| D006801 |
Humans |
Members of the species Homo sapiens. |
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man |
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| D000072340 |
NIMA-Interacting Peptidylprolyl Isomerase |
A highly-conserved peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated SERINE- or THREONINE-PROLINE (pSer/Thr-Pro) motifs and causes conformational changes in certain proteins associated with the CELL CYCLE. It displays a preference for an acidic residue N-terminal to the isomerized proline bond and regulates MITOSIS, possibly by attenuating the mitosis-promoting activity of NIMA-RELATED KINASE 1. |
PIN1 Protein,Peptidyl-Prolyl Cis-Trans Isomerase Pin1,Pin1 Peptidylprolyl Isomerase,Isomerase, NIMA-Interacting Peptidylprolyl,Isomerase, Pin1 Peptidylprolyl,NIMA Interacting Peptidylprolyl Isomerase,Peptidyl Prolyl Cis Trans Isomerase Pin1,Peptidylprolyl Isomerase, NIMA-Interacting,Peptidylprolyl Isomerase, Pin1 |
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| D017360 |
Arabidopsis |
A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development. |
Arabidopsis thaliana,Cress, Mouse-ear,A. thaliana,A. thalianas,Arabidopses,Arabidopsis thalianas,Cress, Mouse ear,Cresses, Mouse-ear,Mouse-ear Cress,Mouse-ear Cresses,thaliana, A.,thaliana, Arabidopsis,thalianas, A. |
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| D017433 |
Protein Structure, Secondary |
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to ALPHA-HELICES; BETA-STRANDS (which align to form BETA-SHEETS), or other types of coils. This is the first folding level of protein conformation. |
Secondary Protein Structure,Protein Structures, Secondary,Secondary Protein Structures,Structure, Secondary Protein,Structures, Secondary Protein |
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| D019696 |
Peptidylprolyl Isomerase |
An enzyme that catalyzes the isomerization of proline residues within proteins. EC 5.2.1.8. |
PPIase,Peptidyl-Prolyl cis-trans-Isomerase,Prolyl Isomerase,Proline Isomerase,Proline Rotamase,Isomerase, Peptidylprolyl,Isomerase, Proline,Isomerase, Prolyl,Peptidyl Prolyl cis trans Isomerase,Rotamase, Proline,cis-trans-Isomerase, Peptidyl-Prolyl |
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| D019906 |
Nuclear Magnetic Resonance, Biomolecular |
NMR spectroscopy on small- to medium-size biological macromolecules. This is often used for structural investigation of proteins and nucleic acids, and often involves more than one isotope. |
Biomolecular Nuclear Magnetic Resonance,Heteronuclear Nuclear Magnetic Resonance,NMR Spectroscopy, Protein,NMR, Biomolecular,NMR, Heteronuclear,NMR, Multinuclear,Nuclear Magnetic Resonance, Heteronuclear,Protein NMR Spectroscopy,Biomolecular NMR,Heteronuclear NMR,Multinuclear NMR,NMR Spectroscopies, Protein,Protein NMR Spectroscopies,Spectroscopies, Protein NMR,Spectroscopy, Protein NMR |
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| D029681 |
Arabidopsis Proteins |
Proteins that originate from plants species belonging to the genus ARABIDOPSIS. The most intensely studied species of Arabidopsis, Arabidopsis thaliana, is commonly used in laboratory experiments. |
Arabidopsis thaliana Proteins,Thale Cress Proteins,Proteins, Arabidopsis thaliana,thaliana Proteins, Arabidopsis |
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