serine and nitrocefin

serine has been researched along with nitrocefin in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Anderson, JC; Magliery, TJ; Schultz, PG	1
Carenbauer, AL; Crowder, MW; Garrity, JD; Periyannan, G; Yates, RB	1

Other Studies

2 other study(ies) available for serine and nitrocefin

Article	Year
Expanding the genetic code: selection of efficient suppressors of four-base codons and identification of "shifty" four-base codons with a library approach in Escherichia coli. Journal of molecular biology, 2001, Mar-30, Volume: 307, Issue:3 Topics: Amino Acid Sequence; Ampicillin; Anticodon; Base Pairing; Base Sequence; beta-Lactamases; Cephalosporins; Codon; Escherichia coli; Frameshift Mutation; Gene Expression Regulation, Bacterial; Gene Library; Genes, Reporter; Genetic Code; Molecular Sequence Data; Mutagenesis; Protein Biosynthesis; RNA, Transfer; RNA, Transfer, Ser; Serine; Substrate Specificity; Suppression, Genetic	2001
Probing substrate binding to metallo-beta-lactamase L1 from Stenotrophomonas maltophilia by using site-directed mutagenesis. BMC biochemistry, 2002, Volume: 3 Topics: Asparagine; beta-Lactamases; Binding Sites; Carbapenems; Cephalosporins; Computational Biology; Isoleucine; Kinetics; Metals; Models, Molecular; Mutagenesis, Site-Directed; Penicillins; Phenylalanine; Protein Binding; Serine; Stenotrophomonas maltophilia; Tyrosine	2002

Article

Year

Expanding the genetic code: selection of efficient suppressors of four-base codons and identification of "shifty" four-base codons with a library approach in Escherichia coli.

Journal of molecular biology, 2001, Mar-30, Volume: 307, Issue:3

Topics: Amino Acid Sequence; Ampicillin; Anticodon; Base Pairing; Base Sequence; beta-Lactamases; Cephalosporins; Codon; Escherichia coli; Frameshift Mutation; Gene Expression Regulation, Bacterial; Gene Library; Genes, Reporter; Genetic Code; Molecular Sequence Data; Mutagenesis; Protein Biosynthesis; RNA, Transfer; RNA, Transfer, Ser; Serine; Substrate Specificity; Suppression, Genetic

2001

Probing substrate binding to metallo-beta-lactamase L1 from Stenotrophomonas maltophilia by using site-directed mutagenesis.

BMC biochemistry, 2002, Volume: 3

Topics: Asparagine; beta-Lactamases; Binding Sites; Carbapenems; Cephalosporins; Computational Biology; Isoleucine; Kinetics; Metals; Models, Molecular; Mutagenesis, Site-Directed; Penicillins; Phenylalanine; Protein Binding; Serine; Stenotrophomonas maltophilia; Tyrosine

2002