Bibliografías temáticas / Molecular cloning

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Literatura académica sobre el tema "Molecular cloning"

Autor: Grafiati

Publicado: 4 de junio de 2021

Última modificación: 9 de junio de 2025

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Artículos de revistas sobre el tema "Molecular cloning"

Xu, Libing, Yuhong Chen, Qiuhua Li, Tianliang He, and Xinhua Chen. "Molecular cloning." Fish & Shellfish Immunology 98 (March 2020): 981–87. http://dx.doi.org/10.1016/j.fsi.2019.10.064.

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Kwak, Inseok. "Molecular Cloning and Characterization of Bovine CYP26A1 Promoter." Journal of Life Science 26, no. 1 (January 30, 2016): 42–49. http://dx.doi.org/10.5352/jls.2016.26.1.42.

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Tu, Kevin, Angela Sun, and Daniel Levin. "A Sweet Method of Modeling Restriction Endonuclease-Based Molecular Cloning." American Biology Teacher 85, no. 1 (January 1, 2023): 52–54. http://dx.doi.org/10.1525/abt.2023.85.1.52.

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Molecular cloning is an invaluable research tool in modern molecular biology. However, it is often difficult for students to grasp conceptually without visual aids and even more difficult to understand how to successfully set up a cloning experiment. Here, we describe a flipped classroom activity that simulates cloning using donuts as models of plasmids. Students noted in semistructured interviews that the interactive nature of this activity made it an engaging introduction to molecular cloning.

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Morimura, Naoko, Yoko Tezuka, Naoko Watanabe, Masafumi Yasuda, Seiji Miyatani, Nobumichi Hozumi, and Ken-ichi Tezuka. "Molecular Cloning of POEM." Journal of Biological Chemistry 276, no. 45 (September 6, 2001): 42172–81. http://dx.doi.org/10.1074/jbc.m103216200.

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Ashwini, Malla, Shanmugaraj Bala Murugan, Srinivasan Balamurugan, and Ramalingam Sathishkumar. "Advances in molecular cloning." Molecular Biology 50, no. 1 (January 2016): 1–6. http://dx.doi.org/10.1134/s0026893316010131.

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Taylor, D. W., J. S. Cordingley, D. W. Dunne, K. S. Johnson, W. J. Haddow, C. E. Hormaeche, V. Nene, and A. E. Butterworth. "Molecular cloning of schistosome genes." Parasitology 92, S1 (January 1986): S73—S81. http://dx.doi.org/10.1017/s003118200008570x.

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As part of an integrated programme investigating human schistosomiasis, work which involves epidemiological surveys and detailed immunological studies as well as biochemical investigations, we have, over the last three years, been cloning schistosome genes in a variety of plasmid and lambda vector systems. In this lecture we present a review of some selected aspects of work primarily aimed at production of experimental vaccines against the disease but which, on a broader front, is also concerned with developmental regulation of gene expression around the parasite's life-cycle. Specifically, we are interested in cloning three groups of genes. First, those encoding surface antigens; second, those associated with sexual maturity and egg production; and third, antigens which may provide a basis for a specific immunodiagnostic test.

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Yamamoto, Kosuke, Suguru Oguri, Susumu Chiba, and Yoshie S. Momonoki. "Molecular cloning ofacetylcholinesterasegene fromSalicornia europaeaL." Plant Signaling & Behavior 4, no. 5 (May 2009): 361–66. http://dx.doi.org/10.4161/psb.4.5.8360.

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Iwaki, Daisuke, Shun-ichiro Kawabata, Yoshiki Miura, Atsuko Kato, Peter B. Armstrong, James P. Quigley, Kare Lehmann Nielsen, Klavs Dolmer, Lars Sottrup-Jensen, and Sadaaki Iwanaga. "Molecular Cloning of Limulusalpha2-Macroglobulin." European Journal of Biochemistry 242, no. 3 (December 15, 1996): 822–31. http://dx.doi.org/10.1111/j.1432-1033.1996.0822r.x.

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Malcolm, S. "Guide to Molecular Cloning Techniques." Journal of Medical Genetics 27, no. 1 (January 1, 1990): 70. http://dx.doi.org/10.1136/jmg.27.1.70.

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Reuter, Harald, and Hartmut Porzig. "Muscle disease and molecular cloning." Nature 336, no. 6195 (November 1988): 113. http://dx.doi.org/10.1038/336113b0.

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Tesis sobre el tema "Molecular cloning"

Bates, Nancy Carol. "Characterization of cbg : a cloned gene encoding an extracellular [beta]-glucosidase from Cellulomonas fimi." Thesis, University of British Columbia, 1987. http://hdl.handle.net/2429/26163.

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A group of Escherichia coli clones harbouring recombinant pBR322 plasmid, containing Cellulomonas fimi DNA inserts, that reacted with antiserum to C.fimi culture supernatant, was screened for their ability to hydrolyze carboxymethyl cellulose (CMC) and 4-methylumbeliferyll-β-D-cellobioside (MUC). A clone, pEC62, hydrolyzed MUC but did not hydrolyze CMC. The recombinant enzyme encoded by pEC62 was shown to be a β-glucosidase (cellobiase). C.fimii itself was shown to encode an extracellular β-glucosidase in C.fimi. This is the first report of an extracellular β-glucosidase from a bacterium. Deletion analysis localized the cloned gene (cbg)to the tet promoter proximal region of the 7.0 kilobase insert of pEC62. Further analysis and sequence data showed a highly active derivative of pEC62 contained a translational gene fusion between lacZ of pUC13 and cbg. From this data, a location for the cbg start site was proposed. Science, Faculty of Microbiology and Immunology, Department of Graduate

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Seto, Nina Oi Ling. "The copper-zinc superoxide dismutase gene from Drosophila melanogaster : attempts to clone the gene using two mixed sequence oligonucleotide probes." Thesis, University of British Columbia, 1987. http://hdl.handle.net/2429/26534.

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Superoxide dismutase is an enzyme which scavenges superoxide radicals and is thought to be a longevity determinant, as there exists a positive correlation between superoxide dismutase concentration and maximum life span potential. The cytosolic CuZn superoxide dismutase in D. melanogaster has been purified and sequenced, but the gene has not been cloned. However, when it is available the CuZn SOD gene may be reintroduced into the Drosophila genome via the P-element transformation system so its effects on the life span potential of Drosophila may be studied. This study describes attempts to clone the CuZn SOD gene from D. melanogaster using two mixed sequence oligonucleotide probes. The SI probe corresponds to amino acids 43-48 of the protein sequence and contains 128 different oligonucleotide sequences representing all possible codon combinations predicted from the amino acid sequence. The GT3 probe is targeted to amino acids 90-95 of the protein. In this probe, deoxyguanosine was placed in positions where all four nucleotides may occur to decrease probe heterogeneity. The probes were used to screen D. melanogaster Canton-S and Oregon-R genomic lambda libraries. Three positive clones isolated from the Canton-S library had identical nucleotide sequence in the GT3 probe binding region, and sequencing of the probe binding site revealed that one member of the GT3 probe had formed a 15 bp duplex with the phage DNA. Screening of the Oregon-R library produced four clones which hybridized with both GT3 and S1 probes. When these phage DNA were hybridized to polytene chromosomes by in situ hybridization, none mapped to 68AB on the third chromosome, the location of the CuZn SOD gene. These results suggest that modification of the classical strategy used in this study is necessary, and implications on probe design are discussed. Medicine, Faculty of Biochemistry and Molecular Biology, Department of Graduate

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Woodruff, Wendy Anne. "Cloning and characterization of the oprF gene for protein F from Pseudomonas aeruginosa." Thesis, University of British Columbia, 1988. http://hdl.handle.net/2429/29218.

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The oprF gene encoding porin protein F from Pseudomonas aeruginosa was cloned onto a cosmid vector into Escherichia coli. Protein F was expressed in large amounts in E. coli and retained its heat- and reduction-modifiable and immunological characteristics. The cloned oprF gene product was purified from E. coli and characterized with respect to pore-forming ability in black lipid bilayers. Small channels, with an average single channel conductance of approximately 0.4 nS, were observed. A similar small channel size was observed for native protein F. The oprF sequences were used as a DNA-DNA hybridization probe with chromosomal DNA from the 17 IATS (International Antigen Typing Scheme) strains of P. aeruginosa, 52 clinical isolates and the non-aeruginosa Pseudomonads. Conservation of oprF sequences was observed among all the P. aeruginosa strains and to a lesser extent among the non-aeruginosa strains of the P. fluorescens rRNA homology group. Insertion mutations in the oprF gene were created in vivo by Tn1mutagenesis of the cloned gene in E. coli and in vitro by insertion of the streptomycin-encoding Ω fragment into the cloned gene, followed by transfer of the mutated protein F gene back into P. aeruginosa and homologous recombination with the chromosome. The oprF mutants were characterized by gel electrophoresis and immunoblotting, and it was shown that the mutants had lost protein F. The P. aeruginosa oprF mutants were characterized with respect to growth rates, antibiotic permeability and cell surface hydrophobicity. The results of these studies indicated that major alterations in the cell surface had occurred and that the cells were unable to grow in a non-defined liquid medium without added electrolytes. Marginal differences were observed in MICs (minimum inhibitory concentrations) of hydrophilic antibiotics for the oprF mutants compared with their protein F-sufficient parents. The putative roles of protein F in antibiotic permeability and general outer membrane permeability are discussed. Evidence for extensive homologies between protein F, the OmpA protein of E. coli and PHIII of Neisseria gonorrhoeae are presented. A role for protein F in prophylactic anti-Pseudomonas therapy, as a target for vaccine development, is proposed. Science, Faculty of Microbiology and Immunology, Department of Graduate

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Boyes, Barry Edward. "Molecular cloning of the human Substantia innominata : characterization of a brain large mRNA." Thesis, University of British Columbia, 1990. http://hdl.handle.net/2429/30960.

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Brain tissue samples were collected from individuals with histologically and biochemically confirmed Alzheimer's Disease (AD), as well as from a group of individuals without any signs of neurological disease (NNC). Ribonucleic acid (RNA) was extracted from these tissues, characterized by several chemical methods, and the yields were compared between AD and NNC groups. High molecular weight RNA could be effectively extracted from frozen postmortem human brain. In comparison to the NNC group, tissue RNA levels were reduced in the AD hippocampus, but not in the temporal cortex or substantia innominata (SI). No difference in the physical integrity of the RNA was apparent between AD and NNC groups. A high complexity complementary deoxyribonucleic acid (cDNA) library was prepared using RNA extracted from the NNC SI. Differential hybridization screening using a variety of cDNA probes was employed to identify mRNAs expressed differentially between AD and NNC tissue, and between SI and other human tissues. Many selected mRNAs were examined for specificity of expression in brain tissue and brain regions. The cDNA clone pSI3a-24 identified an mRNA, which, on Northern blot hybridization, was expressed in brain tissue but not in the other human tissues examined. The identified mRNA was unusually large, with a chain length estimated at 15,500 bases. Quantification of the brain tissue levels of this mRNA was carried out using a ribonuclease protection assay. Tissue levels were higher in the SI (40 pg/μg RNA) than in the temporal cortex (28.6 pg/μg), and were lowest in the cerebellum (11.2 pg/μ9). Levels of the mRNA in temporal cortex samples were increased 29% in the AD group, relative to NNC. No significant difference in the SI tissue levels was observed between AD and NNC groups. Hybridization analysis of human genomic DNA indicated that the mRNA was encoded by a single copy gene. Sequence analysis of the full 3 kilobases of cloned cDNA was completed. Computer database searches failed to identify any known nucleic acid sequence with homology to the cDNA. Examination of the cDNA sequence for potential polypeptide coding regions suggested that the corresponding mRNA has a 3' untranslated region of at least 3 kilobases. Medicine, Faculty of Graduate

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Lush, Michael John. "Molecular cloning of neuropathy target esterase." Thesis, University of Leicester, 1998. http://hdl.handle.net/2381/29627.

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A single ingestion of certain organophosphorus esters (OPs) can cause a syndrome known as Organophosphate Induced Delayed Polyneuropathy (OPIDP), a paralysing neuropathy with degeneration of long axons, developing after a latent period of approximately one to three weeks. The primary target of these OPs has been shown to be a 155kDa neural protein designated Neuropathy Target Esterase (NTE), and the toxic effects apparently due to the covalent inhibition and subsequent secondary modification of this protein. Recently NTE has been purified to apparent homogeneity using a novel biotinylated OP and sufficient pure protein was produced for limited problem sequencing. The aim of this project was to clone NTE cDNA using peptide sequence data. Initially, these sequences were used to design degenerate oligonucleotide primers for amplifying sections of brain cDNA by polymerase chain reaction (PCR). These approaches were unsuccessful. Subsequently, a database searching with the peptide sequences identified a number of Expressed Sequence Tags (EST)s; these could be aligned to form an initial contig of 2.2kbp which encoded the 3' end of NTE cDNA. The 5' end of NTE cDNA, comprising a further 2.2kbp, was obtained by PCR-based technique. The final 4.4kbp contig encoded a 1327 residue polypeptide predicted to have a molecular mass of 146kDa and at least one transmembrane domain. A novel serine esterase domain of approximately 200 residues was present near the C-terminus. NTE is unrelated to any known serine hydrolases but homologous proteins are predicted to be present in diverse prokaryotic and eukaryotic organisms. The homologue in Drosophila is associated with the swisscheese phenotype, an age-dependent neurodegeneration of the brain. NTE was also mapped to chromosome 19p 13.3 between markers D19216 and the D19S413 (using the UniGene database) and an OMIM search reveals that this is near the locus of cerebellar ataxia (Cayman type).

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Long, Graham Stanley. "Molecular cloning of bacteriophage K1E endosialidase." Thesis, University of Cambridge, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.339539.

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McNair, Alan Thomas. "Molecular cloning of Fasciola hepatica antigens." Thesis, Queen's University Belfast, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.335604.

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Choi, Wai To. "Molecular cloning of ribosome-inactivating proteins." HKBU Institutional Repository, 1996. http://repository.hkbu.edu.hk/etd_ra/63.

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Fisher, Adam B. "ex vivo DNA cloning." VCU Scholars Compass, 2015. http://scholarscompass.vcu.edu/etd/3962.

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Genetic engineering of microbes has developed rapidly along with our ability to synthesize DNA de novo. Yet, even with decreasing DNA synthesis costs there remains a need for inexpensive, rapid and reliable methods for assembling synthetic DNA into larger constructs or combinatorial libraries. While technological advances have resulted in powerful techniques for in vitro and in vivo assembly of DNA, each suffers inherent disadvantages. Here, an ex vivo DNA cloning suite using crude cellular lysates derived from E. coli is demonstrated to amplify and assemble DNA containing small sequence homologies. Further, the advantages of an ex vivo approach are leveraged to rapidly optimize several parameters of the ex vivo DNA assembly methodology testing lysates from different engineered strains of E. coli, with various buffer components and using titrations of purified cloning enzymes. Finally, in order to complete the cloning suite, a vector expressing the Pyrococcus furiosis (Pfu) DNA polymerase was designed, constructed and expressed in E. coli to create a ‘functionalized lysate’ capable of ex vivo PCR. Not only do we demonstrate ex vivo cloning methodology as a complete cloning package capable of replacing the expensive cloning reagents currently required by synthetic biologists, but also establish ex vivo as an overarching approach for conducting molecular biology.

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Wakarchuk, Warren William. "The molecular cloning and characterization of a Beta-glucosidase gene from an Agrobacterium." Thesis, University of British Columbia, 1987. http://hdl.handle.net/2429/27559.

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The β-glucosidase (Abg) from ATCC 21400, an Agrobacterium species, was purified to homogeneity. The protein was cleaved with cyanogen bromide and the peptides were purified by reversed phase high pressure liquid chromatography. The partial amino-acid sequences for three CNBr peptides, CNBr1, CNBr2 and CNBr3, were determined by automated Edman degradation. A sequence from CNBr2 was used to synthesize a mixture of oligonucleotides which was used as a hybridization probe to identify a recombinant DNA clone carrying the gene for β-glucosidase. A single clone was isolated which expressed an enzymatic activity that hydrolyzed several β-glucosides. The enzymatic activity produced by this clone could be adsorbed by rabbit antiserum raised against the Agrobacterium enzyme. The direction of transcription of the β-glucosidase gene was determined by verifying the DNA sequence 3' to the oligonucleotide probe binding site. After subcloning the gene a high level of expression was obtained in the plasmid vector pUC18 using the lacZ gene promoter. The nucleotide sequence of the 1599 bp insert in pABG5 was determined using the chain terminator method. The start of the protein coding region was determined by aligning the amino terminal sequence of the protein with the predicted amino acid sequence of the cloned gene. The open reading frame was 1387 nucleotides and contained 458 codons. The molecular weight calculated from the deduced amino acid sequence agreed with that observed from both the native and recombinant enzymes. The predicted amino acid composition from the open reading frame matched with that determined for the native β-glucosidase. The stop codon of this coding region was followed by a potential stem loop structure which may be the transcriptional terminator. There was a region of the deduced Abg sequence which had homology to a region from two other β-glucosidase sequences. This region of homology contained a putative active site by analogy with the active site of hen egg white lysozyme. Science, Faculty of Microbiology and Immunology, Department of Graduate

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Libros sobre el tema "Molecular cloning"

A, Lund Peter, and Minchin Steve, eds. Gene cloning. New York: Taylor & Francis Group, 2007.

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Habener, Joel F., ed. Molecular Cloning of Hormone Genes. Totowa, NJ: Humana Press, 1987. http://dx.doi.org/10.1007/978-1-4612-4824-8.

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Sambrook, Joseph. Molecular cloning: A laboratory manual. 2nd ed. Cold Spring Harbor, N.Y: Cold Spring Harbor Laboratory, 1989.

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Sambrook, Joseph. Molecular cloning: A laboratory manual. 2nd ed. Cold Spring Harbor, N.Y: Cold Spring Harbor Laboratory, 1989.

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Sambrook, Joseph. Molecular cloning: A laboratory manual. 2nd ed. Cold Spring Harbor, N.Y: Cold Spring Harbor Laboratory, 1989.

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Sambrook, Joseph. Molecular cloning: A laboratory manual. 2nd ed. Cold Spring Harbor, N.Y: Cold Spring Harbor Laboratory, 1987.

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Sambrook, Joseph. Molecular cloning: A laboratory manual. 2nd ed. Cold Spring Harbor, N.Y: Cold Spring Harbor Laboratory, 1989.

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Joseph, Sambrook, and Sambrook Joseph, eds. Molecular cloning: A laboratory manual. 4th ed. Cold Spring Harbor, N.Y: Cold Spring Harbor Laboratory Press, 2012.

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F, Fritsch E., and Maniatis Tom, eds. Molecular cloning: A laboratory manual. 2nd ed. Cold Spring Harbor, N.Y: Cold Spring Harbor Laboratory, 1989.

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F, Habener Joel, ed. Molecular cloning of hormone genes. Clifton, N.J: Humana Press, 1987.

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Capítulos de libros sobre el tema "Molecular cloning"

Brown, T. A. "Cloning genes." In Genetics: A Molecular Approach, 375–94. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2312-9_20.

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Deichmann, Annette, and Klaus Deichmann. "Cloning Vectors." In Techniques in Molecular Medicine, 226–54. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-59811-1_15.

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Ohara, Osamu. "ORFeome Cloning." In Methods in Molecular Biology, 3–9. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60761-232-2_1.

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Fontes, Andrew. "Cloning Technologies." In Methods in Molecular Biology, 253–61. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-348-0_20.

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Watson, Jake F., Sandra Arroyo-Urea, and Javier García-Nafría. "DNA Cloning." In Handbook of Molecular Biotechnology, 66–72. Boca Raton: CRC Press, 2024. http://dx.doi.org/10.1201/9781003055211-8.

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Liu, Dongyou. "RNA Cloning." In Handbook of Molecular Biotechnology, 159–62. Boca Raton: CRC Press, 2024. http://dx.doi.org/10.1201/9781003055211-18.

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Gulcher, Jeffrey, and Kari Stefansson. "Positional Cloning." In Methods in Molecular Medicine™, 137–52. Totowa, NJ: Humana Press, 2006. http://dx.doi.org/10.1007/978-1-59745-159-8_10.

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Li, Duanxiang. "Positional Cloning." In Methods in Molecular Medicine™, 125–36. Totowa, NJ: Humana Press, 2006. http://dx.doi.org/10.1007/978-1-59745-159-8_9.

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Julin, Douglas. "Plasmid Cloning Vectors." In Molecular Life Sciences, 1–12. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4614-6436-5_86-1.

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Julin, Douglas. "Cloning Vector Compatibility." In Molecular Life Sciences, 1–2. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4614-6436-5_92-4.

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Actas de conferencias sobre el tema "Molecular cloning"

Edgington, T. S., J. H. Morrissey, and H. Fakhrai. "MOLECULAR CLONING OF HUMAN TISSUE FACTOR cDNA." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643740.

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Tissue factor (TF), the cell-surface receptor and allo-steric activator for factor Vll/VIIa, is important in hemostasis andinflammation. The TF apoprotein was purifiedfrom human brain using factor Vll-affinitychromatography and SDS gel electrophoresis,and was found to consist of a 47 kDa heavy chain plus a 12.5 kDa light chain. Approximately one-third of the heavy chain amino acid sequence was determined for four regions by microsequencing the intact protein and peptides derived from V8-protease digestion. A λgtll cDNA library, made from mRNA derived from the human fibroblastic cell line WI38,was screened with (a) affinity-purified rabbit antibodies to human tissue factor, and (b) a 45-mer oligonucleotide probe based on TF heavy chain amino acid sequence. Five overlapping cDNA clones were identifiedand sequenced which confirmed all four partial TF amino acid sequences. Together these clones span the entire heavy chain coding sequence as well as 5" and 3" nontranslated regions. The N-terminusof the TF heavy chain is preceded by an unusually long signal peptide which appears to be cleaved at alternative sites two amino acids apart. This results in two variants of TF heavy chains which differ slightly in length and amino-terminal sequence.The deduced protein sequence shows no major homology to known protein sequences. However,a relatively uncommon tripeptide sequence, Trp-Lys-Ser (WKS), appears three times in the TF heavy chain. This tripeptidesequence also occurs in HMW kininogen, factor VIII,von Willebrand"s factor andant ithrombin-III. Limited sequence similarity is observed in flanking sequences,andthis may indicate a possible functional domain for the recognition of members ofthe vitamin K-dependent serine protease famil.Supported by NIH grants HL-16411 andCA-41085.

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Lopez, J. A., D. W. Chung, K. Fujikawa, F. S. Hagen, T. Papavannopoulou, and G. J. Roth. "MOLECULAR CLONING OF HUMAN PLATELET GLYCOPROTEIN Ib." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642927.

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Glycoprotein Ib (GPIb) mediates von Willebrand factor-dependent platelet adhesion and participates in the resulting platelet activation process. In the present investigation, the primary structure of human platelet GPIb was studied. GPIb and its proteolytic fragment glycocalicin were purified to near homogeneity from human platelets by affinity chromatography using wheat germ agglutinin and anti-GPIb monoclonal antibody (D. Nugent, University of Washington) coupled to Sepharose. GPIba chain, β chain, and glycocalicin were isolated, reduced and carboxymethylated, and then fragmented by trypsin and S. aureus V8 protease. Peptides were isolated by HPLC and subjected to amino acid sequence analysis. Approximately 200 amino acid residues were identified. Affinity purified rabbit antibodies directed against the a chain, the ft chain, and glycocalicin were prepared and shown to be monospecific by Western blot analysis. Total RNA was prepared from human erythroleukemia cells grown in the presence of phorbol acetate. Poly(A)+ RNA was selected and used to prepare a cDNA library in λgt11. The library was screened with [125]I-labeled polyclonal antibody to glycocalicin. The clone with the largest cDNA insert was sequenced and shown to code for amino acid sequences corresponding to those determined by Edman degradation of glycocalicin. The predicted amino acid sequence contains at least six tandem repeats of 24 amino acids that are highly homologous with 13 repeats present in leucine rich α2 glycoprotein of human plasma. Another region in the protein contains a second repeat rich in threonine and serine, which shows some homology to a 9 amino acid repeat in the connecting region of human factor V. This region is probably the major site of attachment of clusters of O-linked carbohydrate in GPIbα. These results indicate that human platelet glycoprotein Ibα has a multi-domain structure composed of a number of repetitive sequences. Supported in part by grants from the American Heart Association, Robert Wood Johnson Foundation, Veterans Administration, and National Institutes of Health.

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Fang, GuiJie, and XianFeng Qiao. "Molecular Cloning and Analysis of Hubei White Swine Myostatin Gene." In 2010 2nd International Conference on Information Engineering and Computer Science (ICIECS). IEEE, 2010. http://dx.doi.org/10.1109/iciecs.2010.5678159.

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Sun Qingpeng and Yu Yongkun. "Molecular cloning and bioinformatics analysis of genomic DNA of LeWRKY1." In 2010 2nd International Conference on Information Science and Engineering (ICISE). IEEE, 2010. http://dx.doi.org/10.1109/icise.2010.5690845.

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Yin, Heng, Xiaoming Zhao, and Yuguang Du. "Cloning and Molecular Characterization of a SKP1 Gene from Brassica napus." In 2009 3rd International Conference on Bioinformatics and Biomedical Engineering (iCBBE). IEEE, 2009. http://dx.doi.org/10.1109/icbbe.2009.5162512.

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Moheer, Reyad Qaed Al, Farah Diba Abu Bakar, and Abdul Munir Abdul Murad. "Molecular cloning and characterization of alpha - galactosidase gene from Glaciozyma antarctica." In THE 2015 UKM FST POSTGRADUATE COLLOQUIUM: Proceedings of the Universiti Kebangsaan Malaysia, Faculty of Science and Technology 2015 Postgraduate Colloquium. AIP Publishing LLC, 2015. http://dx.doi.org/10.1063/1.4931247.

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Uzan, G., A. Lajmanovich, M. H. Prandini, Ph Frachet, A. Duperray, and G. Marguerie. "MOLECULAR CLONING OF PLATELET GPIIb FROM HEL CELLS AND HUMAN MEGAKARYOCYTES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643960.

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Platelet GP IIb-IIIa is an heterodimer which functions as a receptor for fibrinogen, fibronectin and Von Willebrand factor and is implicated in platelet adhesive reactions. To study the structure function relationship of this glycoprotein, a recombinant DNA approach was initiated. cDNA expression libraries were constructed in » gtll vector, from erythro-leukemia cells (HEL) and megakaryocytes mRNA. The human megakaryocytes were isolated from patients with chronic myeloid leukemia. The HEL library was initially screened with polyclonal antibodies anti GPIIb IIIa. One clone, λIIbI, containing a 1.65 kbp insert reacted with a panel of different polyclonal antibodies anti GPIIb IIIa and a monoclonal antibody anti GPIIb. To further characterize this clone the synthesis of the fusion protein was induced by IPTG. The bacterial protein was then blotted onto nitro cellulose and incubated with antisera anti GPIIb-IIIa. Antibodies that specifically bound with the fusion protein were eluted and tested on platelet membrane extracts. The selected antibodies produced a positive signal at the GPIIb position similar to the signal produced by the monoclonal antibody anti GPIIb on the same membrane extract. Finally on western blotting, a protein of Mr= 170kD reacted with the monoclonal antibody anti GPIIb. λIIbI insert was used to screen the megakaryocyte library and 3 clones, λIIb2,λIIb3 and λIIb4 were isolated. The size of HEL cells and megakaryocytes GPIIb mRNA was estimated by northern blotting. Only one species of 3.9 kb was identified in both cells. The four different clones accounted for 50% of the coding sequence of this mRNA.Sequencing of these cDNAs indicated that the plasmatic domain of GPIIb contains a cystein rich region. The sequence of these clones will allow the study of the adhesines genetic diversity in different cellular systems.

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Zhang, Haiyan, Hongfang Ji, Lingwen Zhang, Xingquan Wu, and Shihua Chen. "Molecular cloning and sequence analysis of the endochitinase from Chaetomium cupreum." In 2010 3rd International Conference on Biomedical Engineering and Informatics (BMEI). IEEE, 2010. http://dx.doi.org/10.1109/bmei.2010.5639736.

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Qiu, Xingyang, Pei Ge, Yueyue Wang, and Hong Zhou. "Molecular Cloning and Identification of STAT4 in Grass Carp (Ctenopharyngodon idella)." In ICBBT '21: 2021 13th International Conference on Bioinformatics and Biomedical Technology. New York, NY, USA: ACM, 2021. http://dx.doi.org/10.1145/3473258.3473272.

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Zhou, Tao, Anchun Cheng, Mingshu Wang, Dekang Zhu, Xiaoyue Chen, An-chun Cheng, Ming-shu Wang, et al. "Molecular Cloning and Characterization of the UL10 Gene from Duck Enteritis Virus." In 2010 4th International Conference on Bioinformatics and Biomedical Engineering (iCBBE). IEEE, 2010. http://dx.doi.org/10.1109/icbbe.2010.5515899.

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Informes sobre el tema "Molecular cloning"

Kun, Ernest. Molecular Cloning of Adenosinediphosphoribosyl Transferase. Fort Belvoir, VA: Defense Technical Information Center, September 1987. http://dx.doi.org/10.21236/ada185458.

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Drager, Robert. Molecular cloning of spinach chloroplast DNA isolated by alkaline lysis. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.5631.

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Sebastian S. Cocioba, Sebastian S. Cocioba. Toward a Universal, Frugal, and Antibiotic-Free Sugar Selection System for Molecular Cloning. Experiment, April 2024. http://dx.doi.org/10.18258/69244.

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Robb, Frank T. Molecular Profiling of Microbial Communities from Contaminated Sources: Use of Subtractive Cloning Methods and rDNA Spacer Sequences. Office of Scientific and Technical Information (OSTI), April 2001. http://dx.doi.org/10.2172/781022.

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Dellaporta, S. L. Molecular cloning and structural characterization of the R locus maize: Annual progress report, September 1, 1987--May 31, 1988. Office of Scientific and Technical Information (OSTI), June 1988. http://dx.doi.org/10.2172/6412467.

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Krawiec, S. Molecular biological enhancement of coal desulfurization: Cloning and expression of the sulfoxide/sulfone/sulfonate/sulfate genes in Pseudomonads and Thiobacillae. Office of Scientific and Technical Information (OSTI), November 1991. http://dx.doi.org/10.2172/5587437.

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Zhang, Hongbin B., David J. Bonfil, and Shahal Abbo. Genomics Tools for Legume Agronomic Gene Mapping and Cloning, and Genome Analysis: Chickpea as a Model. United States Department of Agriculture, March 2003. http://dx.doi.org/10.32747/2003.7586464.bard.

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The goals of this project were to develop essential genomic tools for modern chickpea genetics and genomics research, map the genes and quantitative traits of importance to chickpea production and generate DNA markers that are well-suited for enhanced chickpea germplasm analysis and breeding. To achieve these research goals, we proposed the following research objectives in this period of the project: 1) Develop an ordered BAC library with an average insert size of 150 - 200 kb (USA); 2) Develop 300 simple sequence repeat (SSR) markers with an aid of the BAC library (USA); 3) Develop SSR marker tags for Ascochyta response, flowering date and grain weight (USA); 4) Develop a molecular genetic map consisting of at least 200 SSR markers (Israel and USA); 5) Map genes and QTLs most important to chickpea production in the U.S. and Israel: Ascochyta response, flowering and seed set date, grain weight, and grain yield under extreme dryland conditions (Israel); and 6) Determine the genetic correlation between the above four traits (Israel). Chickpea is the third most important pulse crop in the world and ranks the first in the Middle East. Chickpea seeds are a good source of plant protein (12.4-31.5%) and carbohydrates (52.4-70.9%). Although it has been demonstrated in other major crops that the modern genetics and genomics research is essential to enhance our capacity for crop genetic improvement and breeding, little work was pursued in these research areas for chickpea. It was absent in resources, tools and infrastructure that are essential for chickpea genomics and modern genetics research. For instance, there were no large-insert BAC and BIBAC libraries, no sufficient and user- friendly DNA markers, and no intraspecific genetic map. Grain sizes, flowering time and Ascochyta response are three main constraints to chickpea production in drylands. Combination of large seeds, early flowering time and Ascochyta blight resistance is desirable and of significance for further genetic improvement of chickpea. However, it was unknown how many genes and/or loci contribute to each of the traits and what correlations occur among them, making breeders difficult to combine these desirable traits. In this period of the project, we developed the resources, tools and infrastructure that are essential for chickpea genomics and modern genetics research. In particular, we constructed the proposed large-insert BAC library and an additional plant-transformation-competent BIBAC library from an Israeli advanced chickpea cultivar, Hadas. The BAC library contains 30,720 clones and has an average insert size of 151 kb, equivalent to 6.3 x chickpea haploid genomes. The BIBAC library contains 18,432 clones and has an average insert size of 135 kb, equivalent to 3.4 x chickpea haploid genomes. The combined libraries contain 49,152 clones, equivalent to 10.7 x chickpea haploid genomes. We identified all SSR loci-containing clones from the chickpea BAC library, generated sequences for 536 SSR loci from a part of the SSR-containing BACs and developed 310 new SSR markers. From the new SSR markers and selected existing SSR markers, we developed a SSR marker-based molecular genetic map of the chickpea genome. The BAC and BIBAC libraries, SSR markers and the molecular genetic map have provided essential resources and tools for modern genetic and genomic analyses of the chickpea genome. Using the SSR markers and genetic map, we mapped the genes and loci for flowering time and Ascochyta responses; one major QTL and a few minor QTLs have been identified for Ascochyta response and one major QTL has been identified for flowering time. The genetic correlations between flowering time, grain weight and Ascochyta response have been established. These results have provided essential tools and knowledge for effective manipulation and enhanced breeding of the traits in chickpea.

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Robb, F. T. Molecular profiling of microbial communities from contaminated sources: Use of subtractive cloning methods and rDNA spacer sequences. 1998 annual progress report. Office of Scientific and Technical Information (OSTI), June 1998. http://dx.doi.org/10.2172/13700.

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