Trends in the carbonated beverage industry

Hall, Jennie; Swaine, Robert L.; Miller, W. Todd

doi:10.1080/10408397209527130

Cited by 8 publications

(9 citation statements)

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“…Although somewhat similar discontinuities in the (Gly-X-Y) repeat are seen in the A, B, and C chains of human Clq (25), the fact that these collagenous regions are only approximately 80 residues in length argues against a close relationship between these and the collagen sequences presented here. Also, it appears unlikely that this Drosophila collagen gene represents the collagenous portion of acetylcholinesterase because no in situ hybridization was detected at the 87E2-4 locus (26) assigned to this enzyme. Finally, the fact that this collagenous sequence, like most other known proa chains, is encoded by a large (6.4 kb) RNA argues strongly for its identification as a bonafide collagen gene segment.…”

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confidence: 99%

Expression and novel structure of a collagen gene in Drosophila.

Monson¹,

Natzle²,

Friedman³

et al. 1982

Proc. Natl. Acad. Sci. U.S.A.

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We report the structure and developmental expression of collagen gene sequences in Drosophila melanogaster. Collagen-like genomic clones were isolated by screening a Drosophila genomic library with a chicken proa2(I) cDNA clone as a hybridization probe. A 1.5-kilobase (kb) DNA sequence from a 9.2-kb DNA clone (pDCgl) is presented. Unlike the highly fragmented genes for vertebrate type I collagen, there is no evidence of a 54-base-pair primordial unit within this gene segment. Instead, the fragment is composed of two large coding sequences. Together they specify a sequence of 469 amino acids. This collagen product is composed almost entirely of the Gly-X-Y repeat characteristic of peptides involved in triple helix formation. Within the polypeptide there are four minor discontinuities in the Gly-X-Y pattern. Similar interruptions have been observed in a mouse basement membrane collagen protein sequence. Therefore, the Drosophila collagen gene may encode a nonfibrous collagen such as a basement membrane or cuticle collagen or a novel collagenous protein. By using the DNA segment of known sequence as a hybridization probe, a developmental sequence of polyadenylylated RNA samples was screened for the presence of homologous sequences. A RNA species 6.4 kb in length was detected as a prominent band only in the first-and second-instar larval stages. This pattern of developmental hybridization correlates with the production ofthe cuticle and basement membranes, and the large size of the RNA is consistent with its identification as a collagen-encoding RNA.Much of the current interest in the collagen gene family comes from the key role these extracellular structural proteins play in developmental processes and tissue architecture as well as their complex gene structure. The highly unusual genomic organization of procollagen genes poses some fascinating questions concerning the evolution ofthe collagen gene family. However, to date the only collagen genes examined encode the constituent polypeptide (proa) chains of vertebrate type I collagen. In particular, these are the proa2(I) genes from chicken (1, 2) and sheep (3) and the proal(I) gene from mice (4). Except for the immunoglobulin, viral, and mitochondrial genes, these procollagen genes exhibit the greatest complexity in their genome organization of all the eukaryotic genes studied. For example, in the proa2(I) gene there may be 50 or more intervening sequences distributed over 38 kilobases (kb) of genomic DNA. Even more unusual is the preponderance of 54-base-pair (bp) coding sequences observed in this gene. This observation led to the hypothesis that procollagen genes arose by amplification of a primordial 54-bp unit (1). However, a more compact genomic organization is observed in a proal(I) procollagen gene (4). Here only five of the eight coding sequences studied are 54 bp and the remainder are 108 bp. Thus, a more complex evolutionary history has been postulated for procollagen genes (4). Whether other fibrous procollagen genes resemble either the proal(I)...

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confidence: 99%

Expression and novel structure of a collagen gene in Drosophila.

Monson¹,

Natzle²,

Friedman³

et al. 1982

Proc. Natl. Acad. Sci. U.S.A.

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“…34 and references therein), or a single gene as has been found in Drosophila (35,36). Cloning of cDNAs encoding the catalytic subunits of AcChoEase from Torpedo californica (37) and Torpedo marmorata (38) and analysis of genomic sequences (38,39) indicate that AcChoEase is encoded by a single gene in these species.…”

Section: Resultsmentioning

confidence: 99%

Allelic variants of acetylcholinesterase: genetic evidence that all acetylcholinesterase forms in avian nerves and muscles are encoded by a single gene.

Rotundo

Gómez

Fernández‐Valle

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

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“…Hall found Kankel to be replete with detailed knowledge of Drosophila biology that extended to neuroanatomy and neurochemistry, all of which Hall gratefully absorbed. The pair began collaborating on two projects, both of which progressed surprisingly well, Hall says (4,5 At Brandeis, Hall carried forward the momentum of his work with Kankel, who by that time was working at Yale University (New Haven, CT). A particularly intriguing research thread sprang from an offhand suggestion from Kankel during Hall's last months in California.…”

Section: Universal Slices Of Courtshipmentioning

confidence: 99%

Profile of Jeffrey C. Hall

Nuzzo¹

2005

Proc. Natl. Acad. Sci. U.S.A.

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Trends in the carbonated beverage industry

Cited by 8 publications

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Expression and novel structure of a collagen gene in Drosophila.

Expression and novel structure of a collagen gene in Drosophila.

Allelic variants of acetylcholinesterase: genetic evidence that all acetylcholinesterase forms in avian nerves and muscles are encoded by a single gene.

Profile of Jeffrey C. Hall

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