ArticleNucleic acids research2015
RaftProt: mammalian lipid raft proteome database.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Computational insights on the interplay between electrotaxis and mechanotaxis.PLoS computational biology · 2026Article
- Glutamate, Gangliosides, and the Synapse: Electrostatics at Work in the Brain.International journal of molecular sciences · 2024Review
- DBLiPro: A Database for Lipids and Proteins in Human Lipid Metabolism.Phenomics (Cham, Switzerland) · 2023Article
- A sensitive S-Trap-based approach to the analysis of T cell lipid raft proteome.Journal of lipid research · 2020Article
- Spatiotemporal changes in the human lens proteome: Critical insights into long-lived proteins.Progress in retinal and eye research · 2020Review
- Structural and Functional Determinants of AC8 Trafficking, Targeting and Responsiveness in Lipid Raft Microdomains.The Journal of membrane biology · 2019Article
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
- Understanding Membrane Domain-Partitioning Thermodynamics of Transmembrane Domains with Potential of Mean Force Calculations.The journal of physical chemistry. B · 2019Article
- RaftProt V2: understanding membrane microdomain function through lipid raft proteomes.Nucleic acids research · 2019Article
- Carboxypeptidase O is a lipid droplet-associated enzyme able to cleave both acidic and polar C-terminal amino acids.PloS one · 2018Article
- The mystery of membrane organization: composition, regulation and roles of lipid rafts.Nature reviews. Molecular cell biology · 2017Review
- Proteomic analysis of BmN cell lipid rafts reveals roles in Bombyx mori nucleopolyhedrovirus infection.Molecular genetics and genomics : MGG · 2017Article
- Topologically Diverse Human Membrane Proteins Partition to Liquid-Disordered Domains in Phase-Separated Lipid Vesicles.Biochemistry · 2016Article
- Proteomic Analysis of Lipid Raft-Like Detergent-Resistant Membranes of Lens Fiber Cells.Investigative ophthalmology & visual science · 2015Article
- Diet-induced hypercholesterolemia promotes androgen-independent prostate cancer metastasis via IQGAP1 and caveolin-1.Oncotarget · 2015Article
- Alteration of actin dependent signaling pathways associated with membrane microdomains in hyperlipidemia.Proteome science · 2015Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RaftProt (http://lipid-raft-database.di.uq.edu.au/) is a database of mammalian lipid raft-associated proteins as reported in high-throughput mass spectrometry studies. Lipid rafts are specialized membrane microdomains enriched in cholesterol and sphingolipids thought to act as dynamic signalling and sorting platforms. Given their fundamental roles in cellular regulation, there is a plethora of information on the size, composition and regulation of these membrane microdomains, including a large number of proteomics studies. To facilitate the mining and analysis of published lipid raft proteomics studies, we have developed a searchable database RaftProt. In addition to browsing the studies, performing basic queries by protein and gene names, searching experiments by cell, tissue and organisms; we have implemented several advanced features to facilitate data mining. To address the issue of potential bias due to biochemical preparation procedures used, we have captured the lipid raft preparation methods and implemented advanced search option for methodology and sample treatment conditions, such as cholesterol depletion. Furthermore, we have identified a list of high confidence proteins, and enabled searching only from this list of likely bona fide lipid raft proteins. Given the apparent biological importance of lipid raft and their associated proteins, this database would constitute a key resource for the scientific community.
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