| D003087 |
Colicins |
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. |
Colicin,Colicin E9,Colicine,Colicines,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,E9, Colicin |
|
| D004926 |
Escherichia coli |
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. |
Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli |
|
| D001425 |
Bacterial Outer Membrane Proteins |
Proteins isolated from the outer membrane of Gram-negative bacteria. |
OMP Proteins,Outer Membrane Proteins, Bacterial,Outer Membrane Lipoproteins, Bacterial |
|
| D017434 |
Protein Structure, Tertiary |
The level of protein structure in which combinations of secondary protein structures (ALPHA HELICES; BETA SHEETS; loop regions, and AMINO ACID MOTIFS) pack together to form folded shapes. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. |
Tertiary Protein Structure,Protein Structures, Tertiary,Tertiary Protein Structures |
|
| D018000 |
Receptors, Peptide |
Cell surface receptors that bind peptide messengers with high affinity and regulate intracellular signals which influence the behavior of cells. |
Peptide Hormone Receptors,Peptide Receptors,Peptide Hormone Receptor,Peptide Receptor,Receptors, Peptide Hormones,Receptors, Peptides,Hormone Receptor, Peptide,Hormone Receptors, Peptide,Hormones Receptors, Peptide,Peptide Hormones Receptors,Peptides Receptors,Receptor, Peptide,Receptor, Peptide Hormone,Receptors, Peptide Hormone |
|
| D018272 |
Porins |
Porins are protein molecules that were originally found in the outer membrane of GRAM-NEGATIVE BACTERIA and that form multi-meric channels for the passive DIFFUSION of WATER; IONS; or other small molecules. Porins are present in bacterial CELL WALLS, as well as in plant, fungal, mammalian and other vertebrate CELL MEMBRANES and MITOCHONDRIAL MEMBRANES. |
Pore Protein,Pore Proteins,Porin,Protein, Pore,Proteins, Pore |
|
| D026901 |
Membrane Transport Proteins |
Membrane proteins whose primary function is to facilitate the transport of molecules across a biological membrane. Included in this broad category are proteins involved in active transport (BIOLOGICAL TRANSPORT, ACTIVE), facilitated transport and ION CHANNELS. |
Biological Pump,Membrane Transport Protein,Membrane Transporter,Membrane Transporters,Metabolic Pump,Permease,Biological Pumps,Metabolic Pumps,Permeases,Pump, Biologic,Pump, Biological,Pump, Metabolic,Pumps, Biological,Pumps, Metabolic,Biologic Pump,Protein, Membrane Transport,Transport Protein, Membrane,Transport Proteins, Membrane,Transporter, Membrane,Transporters, Membrane |
|
| D029968 |
Escherichia coli Proteins |
Proteins obtained from ESCHERICHIA COLI. |
E coli Proteins |
|
-transparent.png){kind=logo}
