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Creator | Title | Description | Subject | Date |
1 |
 | Poulter, Charles Dale; Jiang, Yunfeng | BTS1 encodes a geranylgeranyl diphosphate synthase in Saccharomyces cerevisiae | Protein prenylation utilizes different types of isoprenoids groups, namely farnesyl and geranylgeranyl, to modify proteins. These lipophilic moieties attach to carboxyl-terminal cysteine residues to promote the association of soluble proteins to membranes. Most prenylated proteins are geranylgeranyl... | Amino Acid Sequence; Cloning, Molecular; Gene Expression | 1995-09-15 |
2 |
 | Baehr, Wolfgang | Molecular characterization of human and mouse photoreceptor guanylate cyclase-activating protein (GCAP) and chromosomal localization of the human gene | Guanylate cyclase-activating protein (GCAP) is a novel Ca(2+)-binding protein that stimulates synthesis of cGMP in photoreceptors. Molecular cloning of human and mouse GCAP cDNA revealed that the known mammalian GCAPs are more than 90% similar, consist of 201-205 amino acids, and contain three ident... | Amino Acid Sequence; Base Sequence; Cloning, Molecular | 1994 |
3 |
 | Baehr, Wolfgang | Cloning and sequence analysis of the major outer membrane protein genes of two Chlamydia psittaci strains | We cloned and sequenced the gene encoding the major outer membrane protein (MOMP) of two Chlamydia psittaci strains, guinea pig inclusion conjunctivitis (GPIC) strain 1, and meningopneumonitis (Mn) strain Cal-10. Intraspecies alignment of the two C. psittaci MOMP genes revealed 80.6% similarity, and... | Base Sequence; Cloning, Molecular; Amino Acid Sequence | 1989 |
4 |
 | Capecchi, Mario R. | Isolation and characterization of Caenorhabditis elegans DNA sequences homologous to the v-abl oncogene. | DNA sequences homologous to the v-abl oncogene were isolated from a Caenorhabditis elegans genomic library by their ability to hybridize with a v-src probe. The DNA sequence of 2465 nucleotides of one clone was determined. This region corresponds to the 5' protein kinase domain of v-abl plus approxi... | Amino Acid Sequence; Animals; Base Sequence; Gene Expression Regulation; Transcription, Genetic | 1986-04 |
5 |
 | Baehr, Wolfgang | Evaluation of the 17 kda prenyl binding protein as a regulatory protein for phototransduction in retinal photoreceptors | The mammalian rod photoreceptor phosphodiesterase (PDE6) holoenzyme is isolated in both a membrane-associated and a soluble form. Membrane binding is a consequence of prenylation of PDE6 catalytic subunits, whereas soluble PDE6 is purified with a 17-kDa prenyl-binding protein (PDEdelta) tightly boun... | Amino Acid Sequence; Immunohistochemistry; Phosphoric Diester Hydrolases | 2005 |
6 |
 | Gesteland, Raymond F.; Atkins, John F.; Ingram, Jennifer A.; Kelly, Paul J.; Grentzmann, Guido | Dual-luciferase reporter system for studying recoding signals | A new reporter system has been developed for measuring translation coupling efficiency of recoding mechanisms such as frameshifting or readthrough. A recoding test sequence is cloned in between the renilla and firefly luciferase reporter genes and the two luciferase activities are subsequently measu... | Amino Acid Sequence; Genes, Reporter; HIV; Antizyme; Translation | 1998 |
7 |
 | Poulter, Charles Dale | Enzymes encoded by the farnesyl diphosphate synthase gene family in the big sagebrush Artemisia tridentata ssp. spiciformis | Farnesyl diphosphate synthase catalyzes the sequential head-to-tail condensation of two molecules of isopentenyl diphosphate with dimethylallyl diphosphate. In plants the presence of farnesyl diphosphate synthase isozymes offers the possibility of differential regulation. Three full-length cDNAs enc... | Amino Acid Sequence; Base Sequence; Molecular Sequence Data | 2003-08-22 |
8 |
 | Baehr, Wolfgang; Rao, Narayanam V. | Molecular characterization of a third member of the guanylyl cyclase-activating protein subfamily | The mammalian retina contains at least two guanylyl cyclases (GC1 and GC2) and two guanylyl cyclase-activating proteins (GCAP1 and GCAP2). Here we present evidence of the presence of a new photoreceptor-specific GCAP, termed GCAP3, which is closely related to GCAP1. The sequence similarity of GCAP3 ... | Amino Acid Sequence; Cloning, Molecular; Gene Expression Regulation | 1999 |
9 |
 | Baehr, Wolfgang | Cloning and molecular characterization of cGMP-gated ion channels from rod and cone photoreceptors of striped bass ( M. saxatilis ) retina | Vertebrate photoreceptors respond to light with changes in membrane conductance that reflect the activity of cyclic-nucleotide gated channels (CNG channels). The functional features of these channels differ in rods and cones; to understand the basis of these differences we cloned CNG channels from t... | Amino Acid Sequence; Computational Biology; Reverse Transcriptase Polymerase Chain Reaction | 2006 |
10 |
 | Baehr, Wolfgang; Zhang, Kang | Elovl4 mRNA distribution in the developing mouse retina and phylogenetic conservation of Elovl4 genes | PURPOSE: Stargardt-like macular dystrophy (STGD3) is an autosomal dominant form of early onset macular degeneration. The disease causing gene ELOVL4 encodes a protein that belongs to a family of proteins functioning in elongation of long chain fatty acids. The purpose of this study is to characteriz... | Amino Acid Sequence; Cloning, Molecular; Molecular Sequence Data | 2003 |
11 |
 | Baehr, Wolfgang; Zhang, Kang | Characterization of human GRK7 as a potential cone opsin kinase | PURPOSE: Homozygous inactivation of the mouse gene for GRK1 (G protein-coupled receptor kinase 1, or rhodopsin kinase) causes severe defects in the recovery of cone phototransduction. However, electroretinographic (ERG) analyses of human oguchi patients with defective GRK1 alleles showed normal or s... | Amino Acid Sequence; Chromosomes, Human, Pair 3; Fluorescent Antibody Technique, Indirect | 2001 |
12 |
 | Poulter, Charles Dale | Isopentenyl diphosphate:dimethylallyl diphosphate isomerase. An improved purification of the enzyme and isolation of the gene from Saccharomyces cerevisiae. | Isopentenyl diphosphate:dimethylallyl diphosphate isomerase (IPP isomerase) is an enzyme in the isoprenoid biosynthetic pathway which catalyzes the interconversion of the primary five-carbon homoallylic and allylic diphosphate building blocks. We report a substantially improved procedure for purific... | Amino Acid Sequence; Base Sequence; Chromatography, Gel; Chromatography, Ion Exchange | 1989-11-15 |