Anopheles gambiae TEP1 forms a complex with the coiled-coil domain of LRIM1/APL1C following a conformational change in the thioester domain.
Williams, Marni
Anopheles gambiae TEP1 forms a complex with the coiled-coil domain of LRIM1/APL1C following a conformational change in the thioester domain. [electronic resource] - PloS one 2019 - e0218203 p. digital
Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
1932-6203
10.1371/journal.pone.0218203 doi
Alleles
Amino Acid Sequence
Animals
Anopheles--metabolism
Disulfides--metabolism
Esters--metabolism
Hydrolysis
Insect Proteins--chemistry
Protein Binding
Protein Domains
Protein Stability
Sulfhydryl Compounds--metabolism
Anopheles gambiae TEP1 forms a complex with the coiled-coil domain of LRIM1/APL1C following a conformational change in the thioester domain. [electronic resource] - PloS one 2019 - e0218203 p. digital
Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
1932-6203
10.1371/journal.pone.0218203 doi
Alleles
Amino Acid Sequence
Animals
Anopheles--metabolism
Disulfides--metabolism
Esters--metabolism
Hydrolysis
Insect Proteins--chemistry
Protein Binding
Protein Domains
Protein Stability
Sulfhydryl Compounds--metabolism