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  • Articles  (26)
  • Cell & Developmental Biology  (20)
  • cell walls  (6)
  • Polymer and Materials Science
  • Biology  (26)
  • 1
    Electronic Resource
    Electronic Resource
    Substituted truxillic and truxinic acids in cell walls of Cynodon dactylon
    Amsterdam : Elsevier
    Phytochemistry 29 (1990), S. 3699-3703 
    Details
    ISSN: 0031-9422
    Keywords: Cynodon dactylon ; Poaceae ; cell walls ; coastal bermudagrass ; phenolic acids ; photodimerization ; substituted truxillic acids ; substituted truxinic acids.
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0031-9422(90)85316-8
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  • 2
    Electronic Resource
    Electronic Resource
    Cross-linking of cell wall phenolic arabinoxylans in graminaceous plants
    Amsterdam : Elsevier
    Phytochemistry 29 (1990), S. 3705-3709 
    Details
    ISSN: 0031-9422
    Keywords: Cynodon dactylon: Poaceae ; O-[5-O-((E)-feruloyl-α-L-ara- ; O-[5-O-(E)-p-coumaroyl)-α-L- ; arabinoxylans. ; cell walls ; coastal bermudagrass ; photodimerization ; substituted truxillic acids ; substituted truxinic acids
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0031-9422(90)85317-9
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  • 3
    Electronic Resource
    Electronic Resource
    Lignin-carbohydrate complexes from Lolium perenne
    Amsterdam : Elsevier
    Phytochemistry 13 (1974), S. 1161-1165 
    Details
    ISSN: 0031-9422
    Keywords: Gramineae ; Lolium perenne ; UV ; cell walls ; lignin-carbohydrate complexes ; lignin-hemicellulose complexes ; molecular sieve chromatography ; ryegrass
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0031-9422(74)80092-0
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  • 4
    Electronic Resource
    Electronic Resource
    Delignification and hemicellulose extraction of cell walls of Lolium perenne and Trifolium pratense
    Amsterdam : Elsevier
    Phytochemistry 14 (1975), S. 505-508 
    Details
    ISSN: 0031-9422
    Keywords: Leguminosae ; Lolium perenne: Gramineae ; Trifolium pratense ; cell walls ; delignification ; gel filtration. ; hemicelluloses ; red clover ; ryegrass
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0031-9422(75)85118-1
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  • 5
    Electronic Resource
    Electronic Resource
    Isolation and analysis of lignin-carbohydrate complexes from Lolium multiflorum
    Amsterdam : Elsevier
    Phytochemistry 12 (1973), S. 2979-2984 
    Details
    ISSN: 0031-9422
    Keywords: Gramineae ; Lolium multiflorum ; UV spectra ; cell walls ; grass ; hemicelluloses. ; lignin ; lignin-carbohydrate complexes ; molecular sieve chromatography
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0031-9422(73)80518-7
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  • 6
    Electronic Resource
    Electronic Resource
    Delignification and hemicellulose extraction of cell walls of Lolium perenne and Trifolium pratense
    Amsterdam : Elsevier
    Phytochemistry 14 (1975), S. 505-508 
    Details
    ISSN: 0031-9422
    Keywords: Gramineae ; Leguminosae ; Lolium perenne ; Trifolium pratense ; cell walls ; delignification ; gel filtration ; hemicelluloses ; red clover ; ryegrass
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0031-9422(75)85118-1
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  • 7
    Electronic Resource
    Electronic Resource
    Effects of thymosin β4 and thymosin β10 on actin structures in living cells (1994)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 27 (1994), S. 13-25 
    Details
    ISSN: 0886-1544
    Keywords: Tβ4 ; Tβ10 ; β-thymosins ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The β-thymosins are a family of small proteins originally isolated from the thymus. Recently, two of the major mammalian isoforms, thymosin β4 (Tβ4) and thymosin β10 (Tβ10), are identified as significant actin monomer sequestering proteins which may be involved in regulating actin filament assembly. To study the cellular function of β-thymosins, we have used isoform-specific antibodies to determine their concentration and intracellular distribution, and examined the effects of inducing overexpression of Tβ4 and Tβ10 on actin filament structures. Immunofluorescence labeling of peritoneal macrophages showed that both β-thymosins are uniformly distributed within the cytoplasm. cDNA-mediated overexpression of β-thymosins in CV1 fibroblasts induced extensive loss of phalloidinstained actin stress fibers. Stress fibers in the cell center were more susceptible than those at the periphery. There was a decrease in the number of focal adhesions, as evidenced by a decrease in discrete vinculin staining and an increase in diffuse vinculin fluorescence. The majority of the transfected cells had normal shape in spite of extensive loss of actin filaments. Occasionally, cells overexpressing β-thymosin were observed to divide. In these cells, β-thymosin was excluded from the midbody which contains an actin filament-rich contractile ring. Our results indicate that Tβ4 and Tβ10 are functionally very similar and both are effective regulators of a large subset of actin filaments in living cells. © 1994 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970270103
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  • 8
    Electronic Resource
    Electronic Resource
    Vitamin D receptor alleles and bone physiology (1994)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 56 (1994), S. 307-314 
    Details
    ISSN: 0730-2312
    Keywords: vitamin D calcitriol ; bone ; genetics ; steroid hormone receptor ; vitamin D receptor ; retinoic acid receptor ; calcium ; homeostasis ; calcitonin ; parathyroid hormone ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The vitamin D endocrine system is central to the control of bone and calcium homeostasis. The active hormonal aform of vitamin D, 1,25 dihydroxyvitamin D (calcitriol), the circulating level of which is tightly regulated, acts through a specific receptor to mediate its genomic actions on almost every aspect of calcium homeostasis. Because of its transactivation function, it possible that a small difference in vitamin D receptor level could be amplified into a biologically significant alteration in physiological setpoint. The recent finding that polymorphisms in the vitamin D receptor gene are predictive of bone density (morrison et al., Nature 367:284-287, 1994) is the first example of an allelic effect in such a homeostatically controlled system. This raises the possibility that such central operators may exist in other regulatory pathways, and could expllain a large part of the observed “ormal” population distribution that exists for all physiological paraameters.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240560306
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  • 9
    Electronic Resource
    Electronic Resource
    PTH-responsive osteoblast nuclear matrix architectural transcription factor binds to the rat type I collagen promoterThe first two authors contributed equally to this work. (1998)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 69 (1998), S. 336-352 
    Details
    ISSN: 0730-2312
    Keywords: architectural transcription factor ; nuclear matrix ; osteoblast ; parathyroid hormone ; type I collagen ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: In connective tissue, cell structure contributes to type I collagen expression. Differences in osteoblast microarchitecture may account for the two distinct cis elements regulating basal expression, in vivo and in vitro, of the rat type I collagen α1(I) polypeptide chain (COL1A1). The COL1A1 promoter conformation may be the penultimate culmination of osteoblast structure. Architectural transcription factors bind to the minor groove of AT-rich DNA and bend it, altering interactions between other trans-acting proteins. Similarly, nuclear matrix (NM) proteins bind to the minor groove of AT-rich matrix-attachment regions, regulating transcription by altering DNA structure. We propose that osteoblast NM architectural transcription factors link cell structure to promoter geometry and COL1A1 transcription. Our objective was to identify potential osteoblast NM architectural transcription factors near the in vitro and in vivo regulatory regions of the rat COL1A1 promoter. Nuclear protein-promoter interactions were analyzed by gel shift analysis and related techniques. NM extracts were derived from rat osteosarcoma cells and from rat bone. The NM protein, NMP4, and a soluble nuclear protein, NP, both bound to two homologous poly(dT) elements within the COL1A1 in vitro regulatory region and proximal to the in vivo regulatory element. These proteins bound within the minor groove and bent the DNA. Parathyroid hormone increased NP/NMP4 binding to both poly(dT) elements and decreased COL1A1 mRNA in the osteosarcoma cells. NP/NMP4-COL1A1 promoter interactions may represent a molecular pathway by which osteoblast structure is coupled to COL1A1 expression. J. Cell. Biochem. 69:336-352. © 1998 Wiley-Liss, Inc.
    Additional Material: 12 Ill.
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  • 10
    Electronic Resource
    Electronic Resource
    Identification of a vitamin D3 response element in the fibronectin gene that is bound by a vitamin D3 receptor homodimer (1996)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 60 (1996), S. 322-333 
    Details
    ISSN: 0730-2312
    Keywords: fibronectin ; VDR ; homodimer ; vitamin D regulation ; transcription ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Fibronectin (FN) is an important adhesive noncollagenous glycoprotein involved in maintenance of the extracellular matrix and cell adhesiveness, loss of which has been implicated in the metastatic potential of cells. Regulation of FN occurs at the transcriptional level by the active metabolite of vitamin D3, 1,25-dihydroxyvitamin D3 (1,25-(OH)2D3). Transient transfection of homologous and heterologous promoter reporter constructs into ROS 17/2,8 (rat osteosarcoma), NIH 3T3 (mouse fibroblast), and MCF-7 (human mammary carcinoma) cell lines showed a consistent two- to threefold induction of transcription when stimulated with 1,25-(OH)2D3. These heterologous promoter transfection studies with gel shift analysis locate a third, natural DR6-type vitamin D responsive element (VDRE) at nucleotide positions -171 to -154 in the murine FN promoter. Interestingly, this VDRE is also present in rat and human FN promoters. This study shows that 1,25-(OH)2D3 induces FN transcription from an existing elevated basal transcriptional activity by acting through two putative hexameric core binding motifs which bind VDR homodimers. Furthermore, the FN VDRE is the first homodimer-type VDRE that is not overlaid by a DR3-type structure. © 1996 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
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