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Autor: David A. Dean, Warren E. Zimmer, D D Strong

Publikováno v: Gene therapy. 12(11)

Nonviral gene delivery is limited to a large extent by multiple extracellular and intracellular barriers. One of the major barriers, especially in nondividing cells, is the nuclear envelope. Once in the cytoplasm, plasmids must make their way into th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd6cb19ca8e5fbba9a668d577920cc39
https://pubmed.ncbi.nlm.nih.gov/15908994

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Construction of a BAC contig for a 3 cM biologically significant region of mouse chromosome 1

Autor: W K, Gu, X M, Li, B, Edderkaoui, D D, Strong, K H W, Lau, W G, Beamer, L R, Donahue, S, Mohan, D J, Baylink

Publikováno v: Genetica. 114(1)

One QTL and genes and phenotypes have been localized in the region between 92 cM and 95cM of mouse chromosome 1. The QTL locus contributes to approximately 40% of the variation of the peak bone density between C57BL/6J (B6) and CAST/EiJ (CAST) strain

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https://pubmed.ncbi.nlm.nih.gov/11990753

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TWIST, a basic helix-loop-helix transcription factor, can regulate the human osteogenic lineage

Autor: M S, Lee, G N, Lowe, D D, Strong, J E, Wergedal, C A, Glackin

Publikováno v: Journal of cellular biochemistry. 75(4)

Basic helix-loop-helix (bHLH) transcription factors have been shown to play an important role in controlling cell type determination and differentiation. TWIST, a member of the bHLH transcription factor family, is involved in the development of mesod

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https://pubmed.ncbi.nlm.nih.gov/10572240

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Osteogenic protein-1 stimulates production of insulin-like growth factor binding protein-3 nuclear transcripts in human osteosarcoma cells

Autor: J M, Hayden, D D, Strong, D J, Baylink, D R, Powell, T K, Sampath, S, Mohan

Publikováno v: Endocrinology. 138(10)

To begin delineating molecular mechanisms by which osteogenic protein-1 (OP-1) modulates its effect on the insulin-like growth factor (IGF) system in human skeletal cells, we evaluated time-course effects of OP-1 on the expression of IGFBP-3 messenge

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https://pubmed.ncbi.nlm.nih.gov/9322936

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INTERACTION OF FIBRINOGEN WITH STAPHYLOCOCCAL CLUMPING FACTOR AND WITH PLATELETS

Autor: Sheila Timmons, Marek Kloczewiak, D. D. Strong, Russell F. Doolittle, Jacek Hawiger

Publikováno v: Annals of the New York Academy of Sciences. 408:521-535

Fibrinogen, a clottable plasma glycoprotein, participates in cell adhesion phenomena involving prokaryotic cells, e.g. staphylococci, and eukaryotic cell fragments, e.g. platelets. Among the three chains (alpha, beta, gamma) of human fibrinogen, the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3faabcd4936764947697eabdc3e00379
https://doi.org/10.1111/j.1749-6632.1983.tb23270.x

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Antibodies against synthetic peptides reveal that the unidentified reading frame A6L, overlapping the ATPase 6 gene, is expressed in human mitochondria

Autor: Dennis Trovato, Paolo Mariottini, Russell F. Doolittle, Giuseppe Attardi, D. D. Strong, Anne Chomyn

Publikováno v: Cell. 32:1269-1277

Antibodies prepared against chemically synthesized peptides predicted from the DNA sequence have been used to detect human mitochondrial gene products. In particular, antibodies directed against either the NH 2 -terminal decapeptide or the COOH-termi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c606bf0a0606ef1c21a8b7df150e67b
https://doi.org/10.1016/0092-8674(83)90308-2

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Identification of a region of human fibrinogen interacting with staphylococcal clumping factor

Autor: Jacek Hawiger, Barbara A. Cottrell, Sheila Timmons, Russell F. Doolittle, Marcia Riley, D. D. Strong

Publikováno v: Biochemistry. 21:1407-1413

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee920616c2af930ae01a9cda5b218bd0
https://doi.org/10.1021/bi00535a047

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Amino acid sequence studies on the alpha chain of human fibrinogen. Exact location of cross-linking acceptor sites

Autor: Russell F. Doolittle, K. W. K. Watt, Barbara A. Cottrell, D. D. Strong

Publikováno v: Biochemistry. 18(24)

Human fibrinogen was clotted under conditions that promote latent factor XIII activity and in the presence of a radioactive substitute cross-linking donor ([14C]glycine ethyl ester). The labeled fibrin was reduced and alkylated in the presence of 6 M

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https://pubmed.ncbi.nlm.nih.gov/518845

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