Mechanisms of protein folding: molecular chaperones and their application in biotechnology.
about
Soluble expression of recombinant proteins in the cytoplasm of Escherichia coliCellular disulfide bond formation in bioactive peptides and proteinsHeat shock proteins IbpA and IbpB are required for NlpI-participated cell division in Escherichia coliEnhanced bacterial expression of several mammalian cytochrome P450s by codon optimization and chaperone coexpressionChaperone-assisted folding of newly synthesized proteins in the cytosol.Understanding the relationship between the primary structure of proteins and its propensity to be soluble on overexpression in Escherichia coli.Synthesis and evaluation of xylopyranoside derivatives as "decoy acceptors" of human β-1,4-galactosyltransferase 7.Chaperone-Assisted Soluble Expression of a Humanized Anti-EGFR ScFv Antibody in E. Coli.APOBEC3H structure reveals an unusual mechanism of interaction with duplex RNA.Production of soluble eukaryotic recombinant proteins in E. coli is favoured in early log-phase cultures induced at low temperature.A strategy for high-level expression of soluble and functional human interferon alpha as a GST-fusion protein in E. coli.Protein Secretion in Gram-Positive Bacteria: From Multiple Pathways to Biotechnology.Refolding of Aggregation-Prone ScFv Antibody Fragments Assisted by Hydrophobically Modified Poly(sodium acrylate) Derivatives.Structural stability and unfolding properties of cutinases from Thermobifida fusca.Glycosylation of various flavonoids by recombinant oleandomycin glycosyltransferase from Streptomyces antibioticus in batch and repeated batch modes.
P2860
Q24802856-46B6578F-90C8-47E6-B7BA-54C3FAFA3F57Q28080871-13A5E67B-AB79-4BFE-A2BC-F1F74BDD6755Q28650489-BB81CAC3-541F-4132-800E-E8BC029E43AAQ34300984-12858F3B-851D-4DA9-A867-DA0E2438CBA4Q36069355-440F3265-8B42-4619-A475-61C17C65D5B7Q36518002-B0037CC3-82C4-4025-A5C7-A6641D017272Q39590858-DDC8EDF3-EC65-4473-AD28-9D739D9103D6Q42012779-2F1812C1-FE46-406E-9F6E-8F3A37AADEE9Q42380169-24B062AF-2681-4704-9E19-BDF78766EA51Q43224422-F5958849-029A-49B5-889C-B3872A13A25CQ51026480-0F9FC630-2FDB-4CA3-9A92-E9FC6306020CQ51093436-DDAA0713-4D98-42B4-B724-6918029FC67DQ51557597-728FDE52-2B48-417F-B44A-70E9AFB4FBBBQ53480231-2497BAA7-1D9E-46ED-96E2-5A4EF2CA8F66Q54348041-D396557F-8CF7-4DAE-B430-779933EEED75
P2860
Mechanisms of protein folding: molecular chaperones and their application in biotechnology.
description
2002 nî lūn-bûn
@nan
2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Mechanisms of protein folding: ...... application in biotechnology.
@ast
Mechanisms of protein folding: ...... application in biotechnology.
@en
Mechanisms of protein folding: ...... application in biotechnology.
@nl
type
label
Mechanisms of protein folding: ...... application in biotechnology.
@ast
Mechanisms of protein folding: ...... application in biotechnology.
@en
Mechanisms of protein folding: ...... application in biotechnology.
@nl
prefLabel
Mechanisms of protein folding: ...... application in biotechnology.
@ast
Mechanisms of protein folding: ...... application in biotechnology.
@en
Mechanisms of protein folding: ...... application in biotechnology.
@nl
P921
P1433
P1476
Mechanisms of protein folding: ...... application in biotechnology.
@en
P2093
Matthias P Mayer
P304
P356
10.1002/1439-7633(20020902)3:9<807::AID-CBIC807>3.0.CO;2-A
P577
2002-09-01T00:00:00Z