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Refinado por: assunto: srp remover Nome da Publicação: Protein Science remover
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Reprogramming chaperone pathways to improve membrane protein expression in Escherichia coli
Reprogramming chaperone pathways to improve membrane protein expression in Escherichia coli
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Reprogramming chaperone pathways to improve membrane protein expression in Escherichia coli

Nannenga, Brent L. ; Baneyx, François

Protein science, 2011-08, Vol.20 (8), p.1411-1420 [Periódico revisado por pares]

Hoboken: Wiley Subscription Services, Inc., A Wiley Company

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2
Characterization of the SRP68/72 interface of human signal recognition particle by systematic site‐directed mutagenesis
Characterization of the SRP68/72 interface of human signal recognition particle by systematic site‐directed mutagenesis
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Characterization of the SRP68/72 interface of human signal recognition particle by systematic site‐directed mutagenesis

Iakhiaeva, Elena ; Hinck, Cynthia S. ; Hinck, Andrew P. ; Zwieb, Christian

Protein science, 2009-10, Vol.18 (10), p.2183-2195 [Periódico revisado por pares]

Hoboken: Wiley Subscription Services, Inc., A Wiley Company

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3
Rational design of a fusion partner for membrane protein expression in E. coli
Rational design of a fusion partner for membrane protein expression in E. coli
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Rational design of a fusion partner for membrane protein expression in E. coli

Luo, Jianying ; Choulet, Julie ; Samuelson, James C.

Protein science, 2009-08, Vol.18 (8), p.1735-1744 [Periódico revisado por pares]

Hoboken: Wiley Subscription Services, Inc., A Wiley Company

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4
Protein SRP68 of human signal recognition particle: Identification of the RNA and SRP72 binding domains
Protein SRP68 of human signal recognition particle: Identification of the RNA and SRP72 binding domains
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Protein SRP68 of human signal recognition particle: Identification of the RNA and SRP72 binding domains

Iakhiaeva, Elena ; Bhuiyan, Shakhawat Hossain ; Yin, Jiaming ; Zwieb, Christian

Protein science, 2006-06, Vol.15 (6), p.1290-1302 [Periódico revisado por pares]

Bristol: Cold Spring Harbor Laboratory Press

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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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