Colicins. Colicin A . Colicin B . Colicin E . Colicin E1 . Colicin E2 . Colicin E3 . Colicin E8 . Colicin HSC10 . Colicin Ia . Colicin Ib . Colicin K . Colicin K-K235 . Colicin M . Colicin N . Colicin V . Colicins E . Colicins E9 . Precolicin E1 . Colicin K K235 . Colicines . Bacteriocins elaborated by strains of Escherichia coli and related species. They are proteins or protein-lipopolysaccharide complexes lethal to other strains of the same species. . 1.00
Acarbose. Bay g 5421 . Glucobay . Glucor . Glumida . Prandase . Precose . An inhibitor of ALPHA-GLUCOSIDASES that retards the digestion and absorption of DIETARY CARBOHYDRATES in the SMALL INTESTINE. . 0.45
Plasminogen Activator Inhibitor 1. SERPINE1 Protein . Serpin E1 . Type 1 Plasminogen Activator Inhibitor . E1, Serpin . Protein, SERPINE1 . PAI-1 . A member of the serpin family of proteins. It inhibits both the tissue-type and urokinase-type plasminogen activators. . 0.44
Adenovirus E1 Proteins. E1 Proteins, Adenovirus . Proteins, Adenovirus E1 . The very first viral gene products synthesized after cells are infected with adenovirus. The E1 region of the genome has been divided into two major transcriptional units, E1A and E1B, each expressing proteins of the same name (ADENOVIRUS E1A PROTEINS and ADENOVIRUS E1B PROTEINS). . 0.36
P-type ATPases. E1-E2 ATPases . P-type Adenosine Triphosphatases . Phosphorylation-type ATPases . Phosphorylation-type Adenosine Triphosphatases . ATPases, E1-E2 . ATPases, P-type . ATPases, Phosphorylation-type . Adenosine Triphosphatases, P-type . Adenosine Triphosphatases, Phosphorylation-type . E1 E2 ATPases . P type ATPases . P type Adenosine Triphosphatases . Phosphorylation type ATPases . Phosphorylation type Adenosine Triphosphatases . Triphosphatases, P-type Adenosine . Triphosphatases, Phosphorylation-type Adenosine . A highly conserved family of ATPases that facilitate the transport of lipids and cations across the plasma membrane. Structurally, they are elongated ALPHA-HELICES constituting five functionally distinct domains: three cytoplasmic domains A, N, and P which contain the catalytic sites, and two transmembrane domains. The N domain phosphorylates the P-domain at an invariant ASPARTATE residue, which, in turn, is dephosphorylated by the A domain. The phosphorylation and dephosphorylation cycles drive conformational changes in the protein between two states (E1 and E2), which allow the substrate to access the other side of the membrane. . 0.36