Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Cryo-EM study of human liver cell lysate

ABSTRACT: This is the proteomic analysis data of Human liver cell lysate subjected to cryo-EM study.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Liver

SUBMITTER: zhemin zhang

LAB HEAD: Edward W.

PROVIDER: PXD040733 | Pride | 2024-01-26

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	PK1_Lum_22nov0305.raw	Raw
	PK1_mzTab.mzTab	Mztab
	PK1_proteinGroups.txt	Txt
	PK2_Lum_22nov0306.raw	Raw
	PK2_mzTab.mzTab	Mztab

Items per page:

1 - 5 of 7

Publications

High-resolution structural-omics of human liver enzymes.

Su Chih-Chia CC Lyu Meinan M Zhang Zhemin Z Miyagi Masaru M Huang Wei W Taylor Derek J DJ Yu Edward W EW

Cell reports 20230607 6

We applied raw human liver microsome lysate to a holey carbon grid and used cryo-electron microscopy (cryo-EM) to define its composition. From this sample we identified and simultaneously determined high-resolution structural information for ten unique human liver enzymes involved in diverse cellular processes. Notably, we determined the structure of the endoplasmic bifunctional protein H6PD, where the N- and C-terminal domains independently possess glucose-6-phosphate dehydrogenase and 6-phosph ...[more]

PMID: 37289586

Similar Datasets

cryo-EM study of human liver mitochondria lysate

Project description:This is the proteomic analysis data of Human liver mitochondria lysate subjected to cryo-EM study.

2024-01-26 | PXD044860 | Pride

cryo-EM study of bovine retinal pigment epithelium cell lysate

Project description:This is the proteomic analysis data of bovine retinal pigment epithelium cell lysate subjected to cryo-EM study.

2023-01-02 | PXD037186 | Pride

Cryo-EM structure of SETD2/Set2 methyltransferase bound to a nucleosome containing oncohistone mutations

Project description:Setd2 methylate the nucleosome to form H3K36me3. Here we utilized the Cryo-EM to elucidate the structure of SETD2/Set2 bound with nucleosomes. Through this structure analysis, we found that histone H1 may interfere the enzymatic activity of SETD2/Set2 by inhibiting their binding affinity.

2021-05-20 | GSE148235 | GEO

Quality evaluation of Enzymatic Methyl-seq library constructed using crude cell lysate

Project description:Enzymatic Methyl-seq (EM-seq) is an enzyme-based method giving us reliable methylome data from small amounts of purified DNA. However, it is unclear whether EM-seq library can be constructed from crude cell lysate containing genomic DNA. We evaluated the quality of EM-seq libraries directly prepared from crude cell lysate.

2024-02-26 | GSE249962 | GEO

Cryo-EM structure of SETD2/Set2 methyltransferase bound to a nucleosome containing oncohistone mutations

Project description:Cryo-EM structure of SETD2/Set2 methyltransferase bound to a nucleosome containing oncohistone mutations

| PRJNA623561 | ENA

Development, Cryo-EM structure and function of potent monospecific and bispecific monoclonal antibodies that neutralize SARS-CoV-2 and variant B.1.351

Project description:The COVID-19 pandemic prompted an unprecedented effort to develop effective countermeasures against SARS-CoV-2. While efficacious vaccines and certain therapeutic monoclonal antibodies are available, here, we report the development, cryo-EM structures and functional analyses of distinct potent monoclonal antibodies (mAbs) that neutralize SARS-CoV-2 and its variant B.1.351. We established a platform for rapid identification of highly potent and specific SARS-CoV-2-neutralizing antibodies by high-throughput B cell receptor single cell sequencing of spike receptor binding domain immunized animals. We identified two highly potent and specific SARS-CoV-2 neutralizing mAb clones that have single-digit nanomolar affinity and low-picomolar avidity. We also generated a bispecific antibody of these two lead clones. The lead monospecific and bispecific antibodies showed strong neutralization ability against prototypical SARS-CoV-2 and the highly contagious South African variant B.1.351 that post a further risk of reducing the efficacy of currently available therapeutic antibodies and vaccines. The lead mAbs showed potent in vivo efficacy against authentic SARS-CoV-2 in both prophylactic and therapeutic settings. We solved five cryo-EM structures at ~3 resolution of these neutralizing antibodies in complex with the ectodomain of the prefusion spike trimer, and revealed the molecular epitopes, binding patterns and conformations between the antibodies and spike RBD, which are distinct from existing antibodies. Our recently developed antibodies expand the repertoire of the toolbox of COVID-19 countermeasures against the SARS-CoV-2 pathogen and its emerging variants.

2022-01-11 | GSE174635 | GEO

Cryo-EM Structure of the bcc-aa3 respiratory chain supercomplex from Corynebacterium glutamicum

Project description:Cryo-EM Structure of the bcc-aa3 respiratory chain supercomplex from Corynebacterium glutamicum

2019-05-29 | MSV000083873 | MassIVE

In situ structure and dynamics of an alphacoronavirus spike protein by cryo-ET and cryo-EM

Project description:The spike protein of the porcine epidemic diarrhea virus from various strains was generated from different mammalian expression systems. The integration of cryo-EM and MS delineated the glycosylation patterns on Spike proteins and also helped understand how individual glycans contribute to biological functions.

2022-10-15 | PXD035778 | Pride

Cryo-EM structure of the full human PRC2 and regulation by AEBP2 and JARID2

Project description:Structural study of the PRC2 complex and its regulators AEPB2 and JARID2 combining cryo-EM, cross-linking, targeted MS and hydrogen/deuterium exchange MS.

2018-01-25 | PXD008605 | Pride

Cryo-EM structure of the volume-regulated anion channel LRRC8D isoform identifies features important for substrate permeation

Project description:Members of the leucine-rich repeat-containing 8 (LRRC8) protein family, composed of the five LRRC8A-E isoforms, are pore-forming components of the volume-regulated anion channel (VRAC), which is activated by cell swelling and transports halide anions and small organic compounds. Despite the recent availability of the cryo-EM structures of homo-hexameric LRRC8A, the structural basis of how LRRC8 isoforms other than LRRC8A contribute to the functional diversity of VRAC has remained elusive. In this study, we confirmed the absence of LRRC8 isoforms in the purified HsLRRC8D using mass spectrometry, and the structure of the HsLRRC8D homomer was analyzed using the cryo-EM. This work provides structural insights into the functional diversity of the LRRC8 protein family.

2020-05-27 | PXD018780 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

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