| D008297 |
Male |
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Males |
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| D008562 |
Membrane Glycoproteins |
Glycoproteins found on the membrane or surface of cells. |
Cell Surface Glycoproteins,Surface Glycoproteins,Cell Surface Glycoprotein,Membrane Glycoprotein,Surface Glycoprotein,Glycoprotein, Cell Surface,Glycoprotein, Membrane,Glycoprotein, Surface,Glycoproteins, Cell Surface,Glycoproteins, Membrane,Glycoproteins, Surface,Surface Glycoprotein, Cell,Surface Glycoproteins, Cell |
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| D008810 |
Mice, Inbred C57BL |
One of the first INBRED MOUSE STRAINS to be sequenced. This strain is commonly used as genetic background for transgenic mouse models. Refractory to many tumors, this strain is also preferred model for studying role of genetic variations in development of diseases. |
Mice, C57BL,Mouse, C57BL,Mouse, Inbred C57BL,C57BL Mice,C57BL Mice, Inbred,C57BL Mouse,C57BL Mouse, Inbred,Inbred C57BL Mice,Inbred C57BL Mouse |
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| D008840 |
Microfilament Proteins |
Monomeric subunits of primarily globular ACTIN and found in the cytoplasmic matrix of almost all cells. They are often associated with microtubules and may play a role in cytoskeletal function and/or mediate movement of the cell or the organelles within the cell. |
Actin Binding Protein,Actin-Binding Protein,Actin-Binding Proteins,Microfilament Protein,Actin Binding Proteins,Binding Protein, Actin,Protein, Actin Binding,Protein, Actin-Binding,Protein, Microfilament,Proteins, Actin-Binding,Proteins, Microfilament |
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| D009218 |
Myosins |
A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain. |
Myosin ATPase,ATPase, Actin-Activated,ATPase, Actomyosin,ATPase, Myosin,Actin-Activated ATPase,Actomyosin ATPase,Actomyosin Adenosinetriphosphatase,Adenosine Triphosphatase, Myosin,Adenosinetriphosphatase, Actomyosin,Adenosinetriphosphatase, Myosin,Myosin,Myosin Adenosinetriphosphatase,ATPase, Actin Activated,Actin Activated ATPase,Myosin Adenosine Triphosphatase |
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| D011950 |
Receptors, Cholinergic |
Cell surface proteins that bind acetylcholine with high affinity and trigger intracellular changes influencing the behavior of cells. Cholinergic receptors are divided into two major classes, muscarinic and nicotinic, based originally on their affinity for nicotine and muscarine. Each group is further subdivided based on pharmacology, location, mode of action, and/or molecular biology. |
ACh Receptor,Acetylcholine Receptor,Acetylcholine Receptors,Cholinergic Receptor,Cholinergic Receptors,Cholinoceptive Sites,Cholinoceptor,Cholinoceptors,Receptors, Acetylcholine,ACh Receptors,Receptors, ACh,Receptor, ACh,Receptor, Acetylcholine,Receptor, Cholinergic,Sites, Cholinoceptive |
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| D002454 |
Cell Differentiation |
Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs. |
Differentiation, Cell,Cell Differentiations,Differentiations, Cell |
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| D002461 |
Cell Line, Transformed |
Eukaryotic cell line obtained in a quiescent or stationary phase which undergoes conversion to a state of unregulated growth in culture, resembling an in vitro tumor. It occurs spontaneously or through interaction with viruses, oncogenes, radiation, or drugs/chemicals. |
Transformed Cell Line,Cell Lines, Transformed,Transformed Cell Lines |
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| D004268 |
DNA-Binding Proteins |
Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases. |
DNA Helix Destabilizing Proteins,DNA-Binding Protein,Single-Stranded DNA Binding Proteins,DNA Binding Protein,DNA Single-Stranded Binding Protein,SS DNA BP,Single-Stranded DNA-Binding Protein,Binding Protein, DNA,DNA Binding Proteins,DNA Single Stranded Binding Protein,DNA-Binding Protein, Single-Stranded,Protein, DNA-Binding,Single Stranded DNA Binding Protein,Single Stranded DNA Binding Proteins |
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| D004398 |
Dyneins |
A family of multi-subunit cytoskeletal motor proteins that use the energy of ATP hydrolysis, generated by a ring of AAA ATPASES in the dynein heavy chain, to power a variety of cellular functions. Dyneins fall into two major classes based upon structural and functional criteria. |
ATPase, Dynein,Adenosinetriphosphatase, Dynein,Dynein,Dynein ATPase,Dynein Adenosinetriphosphatase,Dynein Heavy Chain,Dynein Intermediate Chain,Dynein Light Chain,Dynein Light Intermediate Chain,Adenosine Triphosphatase, Dynein,Dynein Heavy Chains,Dynein Intermediate Chains,Dynein Light Chains,Dynein Light Intermediate Chains,Chain, Dynein Heavy,Chain, Dynein Intermediate,Chain, Dynein Light,Chains, Dynein Heavy,Chains, Dynein Intermediate,Chains, Dynein Light,Dynein Adenosine Triphosphatase,Heavy Chain, Dynein,Heavy Chains, Dynein,Intermediate Chain, Dynein,Intermediate Chains, Dynein,Light Chain, Dynein,Light Chains, Dynein |
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