Export of a hyperexpressed mammalian globular cytochrome b5 precursor in Escherichia coli is dramatically affected by the nature of the amino acid flanking the secretory signal sequence cleavage bond

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Optimisation of signal peptide for recombinant protein secretion in bacterial hosts.

P2860

Q38093106-C342FAF7-9955-411D-8FBB-F953B5F2CFE6

P2860

Export of a hyperexpressed mammalian globular cytochrome b5 precursor in Escherichia coli is dramatically affected by the nature of the amino acid flanking the secretory signal sequence cleavage bond

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http://www.wikidata.org/entity/Q42379488

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2010 nî lūn-bûn

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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Export of a hyperexpressed mam ...... signal sequence cleavage bond

@en

Export of a hyperexpressed mam ...... signal sequence cleavage bond

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Item

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Export of a hyperexpressed mam ...... signal sequence cleavage bond

@en

Export of a hyperexpressed mam ...... signal sequence cleavage bond

@nl

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Export of a hyperexpressed mam ...... signal sequence cleavage bond

@en

Export of a hyperexpressed mam ...... signal sequence cleavage bond

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P1476

Export of a hyperexpressed mam ...... signal sequence cleavage bond

@en

P2093

Khalil Ahmed

http://www.w3.org/2001/XMLSchema#string

Mustak A Kaderbhai

http://www.w3.org/2001/XMLSchema#string

Naheed N Kaderbhai

http://www.w3.org/2001/XMLSchema#string

P2860

Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites

In vivo half-life of a protein is a function of its amino-terminal residue

The nature of the accessible and buried surfaces in proteins

The complete general secretory pathway in gram-negative bacteria

Modeling Escherichia coli signal peptidase complex with bound substrate: determinants in the mature peptide influencing signal peptide cleavage

Alteration of the amino terminus of the mature sequence of a periplasmic protein can severely affect protein export in Escherichia coli.

The net charge of the first 18 residues of the mature sequence affects protein translocation across the cytoplasmic membrane of gram-negative bacteria.

Ser/Thr/Tyr protein phosphorylation in bacteria - for long time neglected, now well established.

P304

1344-1353

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1002/PRO.411

http://www.w3.org/2001/XMLSchema#string

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P577

2010-07-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

44634014

http://www.w3.org/2001/XMLSchema#string

P698

20506367

http://www.w3.org/2001/XMLSchema#string

P932

2974826

http://www.w3.org/2001/XMLSchema#string

Export of a hyperexpressed mammalian globular cytochrome b5 precursor in Escherichia coli is dramatically affected by the nature of the amino acid flanking the secretory signal sequence cleavage bond

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P2860

P2860

Export of a hyperexpressed mammalian globular cytochrome b5 precursor in Escherichia coli is dramatically affected by the nature of the amino acid flanking the secretory signal sequence cleavage bond

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