Analysis of liver, heart, spleen and lung
Ontology highlight
ABSTRACT:
ORGANISM(S): Mus musculus
PROVIDER: GSE2148 | GEO | 2005/02/12
SECONDARY ACCESSION(S): PRJNA91405
REPOSITORIES: GEO
Similar Datasets
Project description:Analysis of liver, heart, spleen and lung
2008-06-12 | E-GEOD-2148 | biostudies-arrayexpress
Project description:Cy3-labeled cDNA obtained from four pools of three hearts of neonatal C57BL Cx43 null mice were compared to Cy3-labeled cDNA obtained from four pools of three hearts of neonatal C57BL wildtype mice through Cy5-labeled sample reference prepared at once for the entire experiment from aorta, brain, heart, kidney, liver, lung, ovary/testicles, spleen, and stomach - equal amounts from adult male and female C57BL mice. Keywords = Cx32 null vs wildtype neonatal mouse heart
2010-06-05 | E-GEOD-1961 | biostudies-arrayexpress
Project description:Spleen total RNA (Catalog #64044-1) and liver total RNA (Catalog #64042-1) were purchased from Clontech and used as the starting material. Spleen was labeled with Cyanine-3 (Green) while liver was labeled with Cyanine-5 (Red). cRNA was made by the single round amplification method. Keywords: repeat sample
2003-03-07 | GSE334 | GEO
Project description:Spleen total RNA (Catalog #64044-1) and liver total RNA (Catalog #64042-1) were purchased from Clontech and used as the starting material. Spleen was labeled with Cyanine-3 (Green) while liver was labeled with Cyanine-5 (Red). cRNA was made by the double round amplification method. Keywords: repeat sample
2003-03-06 | GSE331 | GEO
Project description:Spleen total RNA (Catalog #64044-1) and liver total RNA (Catalog #64042-1) were purchased from Clontech and used as the starting material. Spleen was labeled with Cyanine-3 (Green) while liver was labeled with Cyanine-5 (Red). cRNA was made by the single round amplification method. Keywords: repeat sample
2003-03-06 | GSE330 | GEO
Project description:Cy3-labeled cDNA obtained from four pools of three hearts of neonatal C57BL Cx43 null mice were compared to Cy3-labeled cDNA obtained from four pools of three hearts of neonatal C57BL wildtype mice through Cy5-labeled sample reference prepared at once for the entire experiment from aorta, brain, heart, kidney, liver, lung, ovary/testicles, spleen, and stomach - equal amounts from adult male and female C57BL mice. Keywords = Cx32 null vs wildtype neonatal mouse heart Keywords: parallel sample
2004-11-13 | GSE1961 | GEO
Project description:Proteins are ubiquitously modified with glycans of varied chemical structures via distinct glycosidic linkages, making the landscape of protein glycosylation challenging to map. Profiling of intact glycopeptides with mass spectrometry (MS) has recently emerged as a powerful tool for revealing matched information of the glycosylation sites and attached glycans (i.e., intact glycosites), which, however, is largely limited to individual glycosylation types. Here, we develop Click-iG, which integrates metabolic labeling of glycans with clickable unnatural sugars, an optimized MS method, and a tailored version of pGlyco3 software to enable simultaneous enrichment and profiling of three types of—N-linked, O-linked, and O-GlcNAcylated—intact glycopeptides. We demonstrated Click-iG by identification of thousands of intact glycosites in cell lines and living mice. From the mouse lung, heart, and spleen, a total of 547 N-glycosylation sites with 161 glycan compositions, 198 O-glycosylation sites with 262 glycans, and 1,947 O‑GlcNAcylation sites were identified. The Click-iG-enabled unprecedent coverage on the protein glycosylation landscape lays the foundation for interrogating crosstalk between different glycosylation pathways.
2025-02-12 | PXD039144 | Pride
Project description:Proteins are ubiquitously modified with glycans of varied chemical structures via distinct glycosidic linkages, making the landscape of protein glycosylation challenging to map. Profiling of intact glycopeptides with mass spectrometry (MS) has recently emerged as a powerful tool for revealing matched information of the glycosylation sites and attached glycans (i.e., intact glycosites), which, however, is largely limited to individual glycosylation types. Here, we develop Click-iG, which integrates metabolic labeling of glycans with clickable unnatural sugars, an optimized MS method, and a tailored version of pGlyco3 software to enable simultaneous enrichment and profiling of three types of—N-linked, O-linked, and O-GlcNAcylated—intact glycopeptides. We demonstrated Click-iG by identification of thousands of intact glycosites in cell lines and living mice. From the mouse lung, heart, and spleen, a total of 547 N-glycosylation sites with 161 glycan compositions, 198 O-glycosylation sites with 262 glycans, and 1,947 O‑GlcNAcylation sites were identified. The Click-iG-enabled unprecedent coverage on the protein glycosylation landscape lays the foundation for interrogating crosstalk between different glycosylation pathways.
2025-02-12 | PXD036339 | Pride
Project description:Proteins are ubiquitously modified with glycans of varied chemical structures via distinct glycosidic linkages, making the landscape of protein glycosylation challenging to map. Profiling of intact glycopeptides with mass spectrometry (MS) has recently emerged as a powerful tool for revealing matched information of the glycosylation sites and attached glycans (i.e., intact glycosites), which, however, is largely limited to individual glycosylation types. Here, we develop Click-iG, which integrates metabolic labeling of glycans with clickable unnatural sugars, an optimized MS method, and a tailored version of pGlyco3 software to enable simultaneous enrichment and profiling of three types of—N-linked, O-linked, and O-GlcNAcylated—intact glycopeptides. We demonstrated Click-iG by identification of thousands of intact glycosites in cell lines and living mice. From the mouse lung, heart, and spleen, a total of 547 N-glycosylation sites with 161 glycan compositions, 198 O-glycosylation sites with 262 glycans, and 1,947 O‑GlcNAcylation sites were identified. The Click-iG-enabled unprecedent coverage on the protein glycosylation landscape lays the foundation for interrogating crosstalk between different glycosylation pathways.
2025-02-12 | PXD036190 | Pride