Literature DB >> 16709166

Phosphatidylinositol-transfer protein and its homologues in yeast.

P Griac1, R Holic, D Tahotna.   

Abstract

Yeast Sec14p acts as a phosphatidylinositol/phosphatidylcholine-transfer protein in vitro. In vivo, it is essential in promoting Golgi secretory function. Products of five genes named SFH1-SFH5 (Sec Fourteen Homologues 1-5) exhibit significant sequence homology to Sec14p and together they form the Sec14p family of lipid-transfer proteins. It is a diverse group of proteins with distinct subcellular localizations and varied physiological functions related to lipid metabolism and membrane trafficking.

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Year:  2006        PMID： 16709166     DOI： 10.1042/BST0340377

Source DB:  PubMed          Journal:  Biochem Soc Trans        ISSN： 0300-5127            Impact factor:   5.407


  3 in total

1.  The phospholipid-binding protein SESTD1 is a novel regulator of the transient receptor potential channels TRPC4 and TRPC5.

Authors:  Susanne Miehe; Andrea Bieberstein; Isabelle Arnould; Orhia Ihdene; Hartmut Rütten; Carsten Strübing
Journal:  J Biol Chem       Date:  2010-02-17       Impact factor: 5.157

2.  In silico evidence for functional specialization after genome duplication in yeast.

Authors:  Ossi Turunen; Ralph Seelke; Jed Macosko
Journal:  FEMS Yeast Res       Date:  2009-02       Impact factor: 2.796

3.  Comparative proteomics reveals the physiological differences between winter tender shoots and spring tender shoots of a novel tea (Camellia sinensis L.) cultivar evergrowing in winter.

Authors:  Shengjie Liu; Jiadong Gao; Zhongjian Chen; Xiaoyan Qiao; Hualin Huang; Baiyuan Cui; Qingfeng Zhu; Zhangyan Dai; Hualing Wu; Yayan Pan; Chengwei Yang; Jun Liu
Journal:  BMC Plant Biol       Date:  2017-11-20       Impact factor: 4.215
  3 in total

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