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Refinado por: assunto: Membrane Proteins remover Base de dados/Biblioteca: DOAJ Directory of Open Access Journals remover
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1
Extracellular calcium alters calcium-sensing receptor network integrating intracellular calcium-signaling and related key pathway
Extracellular calcium alters calcium-sensing receptor network integrating intracellular calcium-signaling and related key pathway
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Extracellular calcium alters calcium-sensing receptor network integrating intracellular calcium-signaling and related key pathway

Gorkhali, Rakshya ; Tian, Li ; Dong, Bin ; Bagchi, Pritha ; Deng, Xiaonan ; Pawar, Shrikant ; Duong, Duc ; Fang, Ning ; Seyfried, Nicholas ; Yang, Jenny

Scientific reports, 2021-10, Vol.11 (1), p.20576-20576, Article 20576 [Periódico revisado por pares]

England: Nature Publishing Group

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2
ORP5 and ORP8 bind phosphatidylinositol-4, 5-biphosphate (PtdIns(4,5)P 2 ) and regulate its level at the plasma membrane
ORP5 and ORP8 bind phosphatidylinositol-4, 5-biphosphate (PtdIns(4,5)P 2 ) and regulate its level at the plasma membrane
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ORP5 and ORP8 bind phosphatidylinositol-4, 5-biphosphate (PtdIns(4,5)P 2 ) and regulate its level at the plasma membrane

Ghai, Rajesh ; Du, Ximing ; Wang, Huan ; Dong, Jiangqing ; Ferguson, Charles ; Brown, Andrew J ; Parton, Robert G ; Wu, Jia-Wei ; Yang, Hongyuan

Nature communications, 2017-10, Vol.8 (1), p.757-14, Article 757 [Periódico revisado por pares]

England: Nature Publishing Group

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3
ER–plasma membrane contact sites contribute to autophagosome biogenesis by regulation of local PI3P synthesis
ER–plasma membrane contact sites contribute to autophagosome biogenesis by regulation of local PI3P synthesis
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ER–plasma membrane contact sites contribute to autophagosome biogenesis by regulation of local PI3P synthesis

Nascimbeni, Anna Chiara ; Giordano, Francesca ; Dupont, Nicolas ; Grasso, Daniel ; Vaccaro, Maria I ; Codogno, Patrice ; Morel, Etienne

The EMBO journal, 2017-07, Vol.36 (14), p.2018-2033 [Periódico revisado por pares]

England: Blackwell Publishing Ltd

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4
Seipin and the membrane-shaping protein Pex30 cooperate in organelle budding from the endoplasmic reticulum
Seipin and the membrane-shaping protein Pex30 cooperate in organelle budding from the endoplasmic reticulum
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Seipin and the membrane-shaping protein Pex30 cooperate in organelle budding from the endoplasmic reticulum

Wang, Sihui ; Idrissi, Fatima-Zahra ; Hermansson, Martin ; Grippa, Alexandra ; Ejsing, Christer S ; Carvalho, Pedro

Nature communications, 2018-07, Vol.9 (1), p.2939-12, Article 2939 [Periódico revisado por pares]

England: Nature Publishing Group

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5
FUNDC1-dependent mitochondria-associated endoplasmic reticulum membranes are involved in angiogenesis and neoangiogenesis
FUNDC1-dependent mitochondria-associated endoplasmic reticulum membranes are involved in angiogenesis and neoangiogenesis
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FUNDC1-dependent mitochondria-associated endoplasmic reticulum membranes are involved in angiogenesis and neoangiogenesis

Wang, Cheng ; Dai, Xiaoyan ; Wu, Shengnan ; Xu, Wenjing ; Song, Ping ; Huang, Kai

Nature communications, 2021-05, Vol.12 (1), p.2616-2616, Article 2616 [Periódico revisado por pares]

England: Nature Publishing Group

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6
SNX19 restricts endolysosome motility through contacts with the endoplasmic reticulum
SNX19 restricts endolysosome motility through contacts with the endoplasmic reticulum
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SNX19 restricts endolysosome motility through contacts with the endoplasmic reticulum

Saric, Amra ; Freeman, Spencer A ; Williamson, Chad D ; Jarnik, Michal ; Guardia, Carlos M ; Fernandopulle, Michael S ; Gershlick, David C ; Bonifacino, Juan S

Nature communications, 2021-07, Vol.12 (1), p.4552-4552, Article 4552 [Periódico revisado por pares]

England: Nature Publishing Group

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7
Human VPS13A is associated with multiple organelles and influences mitochondrial morphology and lipid droplet motility
Human VPS13A is associated with multiple organelles and influences mitochondrial morphology and lipid droplet motility
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Human VPS13A is associated with multiple organelles and influences mitochondrial morphology and lipid droplet motility

Yeshaw, Wondwossen M ; van der Zwaag, Marianne ; Pinto, Francesco ; Lahaye, Liza L ; Faber, Anita Ie ; Gómez-Sánchez, Rubén ; Dolga, Amalia M ; Poland, Conor ; Monaco, Anthony P ; van IJzendoorn, Sven Cd ; Grzeschik, Nicola A ; Velayos-Baeza, Antonio ; Sibon, Ody Cm

eLife, 2019-02, Vol.8 [Periódico revisado por pares]

England: eLife Sciences Publications Ltd

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8
The architecture of EMC reveals a path for membrane protein insertion
The architecture of EMC reveals a path for membrane protein insertion
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The architecture of EMC reveals a path for membrane protein insertion

O'Donnell, John P ; Phillips, Ben P ; Yagita, Yuichi ; Juszkiewicz, Szymon ; Wagner, Armin ; Malinverni, Duccio ; Keenan, Robert J ; Miller, Elizabeth A ; Hegde, Ramanujan S

eLife, 2020-05, Vol.9 [Periódico revisado por pares]

England: eLife Sciences Publications Ltd

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9
Identification of MOSPD2, a novel scaffold for endoplasmic reticulum membrane contact sites
Identification of MOSPD2, a novel scaffold for endoplasmic reticulum membrane contact sites
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Identification of MOSPD2, a novel scaffold for endoplasmic reticulum membrane contact sites

Di Mattia, Thomas ; Wilhelm, Léa P ; Ikhlef, Souade ; Wendling, Corinne ; Spehner, Danièle ; Nominé, Yves ; Giordano, Francesca ; Mathelin, Carole ; Drin, Guillaume ; Tomasetto, Catherine ; Alpy, Fabien

EMBO reports, 2018-07, Vol.19 (7), p.n/a [Periódico revisado por pares]

England: Blackwell Publishing Ltd

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10
Regulation of protein secretion through chemical regulation of endoplasmic reticulum retention signal cleavage
Regulation of protein secretion through chemical regulation of endoplasmic reticulum retention signal cleavage
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Regulation of protein secretion through chemical regulation of endoplasmic reticulum retention signal cleavage

Praznik, Arne ; Fink, Tina ; Franko, Nik ; Lonzarić, Jan ; Benčina, Mojca ; Jerala, Nina ; Plaper, Tjaša ; Roškar, Samo ; Jerala, Roman

Nature communications, 2022-03, Vol.13 (1), p.1323-1323, Article 1323 [Periódico revisado por pares]

England: Nature Publishing Group

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