Page last updated: 2024-09-05

maltoheptaose and leucine

maltoheptaose has been researched along with leucine in 2 studies

Compound Research Comparison

Studies (maltoheptaose)	Trials (maltoheptaose)	Recent Studies (post-2010) (maltoheptaose)	Studies (leucine)	Trials (leucine)	Recent Studies (post-2010) (leucine)
114	0	39	28,515	744	4,178

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Ford, C; Reilly, PJ; Sierks, MR; Svensson, B	1
Feil, SC; Gupta, A; Kemp, BE; Parker, MW; Polekhina, G; Stapleton, D; van Denderen, BJ	1

Other Studies

2 other study(ies) available for maltoheptaose and leucine

Article	Year
Functional roles and subsite locations of Leu177, Trp178 and Asn182 of Aspergillus awamori glucoamylase determined by site-directed mutagenesis. Protein engineering, 1993, Volume: 6, Issue:1 Topics: Amino Acid Sequence; Aspergillus; Base Sequence; Binding Sites; Carbohydrate Sequence; Catalysis; Glucan 1,4-alpha-Glucosidase; Glucans; Isomaltose; Leucine; Maltose; Models, Chemical; Molecular Sequence Data; Mutagenesis, Site-Directed; Sequence Homology, Amino Acid; Structure-Activity Relationship; Substrate Specificity; Tryptophan	1993
Structural basis for glycogen recognition by AMP-activated protein kinase. Structure (London, England : 1993), 2005, Volume: 13, Issue:10 Topics: Amino Acid Sequence; AMP-Activated Protein Kinases; Animals; beta-Cyclodextrins; Binding Sites; Binding, Competitive; Carbohydrate Conformation; Catalytic Domain; Crystallography, X-Ray; Glucans; Glucose; Glycogen; Leucine; Liver; Models, Molecular; Molecular Sequence Data; Multienzyme Complexes; Mutagenesis, Site-Directed; Mutation; Oligosaccharides; Protein Binding; Protein Serine-Threonine Kinases; Protein Structure, Tertiary; Protein Subunits; Rats; Sequence Homology, Amino Acid; Spectrum Analysis, Raman; Tryptophan; Water	2005

Article

Year

Functional roles and subsite locations of Leu177, Trp178 and Asn182 of Aspergillus awamori glucoamylase determined by site-directed mutagenesis.

Protein engineering, 1993, Volume: 6, Issue:1

Topics: Amino Acid Sequence; Aspergillus; Base Sequence; Binding Sites; Carbohydrate Sequence; Catalysis; Glucan 1,4-alpha-Glucosidase; Glucans; Isomaltose; Leucine; Maltose; Models, Chemical; Molecular Sequence Data; Mutagenesis, Site-Directed; Sequence Homology, Amino Acid; Structure-Activity Relationship; Substrate Specificity; Tryptophan

1993

Structural basis for glycogen recognition by AMP-activated protein kinase.

Structure (London, England : 1993), 2005, Volume: 13, Issue:10

Topics: Amino Acid Sequence; AMP-Activated Protein Kinases; Animals; beta-Cyclodextrins; Binding Sites; Binding, Competitive; Carbohydrate Conformation; Catalytic Domain; Crystallography, X-Ray; Glucans; Glucose; Glycogen; Leucine; Liver; Models, Molecular; Molecular Sequence Data; Multienzyme Complexes; Mutagenesis, Site-Directed; Mutation; Oligosaccharides; Protein Binding; Protein Serine-Threonine Kinases; Protein Structure, Tertiary; Protein Subunits; Rats; Sequence Homology, Amino Acid; Spectrum Analysis, Raman; Tryptophan; Water

2005