Hemoglobin subunit

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Instrument Platform

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2025 (31)
2014 (28)
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CHEBI ID

CHEBI:176874 (2)
CHEBI:58530 (2)
CHEBI:64260 (2)
CHEBI:18299 (2)
CHEBI:9068 (2)
CHEBI:80624 (2)
CHEBI:176875 (2)
CHEBI:16752 (2)
CHEBI:34159 (2)
CHEBI:17160 (2)
CHEBI:17540 (2)
CHEBI:16352 (2)
CHEBI:36761 (2)
CHEBI:32798 (2)
CHEBI:16231 (2)
CHEBI:15655 (2)
CHEBI:28792 (2)
CHEBI:33283 (2)
CHEBI:27082 (2)
CHEBI:29042 (2)
CHEBI:28997 (2)
CHEBI:60175 (2)
CHEBI:70958 (2)
CHEBI:16192 (2)
CHEBI:28689 (2)
CHEBI:139123 (2)
CHEBI:62084 (2)
CHEBI:16024 (2)
CHEBI:16556 (2)
CHEBI:48430 (2)

Metabolite Name

Niacinamide (3)
5-Hydroxylysine (3)
Spermidine (3)
L-Isoleucine (3)
L-Leucine (3)
L-Methionine (3)
6-Amino-6-deoxyfutalosine (2)
Indoleglycerol phosphate (2)
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IMP (2)
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Betaine (2)
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Thymine (2)
Thiamine (2)
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Saccharopine (2)

First Public Date

2026 (6)
2023 (6)
2020 (3)
2021 (2)
2017 (2)
2014 (2)
2024 (1)

Study type

Transcription profiling by array (82)
RNA-seq of coding RNA (33)
ChIP-seq (31)
RNA-seq of coding RNA from single cells (30)
Methylation profiling by high throughput sequencing (15)
Unknown experiment type (8)
Other (8)
ChIP-chip by tiling array (5)
Comparative genomic hybridization by array (4)
RNA-seq of total RNA (2)
Genotyping by array (1)
Spatial transcriptomics by high-throughput sequencing (1)
RIP-seq (1)
Methylation profiling by array (1)
CUT&RUN (1)
RNA-seq of non coding RNA (1)

Release Date

2025 (41)
2015 (33)
2014 (33)
2010 (31)
2022 (31)
2013 (29)
2026 (26)
2021 (25)
2012 (24)
2016 (23)
2020 (20)
2017 (19)
2011 (18)
2023 (16)
2024 (15)
2009 (12)
2008 (12)
2019 (10)
2018 (9)
2007 (7)
2006 (5)
2005 (2)
2004 (2)
2003 (2)
2002 (1)
2001 (1)
1999 (1)
1996 (1)

Lab affiliation

Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, and Netherlands Proteomics Centre, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands (1)
Department of Clinical Sciences, Cornell University, Ithaca, NY, USA Department of Surgical and Radiological Sciences, School of Veterinary Medicine, University of California-Davis, Davis, CA, USA (1)
Department of Laboratory Medicine and Pathology, Mayo Clinic, Rochester, Minnesota 55905, United States (1)
Department of Pharmaceutical Biosciences, Uppsala University (1)
Division of clinical sciences (IKVL), Department for infectious diseases, BMC D13, Lund University (1)
Dr. Sanjeeva Srivastava, Proteomics Laboratory, Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Powai, Mumbai 400076, India (Lab head). (1)
Institute of Aquaculture, University of Stirling (1)
Institute of Microbiology of the CAS (1)
Institute of Microbiology, Czech Academy of Science, v.v.i. (1)
Laboratory for Structural and Computational Proteomics, Carlos Chagas Institute, Fiocruz, Paraná, Brazil (1)
Nantong University, China (1)
Physikalisch-Technische Bundesanstalt (PTB), Braunschweig und Berlin, D-38116 Braunschweig, Germany (1)
Proteomics, Josef Cvačka Group, Institute of Organic Chemistry and Biochemistry of the CzechAcademy of Sciences; Flemingovo náměstí 542/2 160 00 Praha 6; Czech Republic (1)
The Wistar Institute Philadelphia, PA USA (1)
Tokyo University of Pharmacy and Life Sciences (1)
University of Colorado Denver - Anschutz Medical Campus, Department of Biochemistry and Molecular Genetics (1)

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Identification of proteolytic fragments of human hemoglobin

The uploaded data is related to the identification of the antibacterial/antiviral human peptide HBB 12-147 in hemoglobin digestion with Napsin-A

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

2020-12-15 | MSV000086600 | MassIVE

Hb Oxidation in stored RBCs and Vesicles

We used a state of the art proteomics workflow, based upon nano-UPLC-MS\MS and advanced database searching to identify oxidative modifications to functional residues of hemoglobin subunit beta . Progressive accumulation of oxidized residues in stored erythrocytes and selective removal in vesicles wa...

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

2016-10-04 | MSV000080222 | MassIVE

DSSBU: novel cross-linker tested on bovine serum albumin and human hemoglobin

Protein cross-linking has assumed an irreplaceable role in structural proteomics. Recently, significant efforts have been made to develop novel MS-cleavable reagents. These cross-linkers enhance the reliability of cross-link identification. Presently, only water-insoluble MS-cleavable cross-linkers ...

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

2025-05-07 | PXD055284 | Pride

Expression data from BCL11A-null and wild-type bone marrow erythroid pregenitors

BCL11A is a critical mediator of hemoglobin switching and gamma-globin silencing. In this study, we showed the BCL11A is required in vivo for developmental silencing of gamma-globin genes in adult animals. We used microarray to determine the changes in gene expression profile after loss of BCL11A in...

ORGANISM(S): Mus musculus

2012-03-22 | E-GEOD-28333 | biostudies-arrayexpress

CUT&RUN of erythroblasts upon perturbation of gamma-hemoglobin repressors (part II)

Through high throughput compound screening, we've identified compounds that induce the expression of fetal hemoglobin. This study contains CUT&RUN data of a novel target, WIZ.

ORGANISM(S): Homo sapiens

2024-06-19 | E-MTAB-13890 | biostudies-arrayexpress

Effects of α subunit substitutions on the oxidation of βCys93 and the stability of sickle cell hemoglobin.

Not available

S-EPMC7594797 | biostudies-literature

Hydroxyl radical footprinting analysis of a human haptoglobin-hemoglobin complex

Methods of structural mass spectrometry have become more popular to study protein structure and dynamics. Among them, fast photochemical oxidation of proteins (FPOP) has several advantages such as irreversibility of modifications and more facile determination of the site of modification with single ...

ORGANISM(S): Homo sapiens (Human)

2021-12-30 | PXD021621 | Pride

Footprinting Hemoglobin Haptoglobin Fpop Timstof pro

NHLBI: Genetic modifiers of sickle cell anemia severity and fetal hemoglobin expression in the Cooperative Study of Sickle Cell Disease (CSSCD)

Phenotypic heterogeneity is characteristic of sickle cell anemia, a Mendelian disorder caused by homozygosity for the sickle HBB gene (glu6val). Patients have different rates of hemolysis/vasculopathy and viscosity/vasoocclusion-related complications. These complications account for a s...

phs000366.v1.p1 | EGA

Monodisperse 130 kDa and 260 kDa Recombinant Human Hemoglobin Polymers as Scaffolds for Protein Engineering of Hemoglobin-Based Oxygen Carriers.

Not available

S-EPMC4031019 | biostudies-literature

Label-free Quantification of Host-Cell Protein Impurity in a Recombinant Hemoglobin Reference Material

Quantitative analysis depends on pure-substance primary calibrators with known mass fractions of impurity. The datasets included were generated using mass spectrometry for the evaluation of label-free quantification (LFQ) as a method for determining the mass fraction of host-cell proteins (HCPs) in...

ORGANISM(S): Homo sapiens (Human) Escherichia coli Saccharomyces cerevisiae (Baker's yeast)

2023-05-09 | PXD041736 | Pride

Protein reference materials Dda-pasef Label-free quantification Host-cell proteins

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