare.com/files/1596603"], "description"=>"<div><p>The use of broad spectrum chemotherapeutic agents to treat breast cancer results in substantial and debilitating side effects, necessitating the development of targeted therapies to limit tumor proliferation and prevent metastasis. In recent years, the list of approved targeted therapies has expanded, and it includes both monoclonal antibodies and small molecule inhibitors that interfere with key proteins involved in the uncontrolled growth and migration of cancer cells. The targeting of plasma membrane proteins has been most successful to date, and this is reflected in the large representation of these proteins as targets of newer therapies. In view of these facts, experiments were designed to investigate the plasma membrane proteome of a variety of human breast cancer cell lines representing hormone-responsive, ErbB2 over-expressing and triple negative cell types, as well as a benign control. Plasma membranes were isolated by using an aqueous two-phase system, and the resulting proteins were subjected to mass spectrometry analysis. Overall, each of the cell lines expressed some unique proteins, and a number of proteins were expressed in multiple cell lines, but in patterns that did not always follow traditional clinical definitions of breast cancer type. From our data, it can be deduced that most cancer cells possess multiple strategies to promote uncontrolled growth, reflected in aberrant expression of tyrosine kinases, cellular adhesion molecules, and structural proteins. Our data set provides a very rich and complex picture of plasma membrane proteins present on breast cancer cells, and the sorting and categorizing of this data provides interesting insights into the biology, classification, and potential treatment of this prevalent and debilitating disease.</p></div>", "links"=>[], "tags"=>["Biochemistry", "proteomics", "cell biology", "Molecular cell biology", "molecular biology", "oncology", "Cancers and neoplasms", "Breast tumors", "breast cancer", "Basic cancer research", "Cancer detection and diagnosis", "Cancer treatment", "carcinogenesis", "chemistry", "Analytical chemistry", "mass spectrometry", "Electrospray ionization mass spectrometry", "membrane", "cancer", "lines", "identifies", "targets"], "article_id"=>1107266, "categories"=>["Biological Sciences"], "users"=>["Yvonne S. Ziegler", "James J. Moresco", "Patricia G. Tu", "John R. Yates III", "Ann M. Nardulli"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0102341.s001", "https://dx.doi.org/10.1371/journal.pone.0102341.s002", "https://dx.doi.org/10.1371/journal.pone.0102341.s003", "https://dx.doi.org/10.1371/journal.pone.0102341.s004", "https://dx.doi.org/10.1371/journal.pone.0102341.s005", "https://dx.doi.org/10.1371/journal.pone.0102341.s006", "https://dx.doi.org/10.1371/journal.pone.0102341.s007"], "stats"=>{"downloads"=>14, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Plasma_Membrane_Proteomics_of_Human_Breast_Cancer_Cell_Lines_Identifies_Potential_Targets_for_Breast_Cancer_Diagnosis_and_Treatment_/1107266", "title"=>"Plasma Membrane Proteomics of Human Breast Cancer Cell Lines Identifies Potential Targets for Breast Cancer Diagnosis and Treatment", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2014-07-16 02:54:46"}
  • {"files"=>["https://ndownloader.figshare.com/files/1596592"], "description"=>"<p>MHC Class I proteins.</p>", "links"=>[], "tags"=>["Biochemistry", "proteomics", "cell biology", "Molecular cell biology", "molecular biology", "oncology", "Cancers and neoplasms", "Breast tumors", "breast cancer", "Basic cancer research", "Cancer detection and diagnosis", "Cancer treatment", "carcinogenesis", "chemistry", "Analytical chemistry", "mass spectrometry", "Electrospray ionization mass spectrometry"], "article_id"=>1107261, "categories"=>["Biological Sciences"], "users"=>["Yvonne S. Ziegler", "James J. Moresco", "Patricia G. Tu", "John R. Yates III", "Ann M. Nardulli"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0102341.t004", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_MHC_Class_I_proteins_/1107261", "title"=>"MHC Class I proteins.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-07-16 02:54:46"}
  • {"files"=>["https://ndownloader.figshare.com/files/1596591"], "description"=>"<p>Parentheses indicate ambiguity in the protein identification.</p>", "links"=>[], "tags"=>["Biochemistry", "proteomics", "cell biology", "Molecular cell biology", "molecular biology", "oncology", "Cancers and neoplasms", "Breast tumors", "breast cancer", "Basic cancer research", "Cancer detection and diagnosis", "Cancer treatment", "carcinogenesis", "chemistry", "Analytical chemistry", "mass spectrometry", "Electrospray ionization mass spectrometry", "adhesion"], "article_id"=>1107260, "categories"=>["Biological Sciences"], "users"=>["Yvonne S. Ziegler", "James J. Moresco", "Patricia G. Tu", "John R. Yates III", "Ann M. Nardulli"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0102341.t005", "stats"=>{"downloads"=>0, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Cell_adhesion_proteins_/1107260", "title"=>"Cell adhesion proteins.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-07-16 02:54:46"}
  • {"files"=>["https://ndownloader.figshare.com/files/1596588"], "description"=>"<p>Each cell line was analyzed for total number of spectra generated and resulting number of proteins identified.</p>", "links"=>[], "tags"=>["Biochemistry", "proteomics", "cell biology", "Molecular cell biology", "molecular biology", "oncology", "Cancers and neoplasms", "Breast tumors", "breast cancer", "Basic cancer research", "Cancer detection and diagnosis", "Cancer treatment", "carcinogenesis", "chemistry", "Analytical chemistry", "mass spectrometry", "Electrospray ionization mass spectrometry"], "article_id"=>1107257, "categories"=>["Biological Sciences"], "users"=>["Yvonne S. Ziegler", "James J. Moresco", "Patricia G. Tu", "John R. Yates III", "Ann M. Nardulli"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0102341.t001", "stats"=>{"downloads"=>0, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Spectral_count_and_protein_totals_/1107257", "title"=>"Spectral count and protein totals.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-07-16 02:54:46"}
  • {"files"=>["https://ndownloader.figshare.com/files/1596587"], "description"=>"<p>A. For Western analysis, PMs were isolated from each of the cell lines, solubilized in detergent buffer, and fractionated on SDS-PAGE gels. Blots were probed with an ErbB2- or KRT17-specific antibody and imaged with the Licor Infrared Imaging System. Spectral ID numbers and cell lines are indicated for each lane on the blot. B. For immunofluorescence, cells were grown in chamber slides, treated with an antibody to ErbB2 or KRT17 (red), and cell nuclei were stained with DAPI (blue). Cells were examined with confocal microscopy. All scale bars  = 25 µ.</p>", "links"=>[], "tags"=>["Biochemistry", "proteomics", "cell biology", "Molecular cell biology", "molecular biology", "oncology", "Cancers and neoplasms", "Breast tumors", "breast cancer", "Basic cancer research", "Cancer detection and diagnosis", "Cancer treatment", "carcinogenesis", "chemistry", "Analytical chemistry", "mass spectrometry", "Electrospray ionization mass spectrometry", "blots", "immunofluorescence", "reflected", "ms"], "article_id"=>1107256, "categories"=>["Biological Sciences"], "users"=>["Yvonne S. Ziegler", "James J. Moresco", "Patricia G. Tu", "John R. Yates III", "Ann M. Nardulli"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0102341.g005", "stats"=>{"downloads"=>0, "page_views"=>16, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Western_blots_and_immunofluorescence_demonstrate_that_protein_levels_are_accurately_reflected_in_the_MS_data_/1107256", "title"=>"Western blots and immunofluorescence demonstrate that protein levels are accurately reflected in the MS data.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-07-16 02:54:46"}
  • {"files"=>["https://ndownloader.figshare.com/files/1596582"], "description"=>"<p>SK-BR-3 plasma membranes were isolated, and the input (IN), crude nuclear pellet (CNP) which also contained unlysed whole cells, cytosol (CYT), total cellular membranes (TM) which included nuclear, mitochondrial, endoplasmic reticular, and plasma membranes, and purified plasma membranes (PM) were subjected to Western blot analysis. ErbB2 is plasma membrane based, prohibitin is anchored in mitochondrial membranes, lamin A/C is found in nuclear membranes, and calnexin is an endoplasmic reticulum protein. All lanes were loaded at 10 µg protein/lane.</p>", "links"=>[], "tags"=>["Biochemistry", "proteomics", "cell biology", "Molecular cell biology", "molecular biology", "oncology", "Cancers and neoplasms", "Breast tumors", "breast cancer", "Basic cancer research", "Cancer detection and diagnosis", "Cancer treatment", "carcinogenesis", "chemistry", "Analytical chemistry", "mass spectrometry", "Electrospray ionization mass spectrometry", "blots", "purification", "plasma", "membrane", "proteins", "aqueous", "two-phase"], "article_id"=>1107251, "categories"=>["Biological Sciences"], "users"=>["Yvonne S. Ziegler", "James J. Moresco", "Patricia G. Tu", "John R. Yates III", "Ann M. Nardulli"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0102341.g002", "stats"=>{"downloads"=>1, "page_views"=>23, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Western_blots_illustrate_the_purification_of_plasma_membrane_proteins_using_an_aqueous_two_phase_system_/1107251", "title"=>"Western blots illustrate the purification of plasma membrane proteins using an aqueous two-phase system.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-07-16 02:54:46"}
  • {"files"=>["https://ndownloader.figshare.com/files/1596596"], "description"=>"<p>Structural proteins.</p>", "links"=>[], "tags"=>["Biochemistry", "proteomics", "cell biology", "Molecular cell biology", "molecular biology", "oncology", "Cancers and neoplasms", "Breast tumors", "breast cancer", "Basic cancer research", "Cancer detection and diagnosis", "Cancer treatment", "carcinogenesis", "chemistry", "Analytical chemistry", "mass spectrometry", "Electrospray ionization mass spectrometry"], "article_id"=>1107265, "categories"=>["Biological Sciences"], "users"=>["Yvonne S. Ziegler", "James J. Moresco", "Patricia G. Tu", "John R. Yates III", "Ann M. Nardulli"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0102341.t008", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Structural_proteins_/1107265", "title"=>"Structural proteins.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-07-16 02:54:46"}
  • {"files"=>["https://ndownloader.figshare.com/files/1596581"], "description"=>"<p>After establishing an effective method for isolating plasma membrane proteins, representatives from each of the currently defined classes of BC were cultured and plasma membranes were isolated and subjected to MS, yielding a comprehensive list of protein identifications having an FDR ≤1%. These data were biologically validated and the data were mined for relevant protein candidates.</p>", "links"=>[], "tags"=>["Biochemistry", "proteomics", "cell biology", "Molecular cell biology", "molecular biology", "oncology", "Cancers and neoplasms", "Breast tumors", "breast cancer", "Basic cancer research", "Cancer detection and diagnosis", "Cancer treatment", "carcinogenesis", "chemistry", "Analytical chemistry", "mass spectrometry", "Electrospray ionization mass spectrometry", "outlines", "obtaining", "plasma", "membrane", "proteome", "bc"], "article_id"=>1107250, "categories"=>["Biological Sciences"], "users"=>["Yvonne S. Ziegler", "James J. Moresco", "Patricia G. Tu", "John R. Yates III", "Ann M. Nardulli"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0102341.g001", "stats"=>{"downloads"=>0, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Workflow_outlines_process_of_obtaining_plasma_membrane_proteome_of_multiple_BC_cell_lines_/1107250", "title"=>"Workflow outlines process of obtaining plasma membrane proteome of multiple BC cell lines.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-07-16 02:54:46"}
  • {"files"=>["https://ndownloader.figshare.com/files/1596594"], "description"=>"<p>Parentheses indicate ambiguity in the protein identification.</p>", "links"=>[], "tags"=>["Biochemistry", "proteomics", "cell biology", "Molecular cell biology", "molecular biology", "oncology", "Cancers and neoplasms", "Breast tumors", "breast cancer", "Basic cancer research", "Cancer detection and diagnosis", "Cancer treatment", "carcinogenesis", "chemistry", "Analytical chemistry", "mass spectrometry", "Electrospray ionization mass spectrometry"], "article_id"=>1107263, "categories"=>["Biological Sciences"], "users"=>["Yvonne S. Ziegler", "James J. Moresco", "Patricia G. Tu", "John R. Yates III", "Ann M. Nardulli"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0102341.t006", "stats"=>{"downloads"=>0, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_GPCRs_and_G_proteins_/1107263", "title"=>"GPCRs and G proteins.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-07-16 02:54:46"}

PMC Usage Stats | Further Information

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Relative Metric

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