Basic ph reversed phase

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Proteomics (646)
Transcriptomics (16)
Unknown (10)
Metabolomics (4)
Genomics (3)
Multiomics (1)

Organisms

Schizosaccharomyces pombe (635)
Oryza sativa Indica Group (635)
Sinorhizobium meliloti BL225C (635)
Sus scrofa domesticus (635)
Ostreococcus tauri (635)
Saccharomyces cerevisiae (635)
Staphylococcus aureus (635)
Rattus norvegicus (635)
Escherichia coli (635)
Cyanophora paradoxa (635)
Entamoeba histolytica (635)
Physcomitrium patens (635)
Methylohalobius crimeensis 10Ki (635)
Homo sapiens (635)
Shigella flexneri (635)
Ctenopharyngodon idella (635)
Danio rerio (635)
Allexis (635)
Shigella (635)
Pseudomonas putida KT2440 (635)
Zea mays (635)
Meleagris gallopavo (635)
Medicago truncatula (635)
Histomonas meleagridis (635)
Pseudomonas fluorescens WH6 (635)
Homo sapiens (6)
Schizosaccharomyces pombe (4)
Saccharomyces cerevisiae (3)
Mus musculus (3)
Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344 (2)

Repository

pride (635)
biostudies-arrayexpress (19)
MassIVE (10)
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jPOST (1)

Tissue

Cell culture (116)
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Disease

Breast cancer (25)
Disease free (18)
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Cardiovascular system disease (8)
Alzheimer's disease (8)
Type 2 diabetes mellitus (7)
Melanoma (6)
Parkinson's disease (6)
Malignant neoplasm of ovary (6)
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COVID-19 (5)
Colon cancer (5)
Acute leukemia (5)
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Obesity (3)
Pancreatic cancer (3)
Kidney cancer (3)
Aortic valve stenosis (2)
Meniere's disease (2)
Endocervical adenocarcinoma (2)
Diabetes mellitus (2)
Lung small cell carcinoma (2)
Skin melanoma (2)
Congenital disorder of glycosylation (2)
Prostate adenocarcinoma (2)
Multiple myeloma (2)
Neuroblastoma (2)

Technology Type

Mass Spectrometry (635)
Shotgun proteomics (402)
Bottom-up proteomics (123)
Data-dependent acquisition (80)
Affinity purification coupled with mass spectrometry proteomics (49)
Data-independent acquisition (22)
SWATH MS (20)
Gel-based experiment (20)
Top-down proteomics (17)
SRM/MRM (6)
Mass spectrometry (4)
Affinity proteomics (4)
All-ion fragmentation (2)
Chemical cross-linking coupled with mass spectrometry proteomics (2)
Immunopeptidomics (1)
DiaPASEF (1)

Instrument Platform

Orbitrap Fusion Lumos (5)
Orbitrap Fusion (4)
Q Exactive (2)
Scanning hardware (1)
TripleTOF 5600 (1)
Q Exactive HF (1)
Liquid Chromatography MS (1)
Liquid Chromatography MS - Alternating (LC-MS (Alt)) (1)
Liquid Chromatography MS - positive - reverse phase (1)
LCQ Deca XP Plus (1)

Publication Date

2025 (95)
2022 (87)
2024 (84)
2023 (78)
2026 (74)
2020 (69)
2021 (61)
2019 (40)
2018 (25)
2017 (15)
2015 (11)
2016 (9)
2014 (7)
2013 (6)
2012 (4)
2011 (1)
2010 (1)
2007 (1)
2004 (1)

CHEBI ID

CHEBI:18344 (3)
CHEBI:46966 (2)
CHEBI:83058 (2)
CHEBI:45441 (2)
CHEBI:28733 (2)
CHEBI:48430 (2)
CHEBI:46961 (2)
CHEBI:5623 (2)
CHEBI:36313 (2)
CHEBI:30865 (2)
CHEBI:16244 (2)
CHEBI:15728 (2)
CHEBI:16958 (2)
CHEBI:16610 (2)
CHEBI:17015 (2)
CHEBI:30746 (2)
CHEBI:16566 (2)
CHEBI:116314 (2)
CHEBI:15940 (2)
CHEBI:4047 (2)
CHEBI:35932 (2)
CHEBI:16919 (2)
CHEBI:15354 (2)
CHEBI:17295 (2)
CHEBI:64563 (2)
CHEBI:17368 (2)
CHEBI:30769 (2)
CHEBI:176837 (1)
CHEBI:176836 (1)
CHEBI:176835 (1)

Metabolite Name

3-ketosphinganine (2)
Indoleacetaldehyde (2)
Kynurenic acid (2)
Glycerophosphocholine (2)
L-Phenylalanine (2)
Quercetin-3-glucuronide (1)
Pterostilbene (1)
Aesculetin (1)
Hydroquinone beta-D-glucopyranoside (1)
4-quinolinecarboxylic acid (1)
Chrysoeriol (1)
Salidroside (1)
Harmane (1)
5-hydroxymethylfurfural (1)
Val-leu-pro-val-pro-gln (1)
Serine-Cholic Acid (1)
5beta-Cholanic acid-3alpha,12alpha-diol-7-one (1)
5beta-Cholanic acid-3alpha-OL-6,7-dione (1)
5beta-Cholanic acid-3alpha-OL-7,12-dione (1)
Pro Phe Ile (1)
(R)-4-((8S,9S,10R,13R,14S,17R)-10,13-dimethyl-3-oxo-2,3,6,7,8,9,10,11,12,13,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-17-yl)pentanoic acid (1)
13,14-dihydro-19-hydroxyPGE1 (1)
15,19-hydroxy Prostaglandin E1 (1)
Met Pro Leu (1)
Docosahexaenoic Acid ethyl ester (1)
Adenosine 3'-monophosphate (3'-AMP) (1)
1-[2-[3-(1-propan-2-ylsulfonylazetidin-3-yl)-1,2,4-oxadiazol-5-yl]pyrrolidin-1-yl]ethanone (1)
2-(1-acetylpiperidin-4-yl)-1-(3-ethyl-3-hydroxy-7-azaspiro[3.5]nonan-7-yl)ethanone (1)
Val Pro Ile (1)
Ile Pro Pro (1)

Modification

N6 (2)
N6-dimethyl-L-lysine (2)
Not available (2)
26.01565 (1)
-17.026549 (1)
42.010565 (1)
15.994915 (1)
2x(15)N labeled L-lysine (1)
4x(15)N labeled L-arginine (1)
57.021464 (1)
4-tetrahydrothiazine-3-carboxylic acid (1)

Study type

Transcription profiling by array (7)
Other (5)
ChIP-seq (3)
Unknown experiment type (1)
RIP-chip by array (1)
ChIP-chip by tiling array (1)
ChIP-chip by array (1)

Release Date

2015 (5)
2013 (5)
2014 (3)
2023 (3)
2012 (2)
2024 (2)
2021 (2)
2011 (1)
2010 (1)
2007 (1)
2004 (1)
2025 (1)
2019 (1)
2017 (1)

Lab affiliation

Basic Immune System of Plants / Protein Mass Spectrometry Max Planck Institute for Plant Breeding Research Carl-von-Linne-Weg 10, 50829 Cologne, Germany (30)
Associate Member, St. Jude Faculty Developmental Neurobiology St. Jude Children's Research Hospital Memphis, TN-38105 (10)
Associate Member Developmental Neurobiology St. Jude Children's Research Hospital (9)
Harvard Medical School (9)
Moffitt Cancer Center Tampa, FL, USA (8)
The Wilmer Eye Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland 21287 USA (7)
David H. Koch Institute for Integrative Cancer Research Howard Hughes Medical Institute Massachusetts Institute of Technology Cambridge, MA 02139, USA (6)
Finley and Gygi lab Cell Biology Department Harvard Medical School US (6)
Proteomics Core Facility, University of Gothenburg (5)
Medical University of Vienna (5)
Institute of Bioinformatics , International Technology Park, Bangalore, India (4)
Department of Clinical Science, University of Bergen, Norway (4)
Professor. Department of Biology and Biological Engineering, Chalmers University of Technology, SE-41296 Gothenburg, Sweden; Wallenberg Center for Protein Research, Chalmers University of Technology, SE-41296 Gothenburg, Sweden; Novo Nordisk Foundation Center for Biosustainability, Chalmers University of Technology, SE-41296 Gothenburg, Sweden; Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, DK-2800 Lyngby, Denmark (4)
Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, Rhode Island, USA (4)
Department of Laboratory Medicine and Pathology, Mayo Clinic, Rochester, Minnesota 55905, United States (4)
Department of Laboratory Medicine and Pathology Mayo Clinic, Rochester, Minnesota 55905 United States (4)
Drug Discovery Moffitt Cancer Center Tampa, FL, USA (4)
Department of Cell Biology, Harvard Medical School, Boston, MA, USA (4)
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX, USA. (3)
Dana-Farber Cancer Institute and Harvard Medical School (3)
Institut für Mikrobiologie, Universität Greifswald, Felix-Hausdorff-Str. 8, 17489 Greifswald (3)
Dpt. of Immunobiology University of Lausanne (UNIL), Boveresses 155 CH-1066 Epalinges (3)
Instituto de Investigación Sanitaria del Principado de Asturias (ISPA), Oviedo, Spain (3)
Molecular Oncology Chemical Biology and Molecular Medicine Moffitt Cancer Center (3)
University of Washington (3)
Department of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth (2)
Harvard Medical School Department of Cell Biology Harvard Medical School Boston, MA, USA (2)
CCBIO, Department of Clinical Medicine, Faculty of Medicine, University of Bergen, Bergen, Norway (2)
iBiMED – Institute of Biomedicine, Department of Medical Sciences, University of Aveiro, Aveiro, Portugal; UnIC – Unidade de Investigação Cardiovascular, Departamento de Cirurgia e Fisiologia, Faculdade de Medicina da Universidade do Porto, Porto, Portugal (2)
Institute of genetics and developmental biology (2)

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Enhancing proteome coverage by using strong anion exchange in tandem with basic-pH reversed-phase chromatography for sample multiplexing-based proteomics

Sample multiplexing-based proteomic strategies rely on fractionation to improve proteome coverage. Tandem mass tag (TMT) experiments, for example, can currently accommodate up to 18 samples with proteins spanning several orders of magnitude, thus necessitating fractionation to achieve reasonable pro...

ORGANISM(S): Homo sapiens (Human)

2023-12-28 | PXD044393 | Pride

Retention time calibration for RP-HPLC at pH 9

The change in pH of the mobile phase drastically changes the retention mechanism of peptides, rendering currently available retention time prediction models useless. The aim of this study is to create a dataset of peptide retention times under basic (pH 9) HPLC conditions, allowing for the creation ...

ORGANISM(S): Homo sapiens (Human)

2026-02-13 | PXD064311 | Pride

Hela Basic ph Rp-hplc

Human pancreatic endocrine cells, LC-MS3

FACS isolated human alpha and beta cells were analyzed by TMT 11-plex labeling, Off-line basic pH reversed phase fractionation and LC-MS3 on an Orbitrap Fusion mass spectrometer.

ORGANISM(S): Homo sapiens (Human)

2019-02-15 | PXD011933 | Pride

Human Endocrine cells Tmt 11-plex Lc-ms3

Enhancing Proteome Coverage by Using Strong Anion-Exchange in Tandem with Basic-pH Reversed-Phase Chromatography for Sample Multiplexing-Based Proteomics.

Not available

S-EPMC11090996 | biostudies-literature

Finding the best column for polar basic analytes across reversed-phase and hydrophilic interaction liquid chromatography.

Not available

S-EPMC11867270 | biostudies-literature

Proteome analysis by charge state-selective separation of peptides: a multidimensional approach

Multidimensional peptide fractionation is widely used in proteomics to reduce the complexity of peptide mixtures prior to mass spectrometric analysis. Here, we describe the sequential use of strong cation exchange and reversed phase liquid chromatography in both basic and acidic pH buffers for separ...

ORGANISM(S): Mus musculus (Mouse)

2013-11-27 | PXD000210 | Pride

Lc-msms Rp-hplc basic ph Mouse Scx

Prediction of the n-Octanol/Water Partition Coefficients of Basic Compounds Using Multi-Parameter QSRR Models Based on IS-RPLC Retention Behavior in a Wide pH Range.

Not available

S-EPMC10005301 | biostudies-literature

Characterization of MS white matter derived extracellular vesicles

This dataset contains proteomic profiles of extracellular vesicles (EVs) isolated from human multiple sclerosis (MS) white matter tissue, alongside the corresponding tissue proteome. The aim of this study is to characterize the protein cargo of MS-derived EVs compared to bulk tissue and to identify ...

ORGANISM(S): Homo sapiens (Human)

2025-11-17 | PXD068695 | Pride

Human brain

Reverse-phase liquid chromatography (RPLC) in Combination with Tip-Based Strong Cation Exchange (SCX-Tip) Fractionation, ReST, an Alternative Approach for Cross-linked Peptides analysis

Chemical cross-linking in combination with mass spectrometry (XL-MS) has emerged as a useful method for structural elucidation of proteins and protein complexes. Efficient enrichment procedures are necessary to analyze cross-linked products due to their relatively low abundance. Currently, strong ca...

ORGANISM(S): Homo sapiens (Human)

2022-06-16 | PXD023817 | Pride

Scx-tip Mass spectrometry Fractionation Chemical cross-linking

Effect of gemfibrozil on yeast proteome

DDA from 6 basic-pH reversed phase of S. cerevisiae. DIA-based quantification of effects of gemfibrozil on yeast for 2 hours or 20 hours.

ORGANISM(S): Saccharomyces Cerevisiae (ncbitaxon:4932)

2018-07-31 | MSV000082675 | MassIVE

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