DOI . ORG {
}
We began analyzing https://link.springer.com/article/10.1007/s10719-023-10116-9, but it redirected us to https://link.springer.com/article/10.1007/s10719-023-10116-9. The analysis below is for the second page.
Title[redir]:
Recently developed glycosphingolipid probes and their dynamic behavior in cell plasma membranes as revealed by single-molecule imaging | Glycoconjugate Journal
Description:
Glycosphingolipids, including gangliosides, are representative lipid raft markers that perform a variety of physiological roles in cell membranes. However, studies aimed at revealing their dynamic behavior in living cells are rare, mostly due to a lack of suitable fluorescent probes. Recently, the ganglio-series, lacto-series, and globo-series glycosphingolipid probes, which mimic the behavior of the parental molecules in terms of partitioning to the raft fraction, were developed by conjugating hydrophilic dyes to the terminal glycans of glycosphingolipids using state-of-art entirely chemical-based synthetic techniques. High-speed, single-molecule observation of these fluorescent probes revealed that gangliosides were scarcely trapped in small domains (100 nm in diameter) for more than 5 ms in steady-state cells, suggesting that rafts including gangliosides were always moving and very small. Furthermore, dual-color, single-molecule observations clearly showed that homodimers and clusters of GPI-anchored proteins were stabilized by transiently recruiting sphingolipids, including gangliosides, to form homodimer rafts and the cluster rafts, respectively. In this review, we briefly summarize recent studies, the development of a variety of glycosphingolipid probes as well as the identification of the raft structures including gangliosides in living cells by single-molecule imaging.
Title[redir]:
Recently developed glycosphingolipid probes and their dynamic behavior in cell plasma membranes as revealed by single-molecule imaging | Glycoconjugate Journal
Description:
Glycosphingolipids, including gangliosides, are representative lipid raft markers that perform a variety of physiological roles in cell membranes. However, studies aimed at revealing their dynamic behavior in living cells are rare, mostly due to a lack of suitable fluorescent probes. Recently, the ganglio-series, lacto-series, and globo-series glycosphingolipid probes, which mimic the behavior of the parental molecules in terms of partitioning to the raft fraction, were developed by conjugating hydrophilic dyes to the terminal glycans of glycosphingolipids using state-of-art entirely chemical-based synthetic techniques. High-speed, single-molecule observation of these fluorescent probes revealed that gangliosides were scarcely trapped in small domains (100 nm in diameter) for more than 5 ms in steady-state cells, suggesting that rafts including gangliosides were always moving and very small. Furthermore, dual-color, single-molecule observations clearly showed that homodimers and clusters of GPI-anchored proteins were stabilized by transiently recruiting sphingolipids, including gangliosides, to form homodimer rafts and the cluster rafts, respectively. In this review, we briefly summarize recent studies, the development of a variety of glycosphingolipid probes as well as the identification of the raft structures including gangliosides in living cells by single-molecule imaging.
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Keywords {🔍}
pubmed, article, google, scholar, cas, cell, suzuki, central, biol, membrane, kusumi, singlemolecule, fujiwara, plasma, receptor, chem, ganglioside, interactions, imaging, cells, gangliosides, probes, ando, lipid, raft, sci, glycosphingolipid, komura, kgn, membranes, fluorescent, molecular, biophys, rafts, gpianchored, hakomori, usa, httpsdoiorgjcb, diffusion, dynamic, revealed, organization, signal, proc, natl, acad, httpsdoiorgpnas, httpsdoiorgs, nat, content,
Topics {✒️}
month download article/chapter transiently recruiting sphingolipids membrane-raft-based molecular interactions fret-based assay system sialic acid research globo-series glycosphingolipid probes g-protein-coupled receptor glycolipids mediate binding gpi-anchored receptor fluorescence correlation spectroscopy chemical-based synthetic techniques stimulation-induced stabilized rafts single-molecule imaging suitable fluorescent probes gpi-anchored proteins single-molecule tracking single molecule tracking gpi-anchored receptors n-linked glcnac termini fluorescent probes revealed single molecule techniques single-molecule techniques sphingolipid-enriched membrane domains full article pdf single-molecule observations gm3-enriched microdomain involved lipid rafts based single-molecule observation fluorescent sphingomyelin analogs n-linked glycan nerve growth factor lipid-anchored proteins receptor-receptor interactions privacy choices/manage cookies amyloid β-protein fluorescent gd2 analog raft-based interactions related subjects fluorescent ganglioside gd3 form homodimer rafts tyrosine kinase activity �glycosphingolipid signaling domain” personal data glyco-core research �lipid raft” concept steady-state cells rafts including gangliosides raft domain structure ganglioside-mediated assembly ampa receptor trafficking
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headline:Recently developed glycosphingolipid probes and their dynamic behavior in cell plasma membranes as revealed by single-molecule imaging
description:Glycosphingolipids, including gangliosides, are representative lipid raft markers that perform a variety of physiological roles in cell membranes. However, studies aimed at revealing their dynamic behavior in living cells are rare, mostly due to a lack of suitable fluorescent probes. Recently, the ganglio-series, lacto-series, and globo-series glycosphingolipid probes, which mimic the behavior of the parental molecules in terms of partitioning to the raft fraction, were developed by conjugating hydrophilic dyes to the terminal glycans of glycosphingolipids using state-of-art entirely chemical-based synthetic techniques. High-speed, single-molecule observation of these fluorescent probes revealed that gangliosides were scarcely trapped in small domains (100 nm in diameter) for more than 5 ms in steady-state cells, suggesting that rafts including gangliosides were always moving and very small. Furthermore, dual-color, single-molecule observations clearly showed that homodimers and clusters of GPI-anchored proteins were stabilized by transiently recruiting sphingolipids, including gangliosides, to form homodimer rafts and the cluster rafts, respectively. In this review, we briefly summarize recent studies, the development of a variety of glycosphingolipid probes as well as the identification of the raft structures including gangliosides in living cells by single-molecule imaging.
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headline:Recently developed glycosphingolipid probes and their dynamic behavior in cell plasma membranes as revealed by single-molecule imaging
description:Glycosphingolipids, including gangliosides, are representative lipid raft markers that perform a variety of physiological roles in cell membranes. However, studies aimed at revealing their dynamic behavior in living cells are rare, mostly due to a lack of suitable fluorescent probes. Recently, the ganglio-series, lacto-series, and globo-series glycosphingolipid probes, which mimic the behavior of the parental molecules in terms of partitioning to the raft fraction, were developed by conjugating hydrophilic dyes to the terminal glycans of glycosphingolipids using state-of-art entirely chemical-based synthetic techniques. High-speed, single-molecule observation of these fluorescent probes revealed that gangliosides were scarcely trapped in small domains (100 nm in diameter) for more than 5 ms in steady-state cells, suggesting that rafts including gangliosides were always moving and very small. Furthermore, dual-color, single-molecule observations clearly showed that homodimers and clusters of GPI-anchored proteins were stabilized by transiently recruiting sphingolipids, including gangliosides, to form homodimer rafts and the cluster rafts, respectively. In this review, we briefly summarize recent studies, the development of a variety of glycosphingolipid probes as well as the identification of the raft structures including gangliosides in living cells by single-molecule imaging.
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Gangliosides
Sialic acid
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Single-molecule imaging
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Biochemistry
general
Pathology
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