These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
223 related articles for article (PubMed ID: 8672717)
1. A bifunctional fusion protein containing the maltose-binding polypeptide and the catalytic chain of aspartate transcarbamoylase: assembly, oligomers, and domains. Yang YR; Schachman HK Biophys Chem; 1996 Apr; 59(3):289-97. PubMed ID: 8672717 [TBL] [Abstract][Full Text] [Related]
2. In vivo formation of allosteric aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains: implications for protein folding and assembly. Zhang P; Schachman HK Protein Sci; 1996 Jul; 5(7):1290-300. PubMed ID: 8819162 [TBL] [Abstract][Full Text] [Related]
3. In vivo formation of active aspartate transcarbamoylase from complementing fragments of the catalytic polypeptide chains. Yang YR; Schachman HK Protein Sci; 1993 Jun; 2(6):1013-23. PubMed ID: 8318886 [TBL] [Abstract][Full Text] [Related]
4. In vivo assembly of aspartate transcarbamoylase from fragmented and circularly permuted catalytic polypeptide chains. Ni X; Schachman HK Protein Sci; 2001 Mar; 10(3):519-27. PubMed ID: 11344320 [TBL] [Abstract][Full Text] [Related]
5. Overexpression of bacterio-opsin in Escherichia coli as a water-soluble fusion to maltose binding protein: efficient regeneration of the fusion protein and selective cleavage with trypsin. Chen GQ; Gouaux JE Protein Sci; 1996 Mar; 5(3):456-67. PubMed ID: 8868482 [TBL] [Abstract][Full Text] [Related]
6. High-level expression of soluble protein in Escherichia coli using a His6-tag and maltose-binding-protein double-affinity fusion system. Pryor KD; Leiting B Protein Expr Purif; 1997 Aug; 10(3):309-19. PubMed ID: 9268677 [TBL] [Abstract][Full Text] [Related]
7. Fusion of the genes encoding Escherichia coli heat-stable enterotoxin b (STb) and the maltose-binding protein to obtain mature STb enterotoxin. Bossé M; Handl CE; Lortié LA; Harel J; Dubreuil JD J Gen Microbiol; 1993 Mar; 139(3):631-8. PubMed ID: 8473869 [TBL] [Abstract][Full Text] [Related]
8. Aspartate-90 and arginine-269 of hamster aspartate transcarbamylase affect the oligomeric state of a chimaeric protein with an Escherichia coli maltose-binding domain. Qiu Y; Davidson JN Biochem J; 1998 Jan; 329 ( Pt 2)(Pt 2):243-7. PubMed ID: 9425105 [TBL] [Abstract][Full Text] [Related]
9. Autoprocessing of the HIV-1 protease using purified wild-type and mutated fusion proteins expressed at high levels in Escherichia coli. Louis JM; McDonald RA; Nashed NT; Wondrak EM; Jerina DM; Oroszlan S; Mora PT Eur J Biochem; 1991 Jul; 199(2):361-9. PubMed ID: 2070793 [TBL] [Abstract][Full Text] [Related]
10. Characterization of purified recombinant Bet v 1 with authentic N-terminus, cloned in fusion with maltose-binding protein. Spangfort MD; Ipsen H; Sparholt SH; Aasmul-Olsen S; Larsen MR; Mørtz E; Roepstorff P; Larsen JN Protein Expr Purif; 1996 Nov; 8(3):365-73. PubMed ID: 8936599 [TBL] [Abstract][Full Text] [Related]
11. Single-step purification and characterization of MBP (maltose binding protein)-DnaJ fusion protein and its utilization for structure-function analysis. Ishii Y; Sonezaki S; Iwasaki Y; Tauchi E; Shingu Y; Okita K; Ogawa HI; Kato Y; Kondo A J Biochem; 1998 Oct; 124(4):842-7. PubMed ID: 9756632 [TBL] [Abstract][Full Text] [Related]
12. Peptide-protein interaction markedly alters the functional properties of the catalytic subunit of aspartate transcarbamoylase. Zhou BB; Schachman HK Protein Sci; 1993 Jan; 2(1):103-12. PubMed ID: 8443583 [TBL] [Abstract][Full Text] [Related]
13. A 70-amino acid zinc-binding polypeptide from the regulatory chain of aspartate transcarbamoylase forms a stable complex with the catalytic subunit leading to markedly altered enzyme activity. Markby DW; Zhou BB; Schachman HK Proc Natl Acad Sci U S A; 1991 Dec; 88(23):10568-72. PubMed ID: 1961722 [TBL] [Abstract][Full Text] [Related]
14. A 70-amino acid zinc-binding polypeptide fragment from the regulatory chain of aspartate transcarbamoylase causes marked changes in the kinetic mechanism of the catalytic trimer. Zhou BB; Waldrop GL; Lum L; Schachman HK Protein Sci; 1994 Jun; 3(6):967-74. PubMed ID: 8069226 [TBL] [Abstract][Full Text] [Related]
15. Reconstitution of active catalytic trimer of aspartate transcarbamoylase from proteolytically cleaved polypeptide chains. Powers VM; Yang YR; Fogli MJ; Schachman HK Protein Sci; 1993 Jun; 2(6):1001-12. PubMed ID: 8318885 [TBL] [Abstract][Full Text] [Related]
16. Thermodynamics of maltose binding protein unfolding. Novokhatny V; Ingham K Protein Sci; 1997 Jan; 6(1):141-6. PubMed ID: 9007986 [TBL] [Abstract][Full Text] [Related]
17. Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: characterization of the active site and evidence for an interdomain carboxy-terminal helix in ornithine transcarbamoylase. Murata LB; Schachman HK Protein Sci; 1996 Apr; 5(4):709-18. PubMed ID: 8845761 [TBL] [Abstract][Full Text] [Related]
18. Expression of recombinant human phenylalanine hydroxylase as fusion protein in Escherichia coli circumvents proteolytic degradation by host cell proteases. Isolation and characterization of the wild-type enzyme. Martinez A; Knappskog PM; Olafsdottir S; Døskeland AP; Eiken HG; Svebak RM; Bozzini M; Apold J; Flatmark T Biochem J; 1995 Mar; 306 ( Pt 2)(Pt 2):589-97. PubMed ID: 7887915 [TBL] [Abstract][Full Text] [Related]
19. Association of the catalytic subunit of aspartate transcarbamoylase with a zinc-containing polypeptide fragment of the regulatory chain leads to increases in thermal stability. Peterson CB; Zhou BB; Hsieh D; Creager AN; Schachman HK Protein Sci; 1994 Jun; 3(6):960-6. PubMed ID: 8069225 [TBL] [Abstract][Full Text] [Related]
20. Overproduction and purification of Lon protease from Escherichia coli using a maltose-binding protein fusion system. Sonezaki S; Kondo A; Oba T; Ishii Y; Kato Y; Nakayama H Appl Microbiol Biotechnol; 1994 Nov; 42(2-3):313-8. PubMed ID: 7765772 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]