(Q56775266)

5

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author name string

Karin Rösch

1

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Dieter Naeher

2

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Vivienne Laird

Journal of Biological Chemistry

3

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language of work or name

English

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publication date

9 March 2000

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published in

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volume

275

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issue

20

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page(s)

14916-14922

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cites work

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Oligomeric complexes involved in translocation of proteins across the membrane of the endoplasmic reticulum

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Signal sequence recognition in cotranslational translocation by protein components of the endoplasmic reticulum membrane

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Topogenic signals in integral membrane proteins

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Predicting the orientation of eukaryotic membrane-spanning proteins

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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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Glycosylation can influence topogenesis of membrane proteins and reveals dynamic reorientation of nascent polypeptides within the translocon

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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

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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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Transmembrane protein insertion orientation in yeast depends on the charge difference across transmembrane segments, their total hydrophobicity, and its distribution.

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The role of the hydrophobic domain in orienting natural signal sequences within the ER membrane

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Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose

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trans-Golgi retention of a plasma membrane protein: mutations in the cytoplasmic domain of the asialoglycoprotein receptor subunit H1 result in trans-Golgi retention

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Patterns of amino acids near signal-sequence cleavage sites

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The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer.

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

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Signal sequence-dependent function of the TRAM protein during early phases of protein transport across the endoplasmic reticulum membrane

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TRAM regulates the exposure of nascent secretory proteins to the cytosol during translocation into the endoplasmic reticulum.

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A protein of the endoplasmic reticulum involved early in polypeptide translocation

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A tetrameric complex of membrane proteins in the endoplasmic reticulum

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A simple method for displaying the hydropathic character of a protein

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Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins

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Uncoupling hydrophobicity and helicity in transmembrane segments. Alpha-helical propensities of the amino acids in non-polar environments.

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Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins

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New hydrophilicity scale derived from high-performance liquid chromatography peptide retention data: correlation of predicted surface residues with antigenicity and X-ray-derived accessible sites

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The nature of the accessible and buried surfaces in proteins

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Experimentally determined hydrophobicity scale for proteins at membrane interfaces

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Oligomeric Rings of the Sec61p Complex Induced by Ligands Required for Protein Translocation

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The hydrophobic region of signal peptides is a determinant for SRP recognition and protein translocation across the ER membrane

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A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane

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Non-random distribution of amino acids in the transmembrane segments of human type I single span membrane proteins

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A measure of helical propensity for amino acids in membrane environments

21 January 2018

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On the hydrophobic nature of signal sequences

21 January 2018

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