| D008841 |
Actin Cytoskeleton |
Fibers composed of MICROFILAMENT PROTEINS, which are predominately ACTIN. They are the smallest of the cytoskeletal filaments. |
Actin Filaments,Microfilaments,Actin Microfilaments,Actin Cytoskeletons,Actin Filament,Actin Microfilament,Cytoskeleton, Actin,Cytoskeletons, Actin,Filament, Actin,Filaments, Actin,Microfilament,Microfilament, Actin,Microfilaments, Actin |
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| D008954 |
Models, Biological |
Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment. |
Biological Model,Biological Models,Model, Biological,Models, Biologic,Biologic Model,Biologic Models,Model, Biologic |
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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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| D009219 |
Myosin-Light-Chain Kinase |
An enzyme that phosphorylates myosin light chains in the presence of ATP to yield myosin-light chain phosphate and ADP, and requires calcium and CALMODULIN. The 20-kDa light chain is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors. The enzyme plays a central role in the regulation of smooth muscle contraction. |
Myosin Kinase,Myosin LCK,Myosin Regulatory Light-Chain Kinase,Kinase, Myosin,Kinase, Myosin-Light-Chain,LCK, Myosin,Myosin Light Chain Kinase,Myosin Regulatory Light Chain Kinase |
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| D003599 |
Cytoskeleton |
The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm. |
Cytoplasmic Filaments,Cytoskeletal Filaments,Microtrabecular Lattice,Cytoplasmic Filament,Cytoskeletal Filament,Cytoskeletons,Filament, Cytoplasmic,Filament, Cytoskeletal,Filaments, Cytoplasmic,Filaments, Cytoskeletal,Lattice, Microtrabecular,Lattices, Microtrabecular,Microtrabecular Lattices |
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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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| D004285 |
Dogs |
The domestic dog, Canis familiaris, comprising about 400 breeds, of the carnivore family CANIDAE. They are worldwide in distribution and live in association with people. (Walker's Mammals of the World, 5th ed, p1065) |
Canis familiaris,Dog |
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| D006801 |
Humans |
Members of the species Homo sapiens. |
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man |
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| D000080865 |
Formins |
A family of multidomain microfilament proteins associated with ACTIN FILAMENTS. They generally have multiple Formin-Homology domains (e.g., FH2 domain) and additionally have a RhoGTPase-binding domain and a diaphanous inhibitory domain. Formins and homologs are involved in actin reorganization. |
DIAPH Protein 1,DIAPH Protein 2,DIAPH Proteins,Diaphanous-Related Formin Homology Proteins,Diaphanous-Related Formins,FMN Protein 1,FMN Protein 2,FMN Proteins,Formin,Formin 1 Protein,Formin 2 Protein,Formin Homology Proteins,Diaphanous Related Formin Homology Proteins,Diaphanous Related Formins,Formins, Diaphanous-Related |
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| D000199 |
Actins |
Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle. |
F-Actin,G-Actin,Actin,Isoactin,N-Actin,alpha-Actin,alpha-Isoactin,beta-Actin,gamma-Actin,F Actin,G Actin,N Actin,alpha Actin,alpha Isoactin,beta Actin,gamma Actin |
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