Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Anna Bielli"'
Autor:
Sergei I. Bannykh, Gavin Gabreski, Anna Bielli, Meir Aridor, Charles J. Haney, Simon C. Watkins
Publikováno v:
The Journal of Cell Biology
The mechanisms by which the coat complex II (COPII) coat mediates membrane deformation and vesicle fission are unknown. Sar1 is a structural component of the membrane-binding inner layer of COPII (Bi, X., R.A. Corpina, and J. Goldberg. 2002. Nature.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77f0bc27b2bdcf5a438e2bdb8aa226f1
https://doi.org/10.1083/jcb.200509095
https://doi.org/10.1083/jcb.200509095
Autor:
Vera Roberti, Anna Bielli, Frances J. Drummond, Mariarosaria Santillo, Cecilia Bucci, Silvia Mora, Mary W. McCaffrey, Giuseppina Cantalupo
Publikováno v:
FEBS Letters. 495:21-30
The small GTPases Rab4, Rab5 and Rab7 are endosomal proteins which play important roles in the regulation of various stages of endosomal trafficking. Rab4 and Rab5 have both been localized to early endosomes and have been shown to control recycling a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29ffb0ea055aaad0f18a639681c428a4
https://doi.org/10.1016/s0014-5793(01)02359-6
https://doi.org/10.1016/s0014-5793(01)02359-6
Autor:
K A Fitzgerald, Alan G. Hendrick, Anna Bielli, Mary W. McCaffrey, Per-Ove Thörnqvist, Robert Finn
Publikováno v:
Biochemical and Biophysical Research Communications. 281:1141-1153
Rab4 belongs to the Rab family of small GTPases involved in the regulation of intracellular transport, and has been localized to early endosomes. We have employed the yeast two-hybrid system to identify proteins that specifically interact with Rab4AQ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7aae7b3c328a1e52d26d8b4040c9d93
https://doi.org/10.1006/bbrc.2001.4468
https://doi.org/10.1006/bbrc.2001.4468
Publikováno v:
The Journal of neuroscience : the official journal of the Society for Neuroscience. 24(15)
The elongated and polarized characteristics of neurons render targeting of receptors to the plasma membrane of distal axonal projections and dendritic branches a major sorting task. Although the majority of biosynthetic cargo synthesis, transport, an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8013f90961e0c05ec42ad1174b777d1
https://pubmed.ncbi.nlm.nih.gov/15084657
https://pubmed.ncbi.nlm.nih.gov/15084657
Autor:
Guillermo Romero, Simon C. Watkins, Sean Alber, Anna Blumental-Perry, Anna Bielli, Meir Aridor, Kuntala Shome, Charles J. Haney, Purnima Pathre
Publikováno v:
The EMBO journal. 22(16)
The small GTPase Sar1p controls the assembly of the cytosolic COPII coat that mediates export from the endoplasmic reticulum (ER). Here we demonstrate that phospholipase D (PLD) activation is required to support COPII-mediated ER export. PLD activity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88bee90fab2b892fe5f1a67cc52ae2a9
https://pubmed.ncbi.nlm.nih.gov/12912905
https://pubmed.ncbi.nlm.nih.gov/12912905
Assembly and intracellular transport of phaseolin, the major storage protein of Phaseolus vulgaris L
Autor:
Roberto Bollini, Alessandro Vitale, Emanuela Pedrazzini, Giovanna Giovinazzo, Aldo Ceriotti, Anna Bielli
Publikováno v:
Journal of plant physiology
145 (1995): 648–653. doi:10.1016/S0176-1617(11)81277-0
info:cnr-pdr/source/autori:A. Ceriotti, E. Pedrazzini, A. Bielli, G. Giovinazzo, R. Bollini e A. Vitale/titolo:Assembly and intracellular transport of phaseolin, the major storage protein of Phaseolus vulgaris L./doi:10.1016%2FS0176-1617(11)81277-0/rivista:Journal of plant physiology (Print)/anno:1995/pagina_da:648/pagina_a:653/intervallo_pagine:648–653/volume:145
145 (1995): 648–653. doi:10.1016/S0176-1617(11)81277-0
info:cnr-pdr/source/autori:A. Ceriotti, E. Pedrazzini, A. Bielli, G. Giovinazzo, R. Bollini e A. Vitale/titolo:Assembly and intracellular transport of phaseolin, the major storage protein of Phaseolus vulgaris L./doi:10.1016%2FS0176-1617(11)81277-0/rivista:Journal of plant physiology (Print)/anno:1995/pagina_da:648/pagina_a:653/intervallo_pagine:648–653/volume:145
Summary Phaseolin is a trimeric glycoprotein that accumulates in the protein storage vacuoles of common bean (Phaseolus vulgaris L.) seeds. The resistance to proteolytic degradation is likely to be an important feature of native phaseolin, allowing i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb133e11f8547edc90cb2acee6b40aa1
http://www.cnr.it/prodotto/i/230405
http://www.cnr.it/prodotto/i/230405
