Name: Cell Surface Glycoengineering - HAP1 Cells
Keywords: Cell surface glycoengineering - hap1 cells

OmicsDI

Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Cell Surface Glycoengineering - HAP1 Cells

ABSTRACT: Cell Surface Glycoengineering of HAP1 Cells using CMP-Neu5Ac Derivatives

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: M. Osman Sheikh

LAB HEAD: Dr. Lance Wells

PROVIDER: PXD024251 | Pride | 2022-06-26

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Publications

Cell surface glycan engineering reveals that matriglycan alone can recapitulate dystroglycan binding and function.

Sheikh M Osman MO Capicciotti Chantelle J CJ Liu Lin L Praissman Jeremy J Ding Dahai D Mead Daniel G DG Brindley Melinda A MA Willer Tobias T Campbell Kevin P KP Moremen Kelley W KW Wells Lance L Boons Geert-Jan GJ

Nature communications 20220624 1

α-Dystroglycan (α-DG) is uniquely modified on O-mannose sites by a repeating disaccharide (-Xylα1,3-GlcAβ1,3-)<sub>n</sub> termed matriglycan, which is a receptor for laminin-G domain-containing proteins and employed by old-world arenaviruses for infection. Using chemoenzymatically synthesized matriglycans printed as a microarray, we demonstrate length-dependent binding to Laminin, Lassa virus GP1, and the clinically-important antibody IIH6. Utilizing an enzymatic engineering approach, an N-link ...[more]

PMID: 35750689

Similar Datasets

Identification of the Tau aggresome in progressive supranuclear palsy by in situ biotinylation by antibody recognition

Project description:Here, we used an unbiased proteomic approach, which combines antibody-mediated proximity-detection of co-aggregated proteins together with mass spectrometry. Biotinylation by antibody recognition (BAR) is a recently developed method, by which a primary antibody recognises the target of interest in fixed samples. A secondary antibody conjugated to horseradish peroxidase (HRP) recognises the primary antibody, and with the addition of biotin phenol and hydrogen peroxide, facilitates biotinylation of proteins in close proximity. Biotinylated proteins are then biochemically isolated and identified using mass spectrometry (MS).

2023-02-27 | PXD028237 | Pride

Dm Snail Affymetrix ChIP

Project description:Genomewide mapping of D. melanogaster Snail protein binding during embryonic development at 2-4 hrs after egg-laying. Two independent repeats were assayed and preimmune-serum was used as a control. The enriched DNA was hybridized to high density Affymetrix GeneChip Drosophila Tiling 1.0R array

2014-01-10 | E-MTAB-1589 | biostudies-arrayexpress

Dm Lmd 6-8hrs Affymetrix ChIP

Project description:Genomewide mapping of D. melanogaster Lame duck protein binding at 6-8hrs after egg laying. Two different rabbit antibodies were used to precipitate the Lmd protein isoform in biological replicates. Additionally a rabbit preimmune-serum was used as a control. The enriched DNA was hybridized to high density Affymetrix GeneChip Drosophila Tiling 1.0R array.

2014-03-01 | E-MTAB-1283 | biostudies-arrayexpress

Proteomic and functional analyses of the periodic membrane skeleton in neurons

Project description:Actin, spectrin, and associated proteins form a membrane-associated periodic skeleton (MPS) in neurons. The molecular composition and functions of the MPS remain incompletely understood. Here, we combined co-immunoprecipitation and mass spectrometry analyses to identify candidate MPS-interacting proteins from cultured hippocampal neurons and adult mouse brains. In addition, we also used quantitative mass spectrometry analysis based on Tandem Mass Tag (TMT) isobaric labeling to determine how the expression levels of proteins are differentially regulated at the proteomic scale upon depletion of βII-spectrin, an important molecular component of the MPS. These results provide a systematic picture of the interactome of the MPS, and new insights into new functions of the MPS in neurons.

2022-05-04 | PXD030886 | Pride

Dm Ttk69 6-8hrs Affymetrix ChIP

Project description:Genomewide mapping of D. melanogaster Tramtrack69 protein binding at 6-8hrs after egg laying. Two different rabbit antibodies were used to precipitate the Tramtrack69 protein isoform in 3 biological replicates. Additionally a rabbit preimmune-serum was used as a control for every precipitation. The enriched DNA was hybridized to high density Affymetrix GeneChip Drosophila Tiling 1.0R array.

2014-03-01 | E-MTAB-1287 | biostudies-arrayexpress

Localization of the priming factors CAPS1 and CAPS2 in mouse sensory neurons is determined by their N-termini

Project description:Both paralogs of the calcium-dependent activator protein for secretion (CAPS) are required for exocytosis of synaptic vesicles (SVs) and large dense core vesicles (LDCVs). Despite approximately 80% sequence identity, CAPS1 and CAPS2 have distinct functions in promoting exocytosis of SVs and LDCVs in dorsal root ganglion (DRG) neurons. However, the molecular mechanisms underlying these differences remain enigmatic. In this study, we applied high- and super-resolution imaging techniques to systematically assess the subcellular localization of CAPS paralogs in DRG neurons deficient in both CAPS1 and CAPS2. CAPS1 was found to be more enriched at the synapses. Using - in-depth sequence analysis, we identified a unique CAPS1 N-terminal sequence, which we introduced into CAPS2. This CAPS1/2 chimera reproduced the pre-synaptic localization of CAPS1 and partially rescued synaptic transmission in neurons devoid of CAPS1 and CAPS2. Using immunoprecipitation combined with mass spectrometry, we identified CAPS1-specific interaction partners that could be responsible for its pre-synaptic enrichment. Taken together, these data suggest an important role of the CAPS1-N terminus in the localization of the protein at pre-synapses.

2022-04-01 | PXD031625 | Pride

CPEB1 or CPEB1 (T171A, S177A) interacting proteome analysis on C2C12 cells

Project description:CPEB1 regulates cellular function by post-transcriptionally controlling its targeted transcripts' translation. After bound to CPEs, CPEB1 recruits cytoplasmic poly (A) polymerase GLD2 to elongate the poly (A) tail for the maintenance of mRNA stability. The stability of mRNA is positively correlated with translational output. It is unexamined whether CPEB1 interacts with translation machinery to regulation translation. Previous reports demonstrate that phosphorylation is required for its regulation on translation. However, it is not well understood whether phosphorylation is essential for CPEB1 interaction with translation machinery or not. Here, we performed mass spectrometry on C2 cells transfected with CPEB1-mVenus or CPEB1 (T171A, S177A)-mVenus after IgG or mVenus antibody immunoprecipitation. After analysis, we identify CPEB1 interacting proteins and the phosphorylation dependent interacting proteins such as ribosomal proteins. Thus, our data suggest that CPEB1 regulate translation by interacting with translation machinery in a phosphorylation dependent manner.

2021-11-04 | PXD020822 | Pride

Profiling of spreading- coupled protein tyrosine phosphorylation

Project description:Protein tyrosine phosphorylation is an important mechanism that regulates cytoskeleton reorganization and cell spreading of migratory cells. A number of cytoskeletal proteins are known to be tyrosine phosphorylated (pY) in different cellular processes. However, the profile of pY proteins during different stages of cell spreading has not been available.

2016-09-28 | PXD004340 | Pride

Chromatin immunopreciptitation of Drosophila DNA using antibodies against RMA polymerase II CTD repeats

Project description:Crosslinked chromatin from wild type flies was sonicated into small fragments, and used in ChIP reactions using a monoclonal antibody, 8WG16, against RNA polymerase II CTD repeats. Input material was removed prior to chIP, and a control chIP was incubated with normal rabbit IgG. The Input and IPed DNA was purified, amplified, and hybridized to Affymetrix Drosophila genomic tiling arrays.

2008-05-20 | E-MEXP-1520 | biostudies-arrayexpress

Chromatin immunoprecipitation of Drosophila to identify Twist protein binding during embryonic development

Project description:Genomewide mapping of D. melanogaster Twist protein binding during embryonic development. Three consecutive timepoints (2-4, 4-6, 6-8 hrs after egg-laying) were assayed in two independent repeats each. Two different antibodies were used to precipitate the Twist protein. Additionally the respective preimmune-serum was used as a control for every precipitation. The enriched DNA was hybridized to high density Affymetrix GeneChip Drosophila Tiling 1.0R array.

2009-11-09 | E-TABM-651 | biostudies-arrayexpress

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data