Protein aggregation in recombinant bacteria: biological role of inclusion bodies.
about
Quality control of inclusion bodies in Escherichia coliSequence determinants of protein aggregation: tools to increase protein solubility.Soluble expression of recombinant proteins in the cytoplasm of Escherichia coliEffects of Environmental Factors on Soluble Expression of a Humanized Anti-TNF-α scFv Antibody in Escherichia coliTherapeutic alpha-interferons protein: structure, production, and biosimilar.Isolation of biologically active nanomaterial (inclusion bodies) from bacterial cells.Overproduced Brucella abortus PdhS-mCherry forms soluble aggregates in Escherichia coli, partially associating with mobile foci of IbpA-YFP.Matrix-assisted refolding and purification of placenta-derived recombinant human interleukin-6 produced in Escherichia coli.Soluble prokaryotic overexpression and purification of bioactive human granulocyte colony-stimulating factor by maltose binding protein and protein disulfide isomerase.AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides.Controlled localization of functionally active proteins to inclusion bodies using leucine zippersA variant of green fluorescent protein exclusively deposited to active intracellular inclusion bodies.Selecting an appropriate method for expressing S locus F-box-S2 recombinant protein.Expression, isolation, and purification of soluble and insoluble biotinylated proteins for nerve tissue regeneration.Kinetic and structural characterization of human mortalinProtein solubility and differential proteomic profiling of recombinant Escherichia coli overexpressing double-tagged fusion proteins.Side effects of chaperone gene co-expression in recombinant protein production.Kinetics of inclusion body formation and its correlation with the characteristics of protein aggregates in Escherichia coli.Localization of chaperones DnaK and GroEL in bacterial inclusion bodiesRecombinant production of human interleukin 6 in Escherichia coliTargeted expression, purification, and cleavage of fusion proteins from inclusion bodies in Escherichia coli.Preparation of Phi29 DNA polymerase free of amplifiable DNA using ethidium monoazide, an ultraviolet-free light-emitting diode lamp and trehalose.Expression and in vitro functional analyses of recombinant Gam1 proteinRNA editing by T7 RNA polymerase bypasses InDel mutations causing unexpected phenotypic changes.Active protein aggregates produced in Escherichia coliKinetics of Thermal Denaturation and Aggregation of Bovine Serum Albumin.Mouse Models of Diabetes, Obesity and Related Kidney Disease.Protein folding and conformational stress in microbial cells producing recombinant proteins: a host comparative overview.Human granulocyte colony stimulating factor (hG-CSF): cloning, overexpression, purification and characterization.Heterologous expression of plasmodial proteins for structural studies and functional annotation.Microbial factories for recombinant pharmaceuticalsStudies on bacterial inclusion bodies.Functional inclusion bodies produced in the yeast Pichia pastoris.Improved activity of a thermophilic cellulase, Cel5A, from Thermotoga maritima on ionic liquid pretreated switchgrass.Protein-stabilizing and cell-penetrating properties of α-helix domain of 30Kc19 proteinMechanism of suppression of protein aggregation by α-crystallin.A novel adjuvant-free H fusion system for the production of recombinant immunogens in Escherichia coli: Its application to a 12 kDa antigen from Cryptosporidium parvum.Sense and nonsense from a systems biology approach to microbial recombinant protein production.Dynamic transcriptional response of Escherichia coli to inclusion body formation.Biological role of bacterial inclusion bodies: a model for amyloid aggregation.
P2860
Q21246020-7479E941-B6B8-464C-AE4B-C8FEFE4431D9Q24795353-C50208F3-B403-4CF0-8A4C-6F7A72B54743Q24802856-D7BA0EA2-0DCB-4C1C-9678-B6A68FD17B90Q26773076-391454F8-B883-4D88-BF78-86C5C73F1D8EQ30361968-6494E06E-3326-4BA6-A4DB-560F9DA4BEDEQ30479487-E996F34E-BB92-4910-8878-DCB2261ADE8BQ30497052-870218ED-DB3E-4B42-9EAB-95CE8614E9E5Q31147299-A0DC92C7-3CD3-444C-ADAE-84F24DF535FFQ31152401-BF8AB076-DA00-4F6A-A784-89A201E28A1DQ33275645-E15A09D2-4E18-4C5A-929A-B8D5D523EF6FQ33711412-702756E5-DA86-4282-A4BD-F03229B82561Q33726748-876D1B13-2C61-4153-B280-DBA763D0CFF9Q33824070-826F659D-FE4C-45D0-9A6B-27B3FBF06E22Q33872665-A62B95B5-09BE-4AF3-8852-65EB79418938Q33919575-46A7BB4E-DE25-4DE5-B69F-E4C9288E4354Q34133521-B9FB3055-BD29-4620-B6CD-B83923475551Q34148952-B56F7EA1-E091-4FC8-BE72-B6A54C4E2018Q34221832-0C6A390A-B326-45F8-AA98-F046665CEFA4Q34557283-69D38D51-C5A5-4CDA-B3CD-3D742E0BB03EQ34571450-20E474DA-A4D8-4542-951F-3D959E76DEFBQ34656333-7F9D0F25-79C0-4787-B41C-31DED5AD9E67Q35088016-317F2216-8330-4CEE-9403-D7EE2B485E62Q35449374-19D36B4A-4C36-4C6D-8EFE-806077BA30FDQ35562126-4FB42705-2582-4524-9041-2ACD22B08A6AQ35600257-03ABCB2A-2CDE-4105-A3FC-6C7F6767023FQ35996228-29B34AF8-395D-4D3D-ADB8-C58189BD7790Q36118363-3B45EAA2-B885-4B3F-A129-1D54357A109DQ36569895-AA8FCD3E-4A7D-4A9C-B478-3DB4BFA47A48Q36593435-8BD5BDE7-5009-442D-9C11-5F748D75FD35Q36938795-329F04B0-10B0-449B-9D30-CA54D41E6936Q37160231-E98F7E68-216C-466F-8C08-07991B07524BQ37225671-EC305C2C-EE69-4D2E-8E79-FCE5FC27B284Q37302292-5D72CAA6-2C08-422A-B8C6-43F4C1B58E6AQ37308752-81CDE306-8561-4B1F-A3E7-5F34380041D7Q37461892-47646F05-DAA8-4275-A674-47182A4923FAQ37462264-FFB5F836-EEF4-4B72-A959-05332C17EEF0Q37607769-677F3E64-FBB7-43B0-A2C0-E6C61CAABE31Q37665886-5BA0E0E2-C95C-498B-A79E-F0DE5B14FBD7Q37672418-C43C04B0-3E62-46D7-90AD-FDED9A475289Q37875227-3877C472-4131-4C2D-A982-56A5DBF604A7
P2860
Protein aggregation in recombinant bacteria: biological role of inclusion bodies.
description
2003 nî lūn-bûn
@nan
2003 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
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
name
Protein aggregation in recombinant bacteria: biological role of inclusion bodies.
@ast
Protein aggregation in recombinant bacteria: biological role of inclusion bodies.
@en
type
label
Protein aggregation in recombinant bacteria: biological role of inclusion bodies.
@ast
Protein aggregation in recombinant bacteria: biological role of inclusion bodies.
@en
prefLabel
Protein aggregation in recombinant bacteria: biological role of inclusion bodies.
@ast
Protein aggregation in recombinant bacteria: biological role of inclusion bodies.
@en
P356
P1476
Protein aggregation in recombinant bacteria: biological role of inclusion bodies
@en
P2093
M Mar Carrió
P2888
P304
P356
10.1023/A:1025024104862
P577
2003-09-01T00:00:00Z
P6179
1042702227