Results 31 to 40 of about 5,911 (153)

COP‐coated vesicles in intracellular protein transport

open access: yesFEBS Letters, 1995
COP‐coated vesicles have originally been implicated in vesicular transport between subcompartments of the Golgi complex in mammals in a cis to trans direction. More recently, a role for COP‐coated vesicles in transport between the endoplasmic reticulum (ER) and Golgi in mammalian cells has been proposed.
openaire   +2 more sources

"Alternative" endocytic mechanisms exploited by pathogens: new avenues for therapeutic delivery? [PDF]

open access: yes, 2007
Some pathogens utilize unique routes to enter cells that may evade the intracellular barriers encountered by the typical clathrin-mediated endocytic pathway.
Medina-Kauwe, LK
core   +1 more source

Functional dissection of COP-I subunits in the biogenesis of multivesicular endosomes [PDF]

open access: yes, 1997
In the present paper, we show that transport from early to late endosomes is inhibited at the restrictive temperature in a mutant CHO cell line (ldlF) with a ts-defect in epsilon coatomer protein (epsilon COP), although internalization and recycling ...
Aniento   +52 more
core   +3 more sources

A Solution for Exosome‐Based Analysis: Surface‐Enhanced Raman Spectroscopy and Artificial Intelligence

open access: yesAdvanced Intelligent Discovery, EarlyView.
Exosomes are emerging as powerful biomarkers for disease diagnosis and monitoring. This review highlights the integration of surface‐enhanced Raman spectroscopy with artificial intelligence to enhance molecular fingerprinting of exosomes. Machine learning and deep learning techniques improve spectral interpretation, enabling accurate classification of ...
Munevver Akdeniz   +2 more
wiley   +1 more source

Identification of a 200-kD, brefeldin-sensitive protein on Golgi membranes [PDF]

open access: yes, 1992
A mAb AD7, raised against canine liver Golgi membranes, recognizes a novel, 200-kD protein (p200) which is found in a wide variety of cultured cell lines.
Burke, B.   +6 more
core   +1 more source

The Proteasomal Deubiquitinating Enzyme PSMD14 Regulates Macroautophagy by Controlling Golgi-to-ER Retrograde Transport [PDF]

open access: yes, 2020
Ubiquitination regulates several biological processes, however the role of specific members of the ubiquitinome on intracellular membrane trafficking is not yet fully understood.
Arias-Muñoz, Eloisa   +16 more
core   +2 more sources

Nanomaterial‐Mediated Near‐Infrared Photothermal Neuromodulation for Neurologic Disorders

open access: yesAdvanced NanoBiomed Research, EarlyView.
This review summarizes how near‐infrared light activates photothermal nanomaterials to enable noninvasive neuromodulation with high spatiotemporal precision. It elucidates the underlying mechanisms, explores targeted therapeutic applications for neurological disorders, discusses integration with optogenetics and biosensors, and addresses future ...
Ting‐Ting Zeng   +9 more
wiley   +1 more source

Boron Neutron Capture Therapy at a Crossroads: Translational Gap and Emerging Delivery Agents

open access: yesChemistry – A European Journal, EarlyView.
This review surveys recent advances in boron delivery agents for BNCT, emphasizing the shift from classical small molecules to multifunctional nanocarriers and theranostic systems. By integrating targeting, imaging, and therapy, next‐generation boron compounds aim to bridge the gap between (bio)chemical innovation and clinical translation.
Christoph Selg, Evamarie Hey‐Hawkins
wiley   +1 more source

GOLPH3-mTOR Crosstalk and Glycosylation: A Molecular Driver of Cancer Progression

open access: yesCells
Originally identified in proteomic-based studies of the Golgi, Golgi phosphoprotein 3 (GOLPH3) is a highly conserved protein from yeast to humans. GOLPH3 localizes to the Golgi through the interaction with phosphatidylinositol-4-phosphate and is required
Anna Frappaolo   +2 more
doaj   +1 more source

The COP II adaptor protein TMED7 is required to initiate and mediate the delivery of TLR4 to the plasma membrane. [PDF]

open access: yes, 2014
Toll-like receptor 4 (TLR4), the receptor for the bacterial product endotoxin, is subject to multiple points of regulation at the levels of signaling, biogenesis, and trafficking.
Bryant, Clare E   +2 more
core   +1 more source

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