about
Highly homologous proteins exert opposite biological activities by using different interaction interfacesLatest approaches for efficient protein production in drug discovery.Native Electrophoresis-Coupled Activity Assays Reveal Catalytically-Active Protein Aggregates of Escherichia coli β-Glucuronidase.High Level Expression and Purification of Recombinant Proteins from Escherichia coli with AK-TAG.Prokaryotic Soluble Overexpression and Purification of Human VEGF165 by Fusion to a Maltose Binding Protein TagPurification and biochemical characterization of recombinant Persicaria minor β-sesquiphellandrene synthase.Quality assessment and optimization of purified protein samples: why and how?Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104.Tools to cope with difficult-to-express proteins.Optimization of expression and purification of HSPA6 protein from Camelus dromedarius in E. coli.In vitro gene expression-coupled bacterial cell chip for screening species-specific antimicrobial enzymes.The vapB-vapC Operon of Acidovorax citrulli Functions as a Bona-fide Toxin-Antitoxin ModuleQuarterly intrinsic disorder digest (January-February-March, 2014).Soluble cysteine-rich tick saliva proteins Salp15 and Iric-1 from E. coli.Guidelines to reach high-quality purified recombinant proteins.Biochemical characterization of INTS3 and C9ORF80, two subunits of hNABP1/2 heterotrimeric complex in nucleic acid binding.Purification of Proteins Fused to Maltose-Binding Protein.Use of the SHuffle Strains in Production of Proteins.Protein fusion tags for efficient expression and purification of recombinant proteins in the periplasmic space of E. coli.High yields of active Thermus thermophilus proline dehydrogenase are obtained using maltose-binding protein as a solubility tag.Bioinformatic and Analyses of Arabidopsis Starch Synthase 2 Reveal Post-translational Regulatory MechanismsSpider silk inspired materials and sustainability: perspective
P2860
Q30009145-22AF22B4-DE31-441F-A3BC-6C7DE6511C34Q35209937-9925497A-363E-4C4D-9C8E-C8A82F094854Q35677002-364CC3C6-A13D-4BB1-A3DF-98F467BC1424Q36026736-41308C18-0DE4-40EB-88BB-10630571CE36Q36032180-C00EDC04-24D4-42CE-B61F-66222E8C15E9Q37676965-A1572CAF-390B-4FAF-8FBE-D000E9F77484Q38303016-431FC2EA-1A87-4C72-9D2F-EE1D66A4C685Q38648239-6118FD57-09A8-4F86-9C56-0A2686CC9FA8Q38808506-91E7C289-F3AA-4441-AD2D-8D103C57DE61Q39802001-B33CAA0B-5387-4C9A-BDF2-313F071734AEQ40267392-4981F59A-AFDC-4281-ACFD-7B46BE5AEF63Q40829045-671DB5C3-D431-4345-A3ED-FE166BCD4592Q42320840-62E878A4-9236-499D-80A3-B95540900B43Q43118363-31A0C6CC-6D2B-4515-A644-6858CD38CD51Q47335936-E5D49EBD-9206-4318-967F-0A8C4ECE6AA3Q47390436-4F5BE6EE-4975-496F-A914-8AB34F823A5AQ51404677-F811FE95-76EA-48C2-A123-213006B89E5CQ51602297-799A9311-5DAC-4018-9DF9-FDB74EAD59F0Q53230714-410D37D7-1206-4D7F-B878-97F6558A860BQ54276023-851E1074-A3D7-4577-A9BD-A3580A6F7975Q57073096-87613186-0FD1-44BA-ABC2-8395ED05034EQ57189700-C527C0B6-5327-4C75-B2A5-015C5D121ACF
P2860
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年学术文章
@wuu
2013年学术文章
@zh-cn
2013年学术文章
@zh-hans
2013年学术文章
@zh-my
2013年学术文章
@zh-sg
2013年學術文章
@yue
2013年學術文章
@zh
2013年學術文章
@zh-hant
name
Production of prone-to-aggregate proteins.
@en
type
label
Production of prone-to-aggregate proteins.
@en
prefLabel
Production of prone-to-aggregate proteins.
@en
P2860
P1433
P1476
Production of prone-to-aggregate proteins.
@en
P2093
Mario Lebendiker
Tsafi Danieli
P2860
P304
P356
10.1016/J.FEBSLET.2013.10.044
P407
P577
2013-11-06T00:00:00Z