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Volumn 13, Issue 10, 2001, Pages 735-741
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The γ subunit of the rod photoreceptor cGMP phosphodiesterase can modulate the proteolysis of two cGMP binding cGMP-specific phosphodiesterases (PDE6 and PDE5) by caspase-3
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Author keywords
Caspases; cGMP; Lung; PDE ; Phosphodiesterase; Testes
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Indexed keywords
AMINO ACID;
CASPASE 3;
CYCLIC GMP;
CYCLIC GMP PHOSPHODIESTERASE;
ISOENZYME;
PHOSPHODIESTERASE;
ALPHA CHAIN;
ARTICLE;
BETA CHAIN;
CONTROLLED STUDY;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME BINDING;
ENZYME PURIFICATION;
ENZYME SPECIFICITY;
ENZYME STRUCTURE;
ENZYME SUBSTRATE;
ENZYME SUBUNIT;
HYDROLYSIS;
INCUBATION TIME;
MOLECULAR WEIGHT;
MOUSE;
NONHUMAN;
NUCLEOTIDE SEQUENCE;
PHOTORECEPTOR;
PRIORITY JOURNAL;
PROTEIN DEGRADATION;
PROTEIN PROTEIN INTERACTION;
RETINA ROD;
3',5'-CYCLIC-GMP PHOSPHODIESTERASE;
ANIMALS;
BASE SEQUENCE;
CASPASE 3;
CASPASES;
CYCLIC GMP;
DRUG INTERACTIONS;
LUNG;
MALE;
MICE;
MOLECULAR SEQUENCE DATA;
PHOSPHORIC DIESTER HYDROLASES;
RNA;
ROD OUTER SEGMENTS;
SEQUENCE HOMOLOGY, NUCLEIC ACID;
TESTIS;
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EID: 0034877538
PISSN: 08986568
EISSN: None
Source Type: Journal
DOI: 10.1016/S0898-6568(01)00193-0 Document Type: Article |
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Times cited : (14)
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References (19)
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