histone posttranslational modifications

Show results for

Unknown (427)
Genomics (152)
Transcriptomics (102)
Proteomics (79)
Methylation profiling (9)
Metabolomics (2)
Models (1)
Other (1)
Multiomics (1)

Organisms

Homo sapiens (87)
Mus musculus (46)
Andropogon gerardi (35)
Bacteria (35)
Canis lupus familiaris (35)
Chromatiales bacterium OalgGamma1 (35)
Clavibacter nebraskensis NCPPB 2581 (35)
Cnidaria (35)
Arabidopsis thaliana (30)
Saccharomyces cerevisiae (8)
Drosophila melanogaster (7)
Danio rerio (4)
Rattus norvegicus (4)
Xenopus laevis (3)
Aspergillus nidulans (2)
Petromyzon marinus (2)
synthetic construct (2)
Caenorhabditis elegans (2)
Escherichia coli (2)
Oreochromis mossambicus (2)
Camponotus floridanus (1)
Tetrahymena thermophila (1)
Hordeum vulgare (1)
Human betaherpesvirus 6A (1)
Oikopleura dioica (1)
Solanum lycopersicum (1)
Hepatitis B virus (1)
Manihot esculenta (1)
Mycobacterium tuberculosis (1)
Mycolicibacterium smegmatis MC2 155 (1)

Organisms

Homo sapiens (31)
Mus musculus (23)
Drosophila melanogaster (5)
Arabidopsis thaliana (5)
Xenopus laevis (3)
Petromyzon marinus (2)
Caenorhabditis elegans (2)
Danio rerio (2)
Aspergillus nidulans (1)
Oikopleura dioica (1)
Solanum lycopersicum (1)
Rattus norvegicus (1)

Repository

biostudies-arrayexpress (95)
ENA (89)
geo (82)
pride (35)
MassIVE (22)
iProX (9)
jPOST (5)
PanoramaPublic (5)
MetaboLights (2)
BioModels (1)
EGA (1)

Tissue

Cell culture (16)
Permanent cell line cell (3)
Blood (2)
HeLa cell (2)
Macrophage (2)
B cell (1)
Binucleate (1)
Blood cell (1)
Brain (1)
Burkitt lymphoma cell line (1)
Cerebellar neuron (1)
Embryonic stem cell (1)
Embryonic stem cell line (1)
Heart (1)
Hepatocyte (1)
Liver (1)
Lymphocyte of B lineage (1)
Melanocyte (1)
Myofibroblast cell (1)
Plant cell (1)
Skin (1)
T cell (1)
Trophozoite (1)
Uveal melanoma cell (1)
Whole body (1)

Disease

Cervix carcinoma (2)
Disease free (2)
Benign skin melanocytic nevus (1)
Breast cancer (1)
Burkitt lymphoma (1)
Giardiasis (1)
Liver cancer (1)
Metastatic melanoma (1)
Myocardial ischemia (1)
Prostate cancer (1)
Schizophrenia (1)

Technology Type

Mass Spectrometry (35)
Shotgun proteomics (21)
Affinity purification coupled with mass spectrometry proteomics (5)
Gel-based experiment (4)
Bottom-up proteomics (3)
Chemical cross-linking coupled with mass spectrometry proteomics (2)
Illumina HiSeq 2000, Illumina HiSeq 2500 (1)
Mass spectrometry assay (1)
Mass spectrometry (1)
All-ion fragmentation (1)
Data-dependent acquisition (1)
Data-independent acquisition (1)
Mass spectrometry imaging (1)
SRM/MRM (1)
SWATH MS (1)

Instrument Platform

Q Exactive (8)
Illumina NovaSeq 6000 (7)
LTQ Orbitrap Velos (3)
Orbitrap Fusion Lumos (3)
LTQ Orbitrap Elite (2)
LTQ Velos (2)
ZenoTOF 7600 (2)
Illumina HiSeq 2000 (1)
Orbitrap Eclipse (1)
Orbitrap Exploris (1)
Orbitrap Exploris 240 (1)
Orbitrap Fusion (1)
Orbitrap Q Exactive (1)
Q Exactive HF (1)
Q Exactive Plus (1)
TripleTOF 5600 (1)
Liquid Chromatography MS - negative - hilic (1)
Liquid Chromatography MS - positive - hilic (1)
Liquid Chromatography MS - negative - reverse phase (1)

Publication Date

2011 (32)
2025 (24)
2024 (24)
2012 (22)
2015 (16)
2014 (16)
2013 (15)
2021 (12)
2016 (11)
2026 (11)
2022 (11)
2020 (10)
2019 (9)
2017 (7)
2010 (7)
2023 (7)
2008 (6)
2018 (4)
2009 (1)
2007 (1)

Metabolite Name

Thr-Pro-Arg (1)
Thr-Gly-Arg (1)
Ser-Asp-Arg (1)
Pyroglu-Asn-Arg (1)
L-valine, n-[[1-(5-fluoropentyl)-1h-indol-3-yl]carbonyl]-, methyl ester (1)
Cys-His-Arg (1)
5-methoxy-4-methyl-3-phenylcoumarin (1)
4-phenylbutan-2-ol (1)
3-quinolinecarboxamide, 1,4-dihydro-8-methoxy-4-oxo-1-pentyl-n-tricyclo[3.3.1.13,7]dec-1-yl- (1)
2-methyl-6(s)-(3-pyridyl)tetrahydro-1,2-oxazine (1)
2-furancarboxylic acid, 5-[3-[4-[2-(4-fluorophenyl)ethoxy]phenyl]propyl]- (1)
1h-indole-3-carboxylic acid, 1-(5-fluoropentyl)-, 8-quinolinyl ester (1)
[1,1':4',1''-terphenyl]-3,4'',5-triol (1)
[[4-[5r-chloro-2z-[3r-cyclohexyl-3s-hydroxy-1r-propenyl]-3s-hydroxycyclopentyl]-2r-butenyl]oxy]-acetic acid, isopropyl ester (1)
(s)-n-(1-amino-1-oxo-3-phenylpropan-2-yl)-1-pentyl-1h-indole-3-carboxamide (1)
(3as,5r,5as,8as,9ar)-5,8a-dimethyl-1-methylidene-3a,4,5,5a,6,7,9,9a-octahydroazuleno[6,7-b]furan-2,8-dione (1)
L-myo-inositol-1,4,5-triphosphate (1)
Arg-asp (1)
2-hdeahpda [dmed-fahfa] (1)
Mepirapim (1)
Tyr-His-Arg (1)
Solasodine base + 2h, 1o, o-hex-hex-hex (1)
Cyanidin 3-o-[2''-o-(xylosyl)-6''-o-(p-o-(glucosyl)-p-coumaroyl) glucoside] 5-o-glucoside (1)
Combrestatin a4 (1)
6-oxomometasone furoate (1)
(z)-2-octylpent-2-enedioic acid (1)
Cocamidoprpylbetaine (1)
Ser-Ser-Arg (1)
Glycerol trioleate (1)
.alpha.-galactosyl-n-stearoylsphingosine (1)

IsPrivate

False (1)

First Public Date

2024 (13)
2026 (11)
2014 (11)
2025 (9)
2013 (9)
2019 (8)
2015 (7)
2022 (5)
2017 (4)
2016 (4)
2023 (3)
2021 (3)
2020 (2)

Classification

fungi (1)

Modelling Approach

Differential equation model (1)

Modification

N6 (3)
3x(2)H labeled N6-acetyl-L-lysine (1)
N6-dimethyl-L-lysine (1)

Study type

ChIP-chip by tiling array (24)
Transcription profiling by array (21)
ChIP-seq (19)
Methylation profiling by array (6)
RNA-seq of coding RNA (6)
Methylation profiling by high throughput sequencing (5)
Hi-C (2)
Proteomic profiling by array (2)
GRO-seq (1)
Unknown experiment type (1)
ChIP-chip by array (1)
Comparative genomic hybridization by array (1)
ATAC-seq (1)
Other (1)
DNA-seq (1)
CUT&RUN (1)
RNA-seq of total RNA (1)
RNA-seq of non coding RNA (1)

Release Date

2011 (45)
2021 (39)
2012 (34)
2015 (33)
2022 (31)
2016 (30)
2014 (30)
2018 (30)
2019 (29)
2013 (27)
2023 (26)
2020 (26)
2025 (24)
2008 (22)
2024 (21)
2017 (21)
2010 (18)
2007 (10)
2009 (8)
2006 (8)
2005 (3)
2026 (2)
2002 (2)
2004 (1)
2003 (1)

Lab affiliation

Epigenetics Program, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania (4)
Department of Biology – Cellular Proteostasis and Mass Spectrometry, University of Konstanz (3)
ProGenTomics, Laboratory of Pharmaceutical Biotechnology, Ghent University, B-9000 Ghent, Belgium (2)
1 Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic 2 Faculty of Science, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic (1)
1 Population Health and Immunity Division, The Walter and Eliza Hall Institute of Medical Research, Melbourne, VIC, Australia Department of Veterinary Biosciences, Melbourne Veterinary School, Faculty of Veterinary and Agricultural Sciences, The University of Melbourne, Parkville, VIC, Australia (1)
Biomedical Center Munich Molecular Biology Großhaderner Strasse 9 82152 Planegg-Martinsried (1)
CEITEC Masaryk University (1)
Department of Biochemistry and Molecular Biology University of Arkansas for Medical Sciences USA (1)
Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, AR 72205, USA Arkansas Children’s Research Institute, 13 Children’s Way, Little Rock, AR 72202, USA (1)
Department of Peptide-based Immunotherapy, University and University Hospital Tübingen, Tübingen, Germany (lab head) (1)
Division of Gastroenterology and Hepatology; Shanghai Institute of Digestive Disease; NHC Key Laboratory of Digestive Diseases; State Key Laboratory for Oncogenes and Related Genes; Renji Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai 200001, China (1)
Dr. rer. nat. Birgit Knebel Institute for Clinical Biochemistry and Pathobiochemistry German Diabetes Center (DDZ) Leibniz Center for Diabetes Research at Heinrich Heine University Düsseldorf Auf´m Hennekamp 65 40225 Düsseldorf, Germany (1)
European Institute of Oncology, Milan (1)
Functional Proteo-Metabolomics Department of Biochemistry University of Innsbruck Austria (1)
Hainan Normal University (1)
Huazhong University of Science and Technology (1)
Institute of Molecular Biology (IMB), Germany (1)
Key Laboratory of Animal Infectious Diseases in Northeast China, Ministry of Education; Key Laboratory of Zoonosis, Shenyang Agricultural University, 120 Dongling Road, Shenyang 110166, China. (1)
Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing 100191, China (1)
Laboratório de Pesquisa em Apicomplexa - Instituto Carlos Chagas – FIOCRUZ/PR. (1)
Protein Analysis Unit ZfP LMU Munich BioMedical Center Grosshaderner Strasse 9 82152 Planegg-Martinsried Tel. +49 89 2180 71804 (1)
Quantitative Proteomics Ackermannweg 4 55122 Mainz Germany (1)
Raymond H. Wittcoff Distinguished Professor and Head Department of Biochemistry and Molecular Biophysics Washington University School of Medicine St. Louis, MO 63110 (1)
Shenyang Agricultural University (1)
Shohei Koide Professor and Chair, Department of Biochemistry and Biophysics Box 712, Rm 3-6710 University of Rochester Medical Center 601 Elmwood Ave Rochester, NY 14642 (1)
Tsinghua University (1)
University of Minnesota at Twin Cities (1)
University of Sheffield (1)
Verna & Marrs McLean Department of Biochemistry & Molecular Biology Department of Molecular and Cellular Biology Baylor College of Medicine (1)

Previous page
1 / 78
You're on page 1
page 2
page 3
page 4
page 5
page ...
page 78
Next page

Sort by:

Relevance

Page size

Posttranslational modification analysis of Histone H3t

Comprehensive posttranslational modifications in the testis-specific histone variant H3t protein validated in tagged knock-in mice.

ORGANISM(S): Mus Musculus (mouse)

2024-09-13 | PXD052428 | JPOST Repository

Histone serotonylation promotes pancreatic cancer development via lipid metabolism remodeling

Neurotransmitter serotonin (5-hydroxytryptamine [5-HT]) has emerged to play parallel roles in both neurobiology and oncology. Apart from receptor-mediated signaling transduction pattern, serotonin can be covalently integrated into histone (the post-translational modification known as histone sero...

2025-06-13 | MTBLS12569 | MetaboLights

Environmental Conditions Elicit a Slow but Enduring Response of Histone Post-Translational Modifications in Mozambique Tilapia

Histone post-translational modifications (PTMs) are epigenetic marks that operate within the central dogma of molecular biology: upon an environmental stimulus, the histone PTMs surrounding DNA can be changed in a way that modifies gene expression, and, therefore, the abundance and composition of RN...

ORGANISM(S): Oreochromis Mossambicus

2024-12-10 | PXD042718 | panorama

Data for: A practical guide for analysis of histone post-translational modifications by mass spectrometry: best practices and pitfalls

Histone proteomics from 5 human cell lines, discussed in publication: "A practical guide for analysis of histone post-translational modifications by mass spectrometry: best practices and pitfalls". Further explanation of data types, methods, and analysis are available in Data Explanation document in...

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

MSV000084298 | MassIVE

Nitric oxide regulates gene expression in cancers by controlling histone posttranslational modifications [HiSeq 2000]

Dynamic changes in histone posttranslational modifications (PTMs) are important regulators of chromatin structure and gene transcription in both normal and disease settings. Herein, we describe a novel signaling mechanism of nitric oxide (â€¢NO) by demonstrating its ability to modulate gene expressi...

ORGANISM(S): Homo sapiens

2015-11-05 | E-GEOD-66318 | biostudies-arrayexpress

Pathology tissue-quantitative mass spectrometry analysis to profile histone post-translational modification patterns in patient samples

Histone post-translational modifications (hPTMs) generate a complex combinatorial code that has been implicated with various pathologies, including cancer. Dissecting such a code in physiological and diseased states may be exploited for epigenetic biomarker discovery, but hPTM analysis in clinical s...

ORGANISM(S): Homo Sapiens (ncbitaxon:9606) Mus Musculus (ncbitaxon:10090)

2016-08-25 | MSV000080100 | MassIVE

Development of a high-throughput (10 minute microflow gradient) platform for quantitation of histone modifications on a new QTOF instrument

Histone post-translational modifications (PTMs) regulate gene expression patterns through epigenetic mechanisms. The 5 histone proteins (H1, H2A, H2B, H3, and H4) are extensively modified, with over 75 distinct modification types spanning more than 200 sites. Despite strong advances in mass spectrom...

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

2024-05-06 | MSV000094696 | MassIVE

Development of a high-throughput (10 minute microflow gradient) platform for quantitation of histone modifications on a new QTOF instrument

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

2024-05-06 | MSV000094695 | MassIVE

Fine mapping of posttranslational modifications of the linker histone H1 from Drosophila melanogaster.

Not available

S-EPMC2212714 | biostudies-literature

Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification

We report the identification of 67 previously undescribed histone modifications, increasing the current number of known histone marks by about 70%. We further investigated one of the marks, lysine crotonylation (Kcr), confirming that it represents an evolutionarily-conserved histone posttranslationa...

ORGANISM(S): Mus musculus

2011-10-06 | E-GEOD-32663 | biostudies-arrayexpress

Previous page
1 / 78
You're on page 1
page 2
page 3
page 4
page 5
page ...
page 78
Next page

Sort by:

Relevance

Page size

773 Results

Show results for

Organisms

Organisms

Repository

Tissue

Disease

Technology Type

Instrument Platform

Publication Date

Metabolite Name

IsPrivate

First Public Date

Classification

Modelling Approach

Modification

Study type

Release Date

Lab affiliation

Tags

OmicsDI is part of the ELIXIR infrastructure

Tweets