Thermo fischer q exactive orbitrap

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Proteomics (239)
Metabolomics (15)
Unknown (1)

Organisms

Aerococcus urinae NBRC 15544 = CCUG 36881 (237)
Alteromonadales (237)
Bacteria (237)
Canis lupus familiaris (237)
Carya cathayensis (237)
Cnidaria (237)
Ectopseudomonas oleovorans CECT 5344 (237)
Ensifer adhaerens (237)
Enterococcus faecalis (237)
Globicatella sanguinis (237)
Halictus scabiosae (237)
Histomonas meleagridis (237)
Human immunodeficiency virus 1 (237)
Mesocricetus auratus (237)
Methylohalobius crimeensis 10Ki (237)
Mus musculus (237)
Ophrys garganica (237)
Ophrys sphegodes (237)
Pseudomonas aeruginosa SJTD-1 (237)
Rabies virus Nishigahara RCEH (237)
Rattus norvegicus (237)
Rattus rattus (237)
Rhodococcus jostii RHA1 (237)
Rhodopseudomonas palustris (237)
Schizosaccharomyces pombe 927 (237)
Shigella (237)
Staphylococcus aureus (237)
Streptococcus dysgalactiae subsp. equisimilis SK1249 (237)
Streptomyces coelicolor A3(2) (237)
Synechocystis sp. PCC 6803 (237)

Repository

pride (238)
MetaboLights (14)
GNPS (1)
MassIVE (1)

Tissue

Cell culture (34)
Epithelial cell (33)
Blood (10)
Brain (10)
Liver (10)
Blood cell (8)
Skin (8)
Colon (7)
Blood plasma (6)
Dental plaque (6)
Lung (6)
Permanent cell line cell (6)
Cell suspension culture (4)
Heart (4)
Kidney (4)
T cell (4)
B cell (3)
Bone (3)
Bone marrow (3)
Embryonic stem cell (3)
Erythroblast (3)
Hemolymph (3)
Lymphoblast (3)
Pancreas (3)
Pancreatic ductal cell (3)
Umbilical cord blood cell (3)
Whole body (3)
Blood serum (2)
Colon epithelial cell (2)
Colonic epithelium (2)

Disease

Colon cancer (13)
Acute leukemia (6)
Disease free (5)
Lung cancer (5)
Melanoma (4)
Colorectal cancer (3)
Hepatocellular carcinoma (3)
Non-small cell lung carcinoma (3)
Pancreatic ductal carcinoma (3)
Pulmonary tuberculosis (3)
Renal cell carcinoma (3)
Acute myeloid leukemia (2)
Bacterial infectious disease (2)
Breast cancer (2)
Pancreatic cancer (2)
Tuberculosis (2)
Acute pancreatitis (1)
Adenovirus infectious disease (1)
Alzheimer's disease (1)
Anus cancer (1)
Atrial fibrillation (1)
Autosomal recessive disease (1)
Bacterial gastritis (1)
Bacterial sepsis (1)
Brain cancer (1)
Brain glioblastoma multiforme (1)
COVID-19 (1)
Fanconi anemia (1)
Huntington Disease (1)
Merkel cell carcinoma (1)

Technology Type

Mass Spectrometry (238)
Shotgun proteomics (163)
Bottom-up proteomics (28)
Affinity purification coupled with mass spectrometry proteomics (23)
Data-dependent acquisition (14)
Gel-based experiment (12)
Mass spectrometry (11)
Top-down proteomics (10)
Chemical cross-linking coupled with mass spectrometry proteomics (9)
SWATH MS (8)
Mass spectrometry assay (3)
Data-independent acquisition (3)

Instrument Platform

Liquid Chromatography MS - alternating - reverse phase (4)
Exactive (Thermo Scientific) (3)
Liquid Chromatography MS - positive - reverse phase (3)
ACQUITY UPLC (2)
Q-Exactive Plus Orbitrap (Thermo-Fischer) (2)
Liquid Chromatography MS - negative - hilic (2)
Liquid Chromatography MS - negative - reverse phase (2)
Liquid Chromatography MS – positive - reverse phase (1)
Liquid Chromatography MS – negative - hilic (1)
Liquid Chromatography MS - Alternating (LC-MS (Alternating)) (1)
Gas Chromatography MS - positive (1)
Liquid Chromatography MS - negative - hilic-(hydrophilic-interaction-liquid-chromatography)-/-beh-amide (1)
Liquid Chromatography MS - (1)
Liquid Chromatography MS - alternating - hilic (1)
Liquid Chromatography MS - positive - hilic (1)

Publication Date

2021 (43)
2022 (36)
2023 (28)
2019 (27)
2024 (19)
2026 (17)
2018 (17)
2025 (17)
2020 (15)
2017 (12)
2015 (11)
2016 (8)
2014 (2)

CHEBI ID

CHEBI:16708 (4)
CHEBI:16335 (4)
CHEBI:73024 (4)
CHEBI:30776 (4)
CHEBI:17992 (3)
CHEBI:17234 (3)
CHEBI:28875 (3)
CHEBI:15741 (3)
CHEBI:28171 (3)
CHEBI:16865 (3)
CHEBI:17306 (3)
CHEBI:28484 (3)
CHEBI:18012 (3)
CHEBI:32816 (3)
CHEBI:30915 (3)
CHEBI:16737 (3)
CHEBI:16414 (3)
CHEBI:27897 (3)
CHEBI:17191 (3)
CHEBI:15603 (3)
CHEBI:17895 (3)
CHEBI:17295 (3)
CHEBI:17596 (3)
CHEBI:15756 (3)
CHEBI:17368 (3)
CHEBI:30769 (3)
CHEBI:140861 (2)
CHEBI:72387 (2)
CHEBI:28941 (2)
CHEBI:45919 (2)

Metabolite Name

Adenine (4)
Tryptophan (4)
Ornithine (3)
Succinic acid (3)
Fumaric acid (3)
Citric acid (3)
Cytosine (3)
Uridine (3)
1-Aminocyclopropane-1-carboxylic acid (2)
Cysteine (2)
3-Methylcrotonylglycine (2)
Phenol (2)
Pyruvic acid (2)
2-Oxovaleric acid (2)
Histidine (2)
Leucine (2)
Trans-Vaccenic acid (2)
Oxalic acid (2)
Beta-Alanine (2)
Glycine (2)
2-Aminoadipic acid (2)
N-Acetyl-L-aspartic acid (2)
L-Alanine (2)
Capryloylglycine (2)
Muramic acid (2)
Uracil (2)
Valine (2)
Thymine (2)
Medroxyprogesterone (2)
L-Proline (2)

Modification

4-tetrahydrothiazine-3-carboxylic acid (1)

Release Date

2018 (1)

Lab affiliation

Amsterdam UMC, Vrije Universiteit Amsterdam, Medical Oncology, Cancer Center Amsterdam, OncoProteomics Laboratory, Amsterdam, Netherlands (28)
OncoProteomics Laboratory, Dept of Medical Oncology, VU University Medical Center, Amsterdam, The Netherlands (20)
BioArCh, University of York, UK (5)
Department of Biochemistry, University of Oxford (4)
MICALIS Institute Université Paris Saclay, INRAE, AgroParisTech 78350 Jouy-en-Josas France (4)
Sir William Dunn School of Pathology, University of Oxford (4)
Department of Food Science and Technology, Biotechnical Faculty, University of Ljubljana, Ljubljana, Slovenia (3)
1. Department I of Internal Medicine, Center for Integrated Oncology (CIO), Aachen-Bonn- Cologne-Duesseldorf, Excellence Cluster for Cellular Stress Response and Aging-Associated Diseases (CECAD), Center for Molecular Medicine Cologne (CMMC), University of Cologne (UoC), 50937 Cologne, Germany 2. Department of Hematology and Cellular Therapy, University of Leipzig, Leipzig, Germany (2)
BioArCh, University of York, United Kingdom (2)
Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute of Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands (2)
Department of Molecular Biology, Faculty of Science, Radboud Institute for Molecular Life Sciences, Oncode Institute, Radboud University Nijmegen, Nijmegen, The Netherlands. Division of Molecular Genetics, The Netherlands Cancer Institute, Amsterdam, The Netherlands. (2)
Dept. Oncology Pathology, Karolinska Institutet, and Scilifelab, Stockholm, Sweden (2)
Inserm, U1016, Institut Cochin, Paris, France Cnrs, UMR8104, Paris, France Plateforme Proteomique 3P5, Université Paris Descartes, Sorbonne Paris Cité, France. (2)
1. Bioanalytics, Institute of Biotechnology, Technische Universität Berlin, 13355 Berlin, Germany 2. Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH93BF, United Kingdom ( lab head ) (1)
1. Center for Medical Biotechnology, VIB, Ghent, Belgium. 2. Department for Biomolecular Medicine, Ghent University, Ghent, Belgium 3. VIB Proteomics Core, VIB, Ghent, Belgium (1)
1Department of Pathology, Dana-Farber/Harvard Cancer Center, PhD Program in Immunology, Harvard Medical School; Department of Laboratory Medicine, Boston Children's Hospital, Enders Research Building, Room 811, Boston, MA, 02115, USA (1)
AmsterdamUMC, Vrije Universiteit Amsterdam, Medical Oncology, Cancer Center Amsterdam, OncoProteomics Laboratory, Amsterdam, The Netherlands (1)
Assistant Professor Department of Medicine, Division of Endocrinology, Metabolism, and Nutrition Department of Pharmacology and Cancer Biology Duke University Medical Center (1)
Associate Professor, Department of Medicine, Division of Endocrinology, Metabolism, and Nutrition, Department of Pharmacology and Cancer Biology Duke University Medical Center (1)
Associate Professor, HSS Reseach Institute, Weill Cornell Medical College, New York (1)
AstraZeneca (1)
Australian Institute for Bioengineering and Nanotechnology, The University of Queensland (1)
Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, the Netherlands Netherlands Proteomics Centre, Padualaan 8, 3584 CH Utrecht, the Netherlands (1)
CR University Grenoble Alpes, Institute for Biosciences, Inserm U1209, CNRS UMR 5309, 38000 Grenoble, France. (1)
Cancer Program, Monash Biomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC, 3800, Australia (1)
Cancer Research UK and Medical Research Council Oxford Institute for Radiation Oncology, Department of Oncology, University of Oxford, Oxford OX3 7DQ, UK (1)
Cell and Molecular Biology Department, at the University of South Florida (1)
Center for Biochemistry, Medical Faculty, University of Cologne, Joseph-Stelzmann-Str. 52, 50931 Cologne, Germany (1)
Center for Integrative Genomics University of Lausanne Quartier Sorge 1015 Lausanne Switzerland (1)
Centre for Functional Protein Assemblies, Technical University of Munich, Ernst-Otto-Fischer-Straße 8, D-85748 Garching, Germany. (1)

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Palaeoproteomic evidence identifies archaic hominins associated with the Châtelperronian at the Grotte du Renne.

The project aimed to characterize the protein composition from 3 Pleistocene bone specimens (AR-7, AR-16, AR-30). Analysed extracts concern standard ZooMS tryptic digests (AR-7, AR-16, AR-30) and additional palaeoproteomic extracts (AR-30A and AR-30B). The latter concern two biological duplicates. A...

ORGANISM(S): Homo

2016-09-27 | PXD003208 | Pride

Human dental calculus LC-MS/MS

The purpose of this study was to investigate oral microbiome and host proteins in archaeological human dental tissues using a shotgun proteomics approach. The research focuses on dental calculus (mineralized plaque), dentine, a carious lesion, and an alveolar bone abscess from the medieval site of D...

ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) Ovis

2014-01-29 | PXD000412 | Pride

Human Caries Ltq-orbitrap velos Cementum Maxis uhr-qq-tof Medieval Dentine Dental calculus Cattle Abscess Bone Dental plaque Q-exactive hybrid quadrupole orbitrap Sheep Archaeological Periodontitis

Urine metabolomic profiling in two siblings with biallelic pathogenic ATG7 variants with healthy control

Ultra-rare biallelic ATG7 variants were recently reported in five families presenting with neurodevelopmental disorders. Two adult female siblings (P1 and P2) from one family carried compound heterozygous loss-of-function variants (c.1975C>T [p.Arg659]; c.2080-2A>G, 39,40NM_006395.2), resulting in u...

2026-09-30 | MTBLS15856 | MetaboLights

Direct evidence of milk consumption from ancient human dental calculus, UK

This study investigated the consumption of milk products in the archaeological record, utilizing human dental calculus as a reservoir of dietary proteins from archaeological samples from across Eurasia. Protein extraction and generation of tryptic peptides from dental calculus was performed using a ...

ORGANISM(S): Homo sapiens (Human)

2015-02-26 | PXD001362 | Pride

Human Beta-lactoglobulin Dental calculus Dental plaque Lc-ms/ms

Direct evidence of milk consumption from ancient human dental calculus, St Helena

ORGANISM(S): Homo sapiens (Human)

2015-02-25 | PXD001357 | Pride

Human Beta-lactoglobulin Dental calculus Dental plaque Lc-ms/ms

Direct evidence of milk consumption from ancient human dental calculus, northern Europe

ORGANISM(S): Homo sapiens (Human)

2015-02-25 | PXD001361 | Pride

Human Beta-lactoglobulin Dental calculus Dental plaque Lc-ms/ms

Urine analysis of 28 designer benzodiazepines by liquid chromatography-high-resolution mass spectrometry.

Not available

S-EPMC11322785 | biostudies-literature

Direct evidence of milk consumption from ancient human dental calculus, central Europe

ORGANISM(S): Homo sapiens (Human)

2015-02-25 | PXD001360 | Pride

Human Beta-lactoglobulin Dental calculus Dental plaque Lc-ms/ms

Direct evidence of milk consumption from ancient human dental calculus, northern southwest Asia

ORGANISM(S): Homo sapiens (Human)

2015-02-26 | PXD001359 | Pride

Human Beta-lactoglobulin Dental calculus Dental plaque Lc-ms/ms

Acyldepsipeptide probes facilitate specific detection of caseinolytic protease P independent of its oligomeric and activity state

Caseinolytic protease P (ClpP) is a tetradecameric peptidase which assembles with chaperones such as ClpX to gain proteolytic activity. Acyldepsipeptides (ADEPs) represent small molecule mimics of ClpX, which bind into hydrophobic pockets on the apical site of the complex and thereby induce activati...

ORGANISM(S): Staphylococcus aureus

2020-05-26 | PXD015244 | Pride

Thermo fischer q exactive orbitrap Photoaffinity labeling S. aureus

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255 Results

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