Characterization of the aggregates formed during recombinant protein expression in bacteria
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
1471-2091
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
online resource.
- Erschienen in
-
Characterization of the aggregates formed during recombinant protein expression in bacteria ; volume:6 ; number:1 ; day:31 ; month:5 ; year:2005 ; pages:1-11 ; date:12.2005
BMC biochemistry ; 6, Heft 1 (31.5.2005), 1-11, 12.2005
- Urheber
-
Schrödel, Andrea
- Beteiligte Personen und Organisationen
-
de Marco, Ario
SpringerLink (Online service)
- DOI
-
10.1186/1471-2091-6-10
- URN
-
urn:nbn:de:1111-201603027320
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
15.08.2025, 07:27 MESZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Schrödel, Andrea
- de Marco, Ario
- SpringerLink (Online service)
Ähnliche Objekte (12)
Cell-mineral aggregates formed by Fe(ll)-oxidizing bacteria : their internal structure and capability for nickel immobilization
Bioaccessibility Characterization of Organic Matter, Nitrogen, and Phosphorus from Microalgae-Bacteria Aggregates
Production of indigo by recombinant bacteria
The Ability of Froth Formed without Chemicals to Hold Bacteria
DJ-1 can inhibit microtubule associated protein 1 B formed aggregates
Fate and propagation of endogenously formed Tau aggregates in neuronal cells
Supernatant of plant-associated bacteria potency against biofilms formed by foodborne pathogen and food spoilage bacteria
Characterization of lower bainite formed below M S *
Selection and characterization of a promoter for expression of single-copy recombinant genes in Gram-positive bacteria
Strain engineering for improved expression of recombinant proteins in bacteria
Lactic acid bacteria: a promising alternative for recombinant protein production
Genetic tools for the development of recombinant lactic acid bacteria
Cell-mineral aggregates formed by Fe(ll)-oxidizing bacteria : their internal structure and capability for nickel immobilization
Bioaccessibility Characterization of Organic Matter, Nitrogen, and Phosphorus from Microalgae-Bacteria Aggregates
Production of indigo by recombinant bacteria
The Ability of Froth Formed without Chemicals to Hold Bacteria
DJ-1 can inhibit microtubule associated protein 1 B formed aggregates
Fate and propagation of endogenously formed Tau aggregates in neuronal cells
Supernatant of plant-associated bacteria potency against biofilms formed by foodborne pathogen and food spoilage bacteria
Characterization of lower bainite formed below M S *
Selection and characterization of a promoter for expression of single-copy recombinant genes in Gram-positive bacteria
Strain engineering for improved expression of recombinant proteins in bacteria
Lactic acid bacteria: a promising alternative for recombinant protein production
Genetic tools for the development of recombinant lactic acid bacteria
Cell-mineral aggregates formed by Fe(ll)-oxidizing bacteria : their internal structure and capability for nickel immobilization
Bioaccessibility Characterization of Organic Matter, Nitrogen, and Phosphorus from Microalgae-Bacteria Aggregates
Production of indigo by recombinant bacteria
The Ability of Froth Formed without Chemicals to Hold Bacteria
DJ-1 can inhibit microtubule associated protein 1 B formed aggregates
Fate and propagation of endogenously formed Tau aggregates in neuronal cells
Supernatant of plant-associated bacteria potency against biofilms formed by foodborne pathogen and food spoilage bacteria
Characterization of lower bainite formed below M S *
Selection and characterization of a promoter for expression of single-copy recombinant genes in Gram-positive bacteria
Strain engineering for improved expression of recombinant proteins in bacteria
Lactic acid bacteria: a promising alternative for recombinant protein production