186 related articles for article (PubMed ID: 11231008)
1. Protein aggregation as bacterial inclusion bodies is reversible.
Carrió MM; Villaverde A
FEBS Lett; 2001 Jan; 489(1):29-33. PubMed ID: 11231008
[TBL] [Abstract][Full Text] [Related]
2. Amyloid-like properties of bacterial inclusion bodies.
Carrió M; González-Montalbán N; Vera A; Villaverde A; Ventura S
J Mol Biol; 2005 Apr; 347(5):1025-37. PubMed ID: 15784261
[TBL] [Abstract][Full Text] [Related]
3. Localization of functional polypeptides in bacterial inclusion bodies.
García-Fruitós E; Arís A; Villaverde A
Appl Environ Microbiol; 2007 Jan; 73(1):289-94. PubMed ID: 17085715
[TBL] [Abstract][Full Text] [Related]
4. Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production in Escherichia coli.
Rinas U; Hoffmann F; Betiku E; Estapé D; Marten S
J Biotechnol; 2007 Jan; 127(2):244-57. PubMed ID: 16945443
[TBL] [Abstract][Full Text] [Related]
5. Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates.
de Groot NS; Ventura S
J Biotechnol; 2006 Aug; 125(1):110-3. PubMed ID: 16621081
[TBL] [Abstract][Full Text] [Related]
6. In situ protein folding and activation in bacterial inclusion bodies.
Gonzalez-Montalban N; Natalello A; García-Fruitós E; Villaverde A; Doglia SM
Biotechnol Bioeng; 2008 Jul; 100(4):797-802. PubMed ID: 18351678
[TBL] [Abstract][Full Text] [Related]
7. Refolding of alpha 1-antitrypsin expressed as inclusion bodies in Escherichia coli: characterization of aggregation.
Kwon KS; Lee S; Yu MH
Biochim Biophys Acta; 1995 Mar; 1247(2):179-84. PubMed ID: 7696306
[TBL] [Abstract][Full Text] [Related]
8. Test bacterial inclusion body for activity prior to start denaturing and refolding processes to obtain active eukaryotic proteins.
Hamidi SR; Safdari Y; Sheikh Arabi M
Protein Expr Purif; 2019 Feb; 154():147-151. PubMed ID: 30389592
[TBL] [Abstract][Full Text] [Related]
9. Solubility of proteins isolated from inclusion bodies is enhanced by fusion to maltose-binding protein or thioredoxin.
Sachdev D; Chirgwin JM
Protein Expr Purif; 1998 Feb; 12(1):122-32. PubMed ID: 9473466
[TBL] [Abstract][Full Text] [Related]
10. Modeling of protein refolding from inclusion bodies.
Zhang T; Xu X; Shen L; Feng Y; Yang Z; Shen Y; Wang J; Jin W; Wang X
Acta Biochim Biophys Sin (Shanghai); 2009 Dec; 41(12):1044-52. PubMed ID: 20011979
[TBL] [Abstract][Full Text] [Related]
11. Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body composition.
Speed MA; Wang DI; King J
Nat Biotechnol; 1996 Oct; 14(10):1283-7. PubMed ID: 9631094
[TBL] [Abstract][Full Text] [Related]
12. Divergent genetic control of protein solubility and conformational quality in Escherichia coli.
García-Fruitós E; Martínez-Alonso M; Gonzàlez-Montalbán N; Valli M; Mattanovich D; Villaverde A
J Mol Biol; 2007 Nov; 374(1):195-205. PubMed ID: 17920630
[TBL] [Abstract][Full Text] [Related]
13. Fine architecture of bacterial inclusion bodies.
Carrió MM; Cubarsi R; Villaverde A
FEBS Lett; 2000 Apr; 471(1):7-11. PubMed ID: 10760503
[TBL] [Abstract][Full Text] [Related]
14. Superactive β-galactosidase inclusion bodies.
Flores SS; Nolan V; Perillo MA; Sánchez JM
Colloids Surf B Biointerfaces; 2019 Jan; 173():769-775. PubMed ID: 30384274
[TBL] [Abstract][Full Text] [Related]
15. Efficient production of a correctly folded mouse α-defensin, cryptdin-4, by refolding during inclusion body solubilization.
Tomisawa S; Sato Y; Kamiya M; Kumaki Y; Kikukawa T; Kawano K; Demura M; Nakamura K; Ayabe T; Aizawa T
Protein Expr Purif; 2015 Aug; 112():21-8. PubMed ID: 25913370
[TBL] [Abstract][Full Text] [Related]
16. Comparing the refolding and reoxidation of recombinant porcine growth hormone from a urea denatured state and from Escherichia coli inclusion bodies.
Cardamone M; Puri NK; Brandon MR
Biochemistry; 1995 May; 34(17):5773-94. PubMed ID: 7727438
[TBL] [Abstract][Full Text] [Related]
17. Soybean disease resistance protein RHG1-LRR domain expressed, purified and refolded from Escherichia coli inclusion bodies: preparation for a functional analysis.
Afzal AJ; Lightfoot DA
Protein Expr Purif; 2007 Jun; 53(2):346-55. PubMed ID: 17287130
[TBL] [Abstract][Full Text] [Related]
18. Concepts and tools to exploit the potential of bacterial inclusion bodies in protein science and biotechnology.
Gatti-Lafranconi P; Natalello A; Ami D; Doglia SM; Lotti M
FEBS J; 2011 Jul; 278(14):2408-18. PubMed ID: 21569207
[TBL] [Abstract][Full Text] [Related]
19. Recovery of functionally-active protein from inclusion bodies using a thermal-cycling method.
Sadavarte R; Filipe CD; Ghosh R
Biotechnol Prog; 2017 Jan; 33(1):133-139. PubMed ID: 27690284
[TBL] [Abstract][Full Text] [Related]
20. Refolding of therapeutic proteins produced in Escherichia coli as inclusion bodies.
Misawa S; Kumagai I
Biopolymers; 1999; 51(4):297-307. PubMed ID: 10618597
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
