| D009131 |
Muscle, Smooth, Vascular |
The nonstriated involuntary muscle tissue of blood vessels. |
Vascular Smooth Muscle,Muscle, Vascular Smooth,Muscles, Vascular Smooth,Smooth Muscle, Vascular,Smooth Muscles, Vascular,Vascular Smooth Muscles |
|
| 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 |
|
| D009320 |
Atrial Natriuretic Factor |
A potent natriuretic and vasodilatory peptide or mixture of different-sized low molecular weight PEPTIDES derived from a common precursor and secreted mainly by the HEART ATRIUM. All these peptides share a sequence of about 20 AMINO ACIDS. |
ANF,ANP,Atrial Natriuretic Peptide,Atrial Natriuretic Peptides,Atriopeptins,Auriculin,Natriuretic Peptides, Atrial,ANF (1-126),ANF (1-28),ANF (99-126),ANF Precursors,ANP (1-126),ANP (1-28),ANP Prohormone (99-126),ANP-(99-126),Atrial Natriuretic Factor (1-126),Atrial Natriuretic Factor (1-28),Atrial Natriuretic Factor (99-126),Atrial Natriuretic Factor Precursors,Atrial Natriuretic Factor Prohormone,Atrial Natriuretic Peptide (1-126),Atrial Pronatriodilatin,Atriopeptigen,Atriopeptin (1-28),Atriopeptin (99-126),Atriopeptin 126,Atriopeptin Prohormone (1-126),Cardiodilatin (99-126),Cardiodilatin Precursor,Cardionatrin I,Cardionatrin IV,Prepro-ANP,Prepro-CDD-ANF,Prepro-Cardiodilatin-Atrial Natriuretic Factor,Pro-ANF,ProANF,Proatrial Natriuretic Factor,Pronatriodilatin,alpha ANP,alpha-ANP Dimer,alpha-Atrial Natriuretic Peptide,beta-ANP,beta-Atrial Natriuretic Peptide,gamma ANP (99-126),gamma-Atrial Natriuretic Peptide,Natriuretic Peptide, Atrial,Peptide, Atrial Natriuretic,Peptides, Atrial Natriuretic,Prepro ANP,Prepro CDD ANF,Prepro Cardiodilatin Atrial Natriuretic Factor,Pro ANF,alpha ANP Dimer,alpha Atrial Natriuretic Peptide,beta ANP,beta Atrial Natriuretic Peptide,gamma Atrial Natriuretic Peptide |
|
| D010716 |
Phosphatidylinositols |
Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to the hexahydroxy alcohol, myo-inositol. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid, myo-inositol, and 2 moles of fatty acids. |
Inositide Phospholipid,Inositol Phosphoglyceride,Inositol Phosphoglycerides,Inositol Phospholipid,Phosphoinositide,Phosphoinositides,PtdIns,Inositide Phospholipids,Inositol Phospholipids,Phosphatidyl Inositol,Phosphatidylinositol,Inositol, Phosphatidyl,Phosphoglyceride, Inositol,Phosphoglycerides, Inositol,Phospholipid, Inositide,Phospholipid, Inositol,Phospholipids, Inositide,Phospholipids, Inositol |
|
| D010766 |
Phosphorylation |
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. |
Phosphorylations |
|
| D011485 |
Protein Binding |
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. |
Plasma Protein Binding Capacity,Binding, Protein |
|
| D002478 |
Cells, Cultured |
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others. |
Cultured Cells,Cell, Cultured,Cultured Cell |
|
| D003600 |
Cytosol |
Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components. |
Cytosols |
|
| D000804 |
Angiotensin II |
An octapeptide that is a potent but labile vasoconstrictor. It is produced from angiotensin I after the removal of two amino acids at the C-terminal by ANGIOTENSIN CONVERTING ENZYME. The amino acid in position 5 varies in different species. To block VASOCONSTRICTION and HYPERTENSION effect of angiotensin II, patients are often treated with ACE INHIBITORS or with ANGIOTENSIN II TYPE 1 RECEPTOR BLOCKERS. |
Angiotensin II, Ile(5)-,Angiotensin II, Val(5)-,5-L-Isoleucine Angiotensin II,ANG-(1-8)Octapeptide,Angiotensin II, Isoleucine(5)-,Angiotensin II, Valine(5)-,Angiotensin-(1-8) Octapeptide,Isoleucine(5)-Angiotensin,Isoleucyl(5)-Angiotensin II,Valyl(5)-Angiotensin II,5 L Isoleucine Angiotensin II,Angiotensin II, 5-L-Isoleucine |
|
| D000818 |
Animals |
Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. |
Animal,Metazoa,Animalia |
|