tryptophan and 5,10-methylenetetrahydrofolic acid

tryptophan has been researched along with 5,10-methylenetetrahydrofolic acid 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
Finer-Moore, JS; Fritz, TA; Liu, L; Stroud, RM	1
Arreola, R; Arvizu-Flores, AA; Garcia-Orozco, KD; Maley, F; Montfort, WR; Sotelo-Mundo, RR; Sugich-Miranda, R; Velazquez-Contreras, EF	1

Other Studies

2 other study(ies) available for tryptophan and 5,10-methylenetetrahydrofolic acid

Article	Year
Tryptophan 80 and leucine 143 are critical for the hydride transfer step of thymidylate synthase by controlling active site access. Biochemistry, 2002, Jun-04, Volume: 41, Issue:22 Topics: Binding Sites; Biological Transport; Deoxyuracil Nucleotides; Escherichia coli; Folic Acid; Leucine; Models, Chemical; Point Mutation; Protons; Quinazolines; Tetrahydrofolates; Thymidylate Synthase; Tryptophan	2002
Role of an invariant lysine residue in folate binding on Escherichia coli thymidylate synthase: calorimetric and crystallographic analysis of the K48Q mutant. The international journal of biochemistry & cell biology, 2008, Volume: 40, Issue:10 Topics: Amino Acid Substitution; Binding Sites; Calorimetry; Catalysis; Circular Dichroism; Crystallography, X-Ray; Escherichia coli; Folic Acid; Folic Acid Antagonists; Ligands; Lysine; Mutant Proteins; Mutation; Nucleotides; Protein Structure, Secondary; Structure-Activity Relationship; Tetrahydrofolates; Thermodynamics; Thymidylate Synthase; Tryptophan	2008

Article

Year

Tryptophan 80 and leucine 143 are critical for the hydride transfer step of thymidylate synthase by controlling active site access.

Biochemistry, 2002, Jun-04, Volume: 41, Issue:22

Topics: Binding Sites; Biological Transport; Deoxyuracil Nucleotides; Escherichia coli; Folic Acid; Leucine; Models, Chemical; Point Mutation; Protons; Quinazolines; Tetrahydrofolates; Thymidylate Synthase; Tryptophan

2002

Role of an invariant lysine residue in folate binding on Escherichia coli thymidylate synthase: calorimetric and crystallographic analysis of the K48Q mutant.

The international journal of biochemistry & cell biology, 2008, Volume: 40, Issue:10

Topics: Amino Acid Substitution; Binding Sites; Calorimetry; Catalysis; Circular Dichroism; Crystallography, X-Ray; Escherichia coli; Folic Acid; Folic Acid Antagonists; Ligands; Lysine; Mutant Proteins; Mutation; Nucleotides; Protein Structure, Secondary; Structure-Activity Relationship; Tetrahydrofolates; Thermodynamics; Thymidylate Synthase; Tryptophan

2008