Results 211 to 220 of about 158,042 (243)
Advanced Science, EarlyView.LRRC4 suppresses GBM by regulating AP2A1‐containing Golgi‐derived clathrin‐coated vesicles. Low LRRC4 allows cytoplasmic AP2A1 to maintain mitochondrial fission‐fusion, MICOS integrity, and OXPHOS, promoting proliferation and invasion. High LRRC4 redirects AP2A1‐containing Golgi‐derived clathrin‐coated vesicles to mitochondria, disrupts MICOS, enhances
Yang Li +5 more
wiley +1 more source
Artificial Host‐Guest Recognition Directs Glycometabolically Engineered Macrophages to Tumors
Advanced Science, EarlyView.Glycoengineered supramolecular macrophages (GSAR‐M) are developed using glycometabolic labeling for bioorthogonal host‐guest tumor targeting. This engineering approach unexpectedly enhances macrophage migration, phagocytosis, and pseudopodia formation. Consequently, GSAR‐M demonstrate robust tumor‐targeting specificity, effectively arrest tumor growth,
Zhiqing Yang +8 more
wiley +1 more source
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Destination: inner nuclear membrane
Trends in Cell Biology, 2014The inner nuclear membrane (INM) of eukaryotic cells is enriched in proteins that are required for nuclear structure, chromosome organization, DNA repair, and transcriptional control. Mislocalization of INM proteins is observed in a wide spectrum of human diseases; however, the mechanism by which INM proteins reach their final destination is poorly ...
Sue Jaspersen +2 more
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Protein quality control at the inner nuclear membrane [PDF]
Nature, 2014 The nuclear envelope is a double membrane that separates the nucleus from the cytoplasm. The inner nuclear membrane (INM) functions in essential nuclear processes including chromatin organization and regulation of gene expression. The outer nuclear membrane is continuous with the endoplasmic reticulum and is the site of membrane protein synthesis ...
Marina Pantazopoulou +2 more
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Highway to the inner nuclear membrane: rules for the road
Nature Reviews Molecular Cell Biology, 2007To enter the nucleus a protein must be chaperoned by a transport factor through the nuclear pore complex or it must be small enough to pass through by diffusion. Although these principles have long described the nuclear import of soluble proteins, recent evidence indicates that they also apply to the import of integral inner nuclear membrane proteins ...
Megan KING +2 more
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Structural Basis of Vesicle Formation at the Inner Nuclear Membrane [PDF]
Cell, 2015 Vesicular nucleo-cytoplasmic transport is becoming recognized as a general cellular mechanism for translocation of large cargoes across the nuclear envelope. Cargo is recruited, enveloped at the inner nuclear membrane (INM), and delivered by membrane fusion at the outer nuclear membrane.
Jens B Bosse Jens Bosse +2 more
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Inner nuclear membrane proteins: functions and targeting
Cellular and Molecular Life Sciences, 2001We summarize the properties of integral membrane proteins that reside in the inner nuclear membrane, including lamin B receptor (LBR), lamina-associated polypeptide (LAP) 1, LAP2, emerin, MAN1 and nurim. Most of these proteins interact with lamins and chromatin.
L, Holmer, H J, Worman
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Inner nuclear membrane proteins and the nuclear lamina
Journal of Cell Science, 2001The nuclear lamina is a scaffolding structure at the nuclear periphery and is required for maintenance of nuclear shape, spacing of nuclear pore complexes, organization of heterochromatin, DNA replication, and regulation of transcription factors.
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Inner nuclear membrane and regulation of Smad-mediated signaling
Biochimica Et Biophysica Acta - Molecular and Cell Biology of Lipids, 2006Smads mediate signal transduction by cytokines of the transforming growth factor-beta family. Recent data show that intrinsic and extrinsic proteins of the inner nuclear membrane affect the activities of Smads. MAN1, an integral protein of the inner nuclear membrane, binds to receptor-regulated Smads and antagonizes signaling by transforming growth ...
Cecilia Östlund
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Inner nuclear membrane and signal transduction
Journal of Cellular Biochemistry, 2005AbstractRecent research has shown that the inner nuclear membrane is a site for regulation of signal transduction from the plasma membrane to the nucleus. This has coincided with discoveries showing that mutations in extrinsic and intrinsic inner nuclear membrane proteins cause a variety of inherited diseases. In most instances, the mechanisms by which
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