Results 251 to 260 of about 1,228,008 (299)

Biophysical Characterization and Proteomic Analysis of Small Extracellular Vesicles Derived From Different Neural Cell Lines

Advanced NanoBiomed Research, EarlyView.
This study systematically compares small extracellular vesicles (sEVs) derived from four neural cell lines, revealing how cellular origin shapes vesicle biophysical properties and proteomic cargo. Distinct, lineage‐specific signatures linked to neuronal, astrocytic, and microglial functions are identified, highlighting the importance of cell source ...
Muhammad Waqas Salim, Wei Zhang, Lyndsey E. Collins‐Praino, Andrew Care, Yuling Wang   +4 more
wiley   +1 more source

Some of the next articles are maybe not open access.

Related searches:

Annexins in the secretory pathway

Cellular and Molecular Life Sciences (CMLS), 1997
Among the multiplicity of roles suggested for proteins of the annexin family, those implicating these proteins in regulated exocytosis remain among the most convincing. Studies in this area of annexin biology have focused on annexin II, which because of its unusually low Ca(2+)-requirement for phospholipid-binding has many of the requisite properties ...
S R, Donnelly, S E, Moss
openaire   +2 more sources

Proton Pumping in the Secretory Pathway

Journal of Membrane Biology, 2001
Contains fulltext : 308741.pdf (Publisher’s version ) (Closed access)
Schoonderwoert, V.T., Martens, G.J.M.
openaire   +3 more sources

Morphodynamics of the Secretory Pathway

2004
A careful scrutiny of the dynamics of secretory compartments in the entire eukaryotic world reveals many common themes. The most fundamental theme is that the Golgi apparatus and related structures appear as compartments formed by the act of transporting cargo. The second common theme is the pivotal importance for endomembrane dynamics of shifting back
Képès, François, Rambourg, Alain, Satiat-Jeunemaître, Béatrice   +2 more
openaire   +4 more sources

Tyrosine Sulfation and the Secretory Pathway

Annual Review of Physiology, 1988
Tyrosine sulfation is a widespread posttranslational modification. Most tyrosine-sulfated proteins identified so far are secretory, including several neuropeptides. Tyrosine sulfation occurs in the trans Golgi and is one of the last processing steps before proteins exit from the Golgi complex.
openaire   +2 more sources

Green light for the secretory pathway

Protoplasma, 1999
Since the advent of green-fluorescent protein (GFP) technology there has been an explosion of interest in applying this molecule to cell biology. This review summarizes new insights in secretory membrane traffic obtained by the use of GFP fusion proteins.
H H, Gerdes, R, Rudolf
openaire   +2 more sources

Molecular dissection of the secretory pathway

Nature, 1992
A combination of biochemistry in animal cell-free systems and genetics in yeast is revealing the molecular machinery of the secretory pathway of eukaryotes. Transporting vesicles have a simple coat structure and employ a general mechanism for fusion that is conserved in evolution.
J E, Rothman, L, Orci
openaire   +2 more sources

A NOVEL PATHWAY FOR SECRETORY PROTEINS?

Trends in Biochemical Sciences, 1990
In eukaryotes, most proteins which are transported to the extracellular space, into mitochondria or into chloroplasts are synthesized as precursor polypeptides containing cleavable N-terminal signal or targeting sequences. We have searched the literature for proteins that are exported from the cytosol without being proteolytically processed.
MUESCH A., HARTMANN E., ROHDE K., RUBARTELLI A., SITIA , ROBERTO, CRAPOPORT T. A.   +5 more
openaire   +3 more sources

The ins and outs of the secretory pathway

Trends in Cell Biology, 1993
O MISCELLANEA *2nd Annaberg Conference: EMBO Workshop on Protein Transport, Sorting and Processing. Annaberg, Austria; 11-16 January 1993. Gabriele Seethaler is at the Institute of Molecular Biology, Austrian Academy of Sciences, Billrothstrasse 11, A-5020 Salzburg, Austria; and Hans- Hermann Gerdes is at the ...
G, Seethaler, H H, Gerdes
openaire   +2 more sources

Quality control in the secretory pathway

Current Opinion in Cell Biology, 1995
Whereas newly synthesized proteins that have acquired a properly folded and assembled structure are transported from the endoplasmic reticulum to their final destinations, incompletely folded and assembled proteins are, as a rule, retained and eventually degraded.
C, Hammond, A, Helenius
openaire   +2 more sources