NH2-terminal substitutions of basic amino acids induce translocation across the microsomal membrane and glycosylation of rabbit cytochrome P450IIC2. (Q35190535)

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English	NH2-terminal substitutions of basic amino acids induce translocation across the microsomal membrane and glycosylation of rabbit cytochrome P450IIC2.	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

7 August 2017

NH2-terminal substitutions of basic amino acids induce translocation across the microsomal membrane and glycosylation of rabbit cytochrome P450IIC2. (English)

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Europe PubMed Central

PubMed publication ID

7 August 2017

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author name string

E Szczesna-Skorupa

1

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Europe PubMed Central

PubMed publication ID

7 August 2017

B Kemper

2

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Europe PubMed Central

PubMed publication ID

7 August 2017

language of work or name

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publication date

1 April 1989

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7 August 2017

number of pages

7

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Journal of Cell Biology

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7 August 2017

108

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7 August 2017

4

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Europe PubMed Central

PubMed publication ID

7 August 2017

1237-1243

1 reference

Europe PubMed Central

PubMed publication ID

7 August 2017

A simple method for displaying the hydropathic character of a protein

1 reference

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Intracellular protein topogenesis

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13 July 2018

Synthesis and insertion of cytochrome P-450 into endoplasmic reticulum membranes

1 reference

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1 reference

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Signal recognition particle is required for co-translational insertion of cytochrome P-450 into microsomal membranes

1 reference

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13 July 2018

Complete amino acid sequence and predicted membrane topology of phenobarbital-induced cytochrome P-450 (isozyme 2) from rabbit liver microsomes

1 reference

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1 reference

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1 reference

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1 reference

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Positive charges at the NH2 terminus convert the membrane-anchor signal peptide of cytochrome P-450 to a secretory signal peptide

1 reference

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13 July 2018

Protein glycosylation in the endoplasmic reticulum: current topological issues

1 reference

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13 July 2018

Determinants of membrane protein topology

1 reference

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13 July 2018

Signals for the incorporation and orientation of cytochrome P450 in the endoplasmic reticulum membrane

1 reference

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Multiple topogenic sequences in bovine opsin

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

1 reference

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1 reference

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The complete amino acid sequence of a constitutive form of liver microsomal cytochrome P-450

1 reference

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Ability of the hydrophobic fusion-related external domain of a paramyxovirus F protein to act as a membrane anchor

1 reference

https://pubmed.ncbi.nlm.nih.gov/2494191

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Mutations in the NH2-terminal domain of the signal peptide of preproparathyroid hormone inhibit translocation without affecting interaction with signal recognition particle

1 reference

https://pubmed.ncbi.nlm.nih.gov/2494191

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

On the membrane topology of vertebrate cytochrome P-450 proteins

1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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10.1083/JCB.108.4.1237

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Europe PubMed Central

PubMed publication ID

7 August 2017

release_ktb3sr33lzaqlh6jhod76i7jsi

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Europe PubMed Central

PubMed publication ID

7 August 2017

PubMed publication ID

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Europe PubMed Central

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7 August 2017

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