(Q54535920)

English

Recombinant human insulin IX. Investigation of factors, influencing the folding of fusion protein-S-sulfonates, biotechnological precursors of human insulin.

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Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12406671

Recombinant human insulin IX. Investigation of factors, influencing the folding of fusion protein-S-sulfonates, biotechnological precursors of human insulin. (English)

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12406671

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protein folding

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1 reference

based on heuristic

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author name string

Roman V Tikhonov

1

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12406671

Sergey E Pechenov

2

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12406671

Irina A Belacheu

3

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12406671

Sergey A Yakimov

4

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12406671

Vadim E Klyushnichenko

5

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12406671

Heloisa Tunes

6

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12406671

Josef E Thiemann

7

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12406671

Luciano Vilela

8

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12406671

Andrey N Wulfson

9

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12406671

publication date

1 November 2002

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12406671

Protein Expression and Purification

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12406671

26

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12406671

2

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12406671

187-193

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12406671

Advances in refolding of proteins produced in E. coli

1 reference

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7 January 2021

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Recombinant human insulin

1 reference

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Metal affinity engineering of proinsulin carrying genetically attached (His)10-X-Met affinity tail and removal of the tag by cyanogen bromide.

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Production of human insulin in an E. coli system with Met-Lys-human proinsulin as the expressed precursor.

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Expression and folding of an interleukin-2-proinsulin fusion protein and its conversion into insulin by a single step enzymatic removal of the C-peptide and the N-terminal fused sequence.

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Convenient and efficient in vitro folding of disulfide-containing globular protein from crude bacterial inclusion bodies

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Recombinant human insulin. VIII. Isolation of fusion protein--S-sulfonate, biotechnological precursor of human insulin, from the biomass of transformed Escherichia coli cells

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Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network.

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Proteinotopic feature maps

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

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In vitro folding of inclusion body proteins.

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Recombinant human insulin. III. High-performance liquid chromatography and high-performance capillary electrophoresis control in the analysis of step-by-step production of recombinant human insulin

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https://api.crossref.org/works/10.1016%2FS1046-5928%2802%2900531-4

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Refolding of recombinant proteins

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Efficient in vitro folding of the three-disulfide derivatives of hen lysozyme in the presence of glycerol

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Purification of overproduced Escherichia coli RNA polymerase sigma factors by solubilizing inclusion bodies and refolding from Sarkosyl

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Pathway of detergent-mediated and peptide ligand-mediated refolding of heterodimeric class II major histocompatibility complex (MHC) molecules

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Comparing the refolding and reoxidation of recombinant porcine growth hormone from a urea denatured state and from Escherichia coli inclusion bodies.

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Effect of additives on the renaturation of reduced lysozyme in the presence of 4 M urea.

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Effect of inclusion body contaminants on the oxidative renaturation of hen egg white lysozyme

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[Methods of preparation of recombinant proteins-cytokines. IV. Renaturation of recombinant human interleukin-3]

1 reference

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7 January 2021

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A general approach to renaturation of recombinant proteins produced as inclusion bodies

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7 January 2021

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Identifiers

10.1016/S1046-5928(02)00531-4

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12406671

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

31 May 2018

http://europepmc.org/abstract/MED/12406671

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