المؤلفون: Liviana Cozzi, Monica Mosca, Robert Schwarcz, Luca Benatti, Carmela Speciale, Etsuo Okuno, Jerome Breton

المصدر: FEBS Letters. 353:21-24

مصطلحات موضوعية: DNA, Complementary, Molecular Sequence Data, Biophysics, Lyases, Biology, Molecular cloning, Kidney, Biochemistry, Cell Line, chemistry.chemical_compound, Kynurenic acid, Structural Biology, Complementary DNA, Genetics, Animals, Coding region, Amino Acid Sequence, Cloning, Molecular, Molecular Biology, Transaminases, chemistry.chemical_classification, Messenger RNA, Kynurenine aminotransferase, Base Sequence, Excitatory amino acid, Cell Biology, Transfection, Molecular biology, Neuroprotection, Rats, Amino acid, Enzyme, chemistry, Glutamine transaminase K, Cysteine conjugate β-1yase

الوصف: The enzyme kynurenine aminotransferase (KAT) catalyses the conversion of l-kynurenine to kynurenic acid. A combination of polymerase chain reaction techniques and hybridization screening was used to isolate a cDNA clone encompassing the entire coding region of KAT from rat kidney. Identification of the cDNA as coding for KAT was based both on the comparison of amino acid sequences obtained from purified rat KAT and on the expression of KAT activity in COS-1 cells transfected with the cDNA. RNA blot analysis indicated that KAT mRNA is widely expressed in rat tissues. Cultured cells transfected with the cDNA for KAT also showed glutamine transaminase K activity. Based mainly on sequence data, these results demonstrate that rat kidney KAT is identical with glutamine transaminase K.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b18e1fec15a530bce6d5727f6cb3db39Test
https://doi.org/10.1016/0014-5793Test(94)01003-x

المؤلفون: Kay Hofmann, Maria Düker, Wilhelm Stoffel

المصدر: FEBS Letters. 333:119-122

مصطلحات موضوعية: Transcription, Genetic, Molecular Sequence Data, Restriction Mapping, Biophysics, Mitochondria, Liver, β-Oxidation, Molecular cloning, Enoyl CoA isomerase, Biology, Dodecenoyl-CoA Isomerase, Biochemistry, Primer extension, Mice, Gene organization, Structural Biology, cDNA and derived amino acid sequence, Complementary DNA, Genetics, Animals, Coding region, Amino Acid Sequence, Cloning, Molecular, Isomerases, Molecular Biology, Gene, Base Sequence, Sequence Homology, Amino Acid, Nucleic acid sequence, DNA, Cell Biology, Carbon-Carbon Double Bond Isomerases, Molecular biology, Introns, Rats, Open reading frame, 3,2-trans-Enoyl-CoA isomerase

الوصف: 3,2-trans-enoyl-CoA isomerase (mECI, E.C. 5.3.3.8) is the key enzyme of mitochondrial β-oxidation of unsaturated fatty acids. A mouse cDNA clone spanning the entire coding region of mECI was isolated and sequenced. Subsequently, two overlapping genomic clones containing the complete mECI gene were isolated and characterized. The mouse mECI cDNA comprises an open reading frame of 867 bp, encoding a protein of 32 kDa. The mECI gene, spanning about 15 kb, consists of seven exons. Multiple transcription starts were determined by primer extension experiments. Knowledge of the gene organization and availability of genomic clones for mouse mECI will facilitate the study of unsaturated fatty acid metabolism in normal and pathological states.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d97b4ef0693ee8887a25756ca9abe692Test
https://doi.org/10.1016/0014-5793Test(93)80387-a

المؤلفون: Tatjana Simonic, Severino Ronchi, Rosanna Asselta, Fabrizio Ceciliani, Bice Strumbo, Stefano Duga

المصدر: FEBS letters. 469(1)

مصطلحات موضوعية: Untranslated region, Models, Molecular, Prions, Molecular Sequence Data, Biophysics, Molecular cloning, Biology, Biochemistry, Exon, Reptile prion protein, Gene organization, Structural Biology, Complementary DNA, Genetics, Coding region, Animals, Amino Acid Sequence, RNA, Messenger, Prion protein, Cloning, Molecular, Molecular Biology, Conserved Sequence, Cdna cloning, Base Sequence, EF-hand Ca2+ binding motif, Calcium-Binding Proteins, Intron, Cell Biology, Turtles, cDNA cloning, Sequence Alignment

الوصف: Cloning of the cDNA coding for the 270-residue turtle prion protein is reported. It represents the most remote example thus far described. The entire coding region is comprised in a single exon, while a large intron interrupts the 5′ UTR. The common structural features of the known prion proteins are all conserved in turtle PrP, whose identity degree to mammalian and avian proteins is about 40 and 58%, respectively. The most intriguing feature, unique to the turtle prion, is the presence of an EF-hand Ca2+ binding motif in the C-terminal half of the protein.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd35866cbab20e98cac94a1a4baf5247Test
https://pubmed.ncbi.nlm.nih.gov/10708751Test

المؤلفون: Ikuro Ito, Shigeo Igarashi, Yoshihisa Hasegawa, Kaoru Miyamoto, Manabu Nakamura, Yuzuru Eto, Hiromitsu Shinozaki, Yoshito Ibuki, Takashi Minegishi, Kazuto Nakamura

المصدر: FEBS letters. 312(1)

مصطلحات موضوعية: Gonadotropins, Equine, mRNA, Activin Receptors, Molecular Sequence Data, Biophysics, Receptors, Cell Surface, Biology, Molecular cloning, Protein Serine-Threonine Kinases, Biochemistry, Chorionic Gonadotropin, Structural Biology, Complementary DNA, Genetics, Coding region, Animals, Humans, Northern blot, Amino Acid Sequence, RNA, Messenger, Cloning, Molecular, Rats, Wistar, Molecular Biology, Peptide sequence, Base Sequence, Sequence Homology, Amino Acid, cDNA library, Ovary, Cell Biology, Activin receptor, DNA, Molecular biology, Rats, RNA, Female, Poly A, ACVR2B

الوصف: A full-length cDNA for a rat type II activin receptor was cloned by hybridization from a rat ovary cDNA library. The deduced amino acid sequence (513 residues) containing a single membrane-spanning domain and an intracellular kinase domain with predicted serine/threonine specificity. The amino acid sequence is 99.8% and 99.4% identical in the coding region with the previously cloned mouse and human type II activin receptor, and only 66.7% identical in the coding region with the previously cloned rat type IIB activin receptor. We examined the effect of PMSG-hCG on the mRNA level of type II activin receptor in immature rat ovaries. Northern blot analysis of ovarian RNA revealed two mRNAs (3.0 kb and 6.0 kb).

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b4a787e824f3b1cc7d52a349ce9f5bcfTest
https://pubmed.ncbi.nlm.nih.gov/1385212Test

المؤلفون: Ikuko Hara-Nishimura, Tetsunori Matsumoto, Hitoshi Mori, Reiko Hara, Mikio Nishimura, T. Hara

المصدر: FEBS letters. 271(1-2)

مصطلحات موضوعية: Rhodopsin, genetic structures, Retinal binding, Molecular Sequence Data, Biophysics, Biology, Molecular cloning, Retinochrome, Biochemistry, Retina, Structural Biology, Complementary DNA, Sequence Homology, Nucleic Acid, Genetics, Coding region, Animals, Amino Acid Sequence, Cloning, Molecular, Isomerases, Molecular Biology, Binding Sites, Base Sequence, Todarodespacificus, Nucleic acid sequence, Decapodiformes, Photoisomerase, Cell Biology, Retinal isomerase, DNA, Myeloid body, Retinal protein, Molecular biology, Visual cell, Solubility, biology.protein, Cattle, Retinal Pigments

الوصف: The Rhodopsin-retinochrome system is essential for the visual photoreception of molluscs. cDNA coding for retinochrome of the squid (Todarodespacificus) was cloned and the nucleotide sequence has been determined. The sequence (2.1 kb) covers the whole coding region of 903 bp. The deduced primary sequence suggests that retinochrome contains seven transmembrane spanning domains. The homology with bovine rhodopsin and the possible retinal binding site are also discussed.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e378ebfc21bb781ffab0ffb93037551Test
https://pubmed.ncbi.nlm.nih.gov/2226795Test

المؤلفون: Shmuel Rozenblatt, Rafael Arango, Nathan Sharon

المصدر: FEBS letters. 264(1)

مصطلحات موضوعية: Sequence analysis, Molecular Sequence Data, Restriction Mapping, Biophysics, Biology, Molecular cloning, Biochemistry, Structural Biology, Complementary DNA, Lectins, Sequence Homology, Nucleic Acid, Genetics, Coding region, Amino Acid Sequence, RNA, Messenger, Cloning, Molecular, Legume lectin, Molecular Biology, Peptide sequence, Erythrina, chemistry.chemical_classification, Plants, Medicinal, Base Sequence, cDNA library, Cell Biology, DNA, Molecular biology, Stop codon, Amino acid, chemistry, RNA, Plant Lectins, Poly A

الوصف: Examination of the hemagglutinating activity of extracts from seeds of Erythrina corallodendron at various maturation stages revealed that the level of lectin increases markedly past mid-maturation. Seeds at this stage of maturation served as a source of mRNA for the construction of an expression cDNA library in the vector λ Zap, which generates fusion proteins with an N-terminal portion of β-galactosidase. The library was screened with rabbit polyclonal anti-ECorL antiserum. Four immunopositive clones were isolated. Western blot analysis of cell extracts from one of the clones (pIEcL-B) showed a 36 kDa protein that reacted with the antiserum, as well as with a mouse monoclonal antibody raised against the lectin. DNA sequence analysis by the chain termination method revealed that clone pIEcl-C has an insert of 1017 bp with the entire coding sequence of ECorL, beginning with an initiation codon ATG at position 26 and ending with stop codon TAA at position 868. This fragment encodes a polypeptide of 281 amino acids consisting of a signal leader sequence of 25 amino acids and a mature protein of 256 amino acids. The deduced amino acid sequence from this fragment is identical to the sequence of the first 244 amino acids of ECorL, as determined at the protein level, except at 7 positions.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7befccac18c8874cdacd095fb9257b9bTest
https://pubmed.ncbi.nlm.nih.gov/1692539Test

المؤلفون: J.D. Falk, J.T. Triantafyllos, Wolfgang Baehr, James F. McGinnis, Kuyas Bugra

المصدر: FEBS Letters. 238:253-256

مصطلحات موضوعية: Opsin, Transcription, Genetic, genetic structures, Molecular Sequence Data, DNA, Recombinant, Biophysics, Molecular cloning, Biology, Biochemistry, Retina, Mice, Gene cloning, Structural Biology, Sequence Homology, Nucleic Acid, Complementary DNA, Peptide sequence, Genetics, Animals, Coding region, Photoreceptor Cells, Amino Acid Sequence, Eye Proteins, Molecular Biology, Gene, Base Sequence, Rod Opsins, Intron, RNA, DNA, DNA Restriction Enzymes, Exons, Cell Biology, Molecular biology, Introns, eye diseases, Mice, Inbred C57BL, (Mouse retina), Visual pigment, cDNA cloning, sense organs, Retinal Pigments

الوصف: We have identified three overlapping 5′-truncated mouse opsin cDNA clones by immunologically screening a λgt11 retina expression library. Using one of the cDNA clones as a probe, we isolated a 5 kb genomic fragment that encompassed the complete coding sequence for mouse opsin. The coding region for opsin was interrupted by four introns positioned precisely as those previously described for other mammalian opsins. In contrast to the single major opsin mRNA in the bovine and human retina, Northern analysis of mouse retina RNA demonstrated the presence of at least five distinct species of polyadenylated opsin mRNAs. Their sizes ranged from 1.7 kb to 5.1 kb.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::313ed4d919546e0f03d697362a5e5cf5Test
https://doi.org/10.1016/0014-5793Test(88)80490-3

المؤلفون: Noriko Imagawa, Kazuhiko Maekawa, Masaaki Nagamatsu, Shigenori Harada

المصدر: FEBS Letters. (2):200-206

مصطلحات موضوعية: Adult, Gene isoform, DNA, Complementary, Molecular Sequence Data, Phosphatase, education, Biophysics, Protein tyrosine phosphatase, Biology, Molecular cloning, Human basophil, Polymerase Chain Reaction, Biochemistry, Fetus, PTP-BAS, Pregnancy, Structural Biology, Complementary DNA, Genetics, Humans, Coding region, Amino Acid Sequence, Cloning, Molecular, Repeated sequence, GLGF repeat, Molecular Biology, Conserved Sequence, Protein-tyrosine phosphatase, DNA Primers, Repetitive Sequences, Nucleic Acid, Sequence Deletion, Protein Tyrosine Phosphatase, Non-Receptor Type 1, chemistry.chemical_classification, Base Sequence, Sequence Homology, Amino Acid, Membrane-binding domain, Cell Biology, Blotting, Northern, Molecular biology, Recombinant Proteins, Basophils, Amino acid, Isoenzymes, chemistry, Organ Specificity, Female, Protein Tyrosine Phosphatases

الوصف: A full-length cDNA encoding a novel cytosolic protein-tyrosine phosphatase (PTP), PTP-BAS, was cloned from human basophils. Due to in-frame deletions in the coding region, PTP-BAS exists in three isoforms: 7,455 bp (2,485 aa) for type 1, 7,398 bp (2,466 aa) for type 2 and 6,882 bp (2,294 aa) for type 3. All three isoforms contain a single PTP catalytic domain at the carboxyl termini as well as two distinct structural sequences. Amino terminal sequences of 300 amino acids are homologous to membrane-binding domains of eytoskeleton-associated proteins. Three 90 amino acid internal repetitive sequences are homologous to the GLGF repeats found in guanylate kinase proteins. PTP-BAS was expressed in various human tissues, especially highly in the kidney and lung. Interestingly, the BAS mRNA level in the fetal brain was remarkably high.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05c0145b01c998461ccb33cf2bdefb6dTest

المؤلفون: Marketta Hänninen, Kati Elima, Merja Perälä, Johanna Hästbacka, Eero Vuorio

المصدر: FEBS Letters. (1-2):177-180

مصطلحات موضوعية: mRNA, Molecular Sequence Data, Restriction Mapping, Biophysics, Human chromosome 1, Molecular cloning, Biology, Biochemistry, 03 medical and health sciences, Exon, Mice, 0302 clinical medicine, Restriction map, Structural Biology, Complementary DNA, Genetics, Coding region, Animals, Humans, Amino Acid Sequence, Cloning, Molecular, 10. No inequality, Molecular Biology, Peptide sequence, Gene, 030304 developmental biology, 0303 health sciences, Base Sequence, Nucleic acid sequence, Chromosome Mapping, Cell Biology, DNA, Molecular biology, Polymerase chain reaction, Cartilage, Chromosomes, Human, Pair 1, Collagen, 030217 neurology & neurosurgery

الوصف: Type IX collagen, a heterotrimer of alpha 1(IX), alpha 2(IX) and alpha 3(IX) chains, is a cartilage-specific fibril-associated collagen. In the process of characterizing genomic clones for the mouse alpha 2(IX) collagen gene four pairs of oligonucleotide primers designed for amplification of murine exon sequences were also utilized to construct cDNA clones for human alpha 2(IX) collagen spanning > 90% of the coding region. The amino acid and nucleotide sequence identities between human and chick are 78% and 71%, respectively. Localization of the COL9A2 gene to human chromosome 1 was subsequently performed using a panel of DNAs from human/rodent somatic cell hybrids.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78223257310fc8c78ae47b693aa95d9cTest

المؤلفون: Michael Loos, Franz Petry, Kenneth B.M. Reid

المصدر: FEBS Letters. (1):89-93

مصطلحات موضوعية: mRNA, Molecular Sequence Data, Biophysics, Protein Sorting Signals, Molecular cloning, Biology, Biochemistry, Mice, Structural Biology, Sequence Homology, Nucleic Acid, Complementary DNA, Genetics, Animals, Humans, Coding region, Genomic library, RNA, Messenger, Northern blot, Cloning, Molecular, Promoter Regions, Genetic, Molecular Biology, Gene, Mice, Inbred BALB C, Messenger RNA, Complement C1q, Nucleic Acid Hybridization, RNA, DNA, RNA Probes, Cell Biology, Blotting, Northern, Molecular biology, Clq, Nucleotide sequence, Cloning

الوصف: cDNA clones coding for the B-chain of murine Clq were isolated from a mouse macrophage library. The characterized clones include the total coding region plus a leader sequence. High homology was found with human Clq B-chain in the coding region (81%). Northern blot analysis of total RNA from different tissues of Balb/c mice showed one band of approximately 1.2 kb. The highest signal was found in RNA preparations of thioglycolate-activated peritoneal macrophages. The probe also hybridized with mRNA from spleen, thymus and heart. Extremely weak signals were found in liver, kidney, lung and intestine tissues.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::845fc212e15ecd623993914095100222Test