(Q34100613)

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Amino acid residues before the hydrophobic region which are critical for membrane translocation of the N-terminal domain of synaptotagmin II.

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31 July 2017

Amino acid residues before the hydrophobic region which are critical for membrane translocation of the N-terminal domain of synaptotagmin II. (English)

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Europe PubMed Central

PubMed publication ID

31 July 2017

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Kida Y

1

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31 July 2017

Sakaguchi M

2

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31 July 2017

Fukuda M

3

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31 July 2017

Mikoshiba K

4

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31 July 2017

Mihara K

5

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31 July 2017

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1 November 2001

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31 July 2017

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31 July 2017

507

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31 July 2017

3

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31 July 2017

341-345

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31 July 2017

Eukaryotic protein secretion

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Membrane topogenesis of a type I signal-anchor protein, mouse synaptotagmin II, on the endoplasmic reticulum

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Multiple determinants direct the orientation of signal-anchor proteins: the topogenic role of the hydrophobic signal domain

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Functions of signal and signal-anchor sequences are determined by the balance between the hydrophobic segment and the N-terminal charge

1 reference

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21 January 2018

Topogenesis of membrane proteins: determinants and dynamics.

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Synaptotagmins: C2-domain proteins that regulate membrane traffic

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The function of inositol high polyphosphate binding proteins

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Synaptotagmins in membrane traffic: which vesicles do the tagmins tag?

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Preparation of microsomal membranes for cotranslational protein translocation.

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Mitochondrial porin can be translocated across both endoplasmic reticulum and mitochondrial membranes

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Topology of eukaryotic type II membrane proteins: importance of N-terminal positively charged residues flanking the hydrophobic domain

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Signal sequence recognition in posttranslational protein transport across the yeast ER membrane.

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[4] Preparation and use of nuclease-treated rabbit reticulocyte lysates for the translation of eukaryotic messenger RNA

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Properties of N-terminal tails in G-protein coupled receptors: a statistical study

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Turns in transmembrane helices: determination of the minimal length of a “helical hairpin” and derivation of a fine-grained turn propensity scale 1 1Edited by F. E. Cohen

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21 January 2018

Membrane topology of NADPH-cytochrome P450 reductase on the endoplasmic reticulum

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21 January 2018

Forced transmembrane orientation of hydrophilic polypeptide segments in multispanning membrane proteins

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21 January 2018

A turn propensity scale for transmembrane helices

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Structural requirements for interruption of protein translocation across rough endoplasmic reticulum membrane

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21 January 2018

A short amino-terminal segment of microsomal cytochrome P-450 functions both as an insertion signal and as a stop-transfer sequence.

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The amino-terminal structures that determine topological orientation of cytochrome P-450 in microsomal membrane.

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Transmembrane orientation of signal-anchor proteins is affected by the folding state but not the size of the N-terminal domain.

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7 January 2021

Identifiers

10.1016/S0014-5793(01)03000-9

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Europe PubMed Central

PubMed publication ID

31 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

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