Overview of the purification of recombinant proteins produced in Escherichia coli.

about

Anti-human fibroblast growth factor-21 monoclonal antibody preparation, characterization and analysis of in vitro bioactivity.Screening for antifibrotic compounds using high throughput system based on fluorescence polarization.

P2860

Q37406671-A459809B-9F47-48AB-96CB-712AD821A6F2 Q42723938-06217F57-34E2-44EE-9D91-0419A0E59AE3

P2860

Overview of the purification of recombinant proteins produced in Escherichia coli.

Item

http://www.wikidata.org/entity/Q42169778

description

2003 nî lūn-bûn

@nan

2003年の論文

@ja

2003年論文

@yue

2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

2003年论文

@zh

2003年论文

@zh-cn

name

Overview of the purification of recombinant proteins produced in Escherichia coli.

@en

Overview of the purification of recombinant proteins produced in Escherichia coli.

@nl

type

Item

label

Overview of the purification of recombinant proteins produced in Escherichia coli.

@en

Overview of the purification of recombinant proteins produced in Escherichia coli.

@nl

prefLabel

Overview of the purification of recombinant proteins produced in Escherichia coli.

@en

Overview of the purification of recombinant proteins produced in Escherichia coli.

@nl

P1476

Overview of the purification of recombinant proteins produced in Escherichia coli

@en

P2093

Paul T Wingfield

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

P2860

Human immunodeficiency virus type 1 Nef binds to tumor suppressor p53 and protects cells against p53-mediated apoptosis.

Human growth hormone and extracellular domain of its receptor: crystal structure of the complex

Three-dimensional solution structure of the 44 kDa ectodomain of SIV gp41

Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm

The crystal structure of the SIV gp41 ectodomain at 1.47 A resolution

Three-dimensional structure of recombinant human interferon-gamma

A novel dimer configuration revealed by the crystal structure at 2.4 A resolution of human interleukin-5

How to measure and predict the molar absorption coefficient of a protein

Methionine or not methionine at the beginning of a protein

Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli

P304

Unit 6.1

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

P31

scholarly article

P356

10.1002/0471140864.PS0601S30

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

P478

Chapter 6

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

P50

P T Wingfield

P577

2003-02-01T00:00:00Z

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

P698

18429246

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

Overview of the purification of recombinant proteins produced in Escherichia coli.

about

P2860

P2860

Overview of the purification of recombinant proteins produced in Escherichia coli.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P478

P50

P577

P698