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  • 1
    Electronic Resource
    Electronic Resource
    Evolution of estrogen binding in rat and mouse alpha-fetoprotein (1989)
    New York, NY : Wiley-Blackwell
    BioEssays 11 (1989), S. 112-114 
    Details
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bies.950110409
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  • 2
    Electronic Resource
    Electronic Resource
    Molecular genetic aspects of sex determination in Drosophila (1987)
    New York, NY : Wiley-Blackwell
    BioEssays 6 (1987), S. 66-70 
    Details
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Analysis of the mechanisms underlying sex determination and sex differentiation in Drosophila has provided evidence for a complex but comprehensible regulatory hierarchy governing these developmental decisions. It is suggested here that the pattern of sexual differentiation and dosage compensation characteristic of the male is a default regulatory state. Recent results have provided, in addition, some surprising and intriguing conclusions: (1) that several of the critical controlling genes produce more transcripts than was predicted from the genetic analyses; (2) that setting of the alternative sex-specific states of the doublesex (dsx) locus involves differential transcript processing; and (3) that some aspects of sexual differentation require the prolonged action of certain elements of the regulatory hierarchy. These findings are discussed in connection with the current model of sex determination in Drosophila.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bies.950060206
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  • 3
    Electronic Resource
    Electronic Resource
    Nayudamma memorial symposium - madras, India, 15-17 December 1986 (1988)
    New York, NY : Wiley-Blackwell
    BioEssays 8 (1988), S. 130-132 
    Details
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bies.950080410
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  • 4
    Electronic Resource
    Electronic Resource
    Partial purification of microsomal signal peptidase from hen oviduct (1986)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 32 (1986), S. 193-200 
    Details
    ISSN: 0730-2312
    Keywords: hen oviduct ; human preplacental lactogen ; phosphlipid reactivation ; purification ; signal peptidase ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Signal peptidase has been purified approximately 600-fold from hen oviduct microsomes. Treatment of microsomes with ice-cold sodium carbonate at pH 11.5 removes soluble and extrinsic membrane proteins prior to solubilization of signal peptidase with Nonidet P-40. After dialysis to pH 8.2, the solubilized enzyme is chromatographed on diethylaminoethyl cellulose at pH 8.2. More than 90% of contaminating proteins bind to the column while signal peptidase and endogenous phospholipid are eluted in the column void volume. Enzyme activity subsequently binds to carboxymethyl cellulose at pH 5.8 and is eluted by approximately 100 to 200 mM NaCl during a NaCl gradient. Polypeptides present in partially purified hen oviduct signal peptidase have relative molecular masses ranging from 54 kD to less than 11 kD with major bands at 29, 23, 22, 19, 18 and 13 kD. The purified peptidase requires phospholipid for activity and is maximally active in the presence of 2 mg/ml phosphatidylcholine.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240320305
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  • 5
    Electronic Resource
    Electronic Resource
    Formation of protease nexin-thrombin complexes on the platelet surface (1986)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 32 (1986), S. 201-206 
    Details
    ISSN: 0730-2312
    Keywords: protease nexin ; thrombin ; platelets ; protease inhibitor ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: We have recently described a platelet factor that is similar to the fibroblast thrombin inhibitor protease nexin I (PNI) [12]. The present manuscript shows that this platelet form of PN (PNp) does not complex [125I]-thrombin that has been blocked at its active site, consistent with the conclusion that it is a thrombin inhibitor. When platelets are incubated with [125I]-thrombin, PNp-[125MI]-thrombin complexers accumulate both in the medium and on the platelet surface. In the case of fibroblasts, PNI-[125I]-thrombin Complexes that form in solution bind to the cells as a consequence of a receptor-mediated clearance process [Low et al, Proc Natl Acad Sci USA 78:2340, 1981]. We show here that the PNp-[125I]-thrombin complexes that accumulate in platelet-binding incubation medium do not bind to platelets. Thus, the platelet-associated complexes must form by [125I]-thrombin binding to PNp that is associated with the platelet surface. Pretreatment of platelets with heparin markedly increases the number of PNp-[125I]-thrombin complexes that form on platelets. The basis for this increase in unclear. This effect seems incompatible with a heparinlike factor acting as the surface binding site for PNp.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240320306
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  • 6
    Electronic Resource
    Electronic Resource
    Transport of proteins into yeast mitochondria (1988)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 36 (1988), S. 59-71 
    Details
    ISSN: 0730-2312
    Keywords: origin of presequences ; intracellular ; intramitochondrial protein sorting ; stop-transport sequence ; ATP requirement ; protein unfolding ; translocation machinery ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The amino-terminal sequences of several imported mitochondrial precursor proteins have been shown to contain all the information required for transport to and sorting within mitochondria. Proteins transported into the matrix contain a matrix-targeting sequence. Proteins destined for other submitochondrial compartments contain, in addition, an intramitochondrial sorting sequence. The sorting sequence in the cytochrome c1 presequence is a stop-transport sequence for the inner mitochondrial membrane. Proteins containing cleavable presequences can reach the intermembrane space by either of two pathways: (1) Part of the presequence is transported into the matrix; the attached protein, however, is transported across the outer but not the inner membrane (eg, the cytochrome c1 presequence). (2) The precursor is first transported into the matrix; part of the presequence is then removed, and the protein is reexported across the inner membrane (eg, the precursor of the iron-sulphur protein of the cytochrome bc1 complex).Matrix-targeting sequences lack primary amino acid sequence homology, but they share structural characteristics. Many DNA sequences in a genome can potentially encode a matrix-targeting sequence. These sequences become active if positioned upstream of a protein coding sequence. Artificial matrix-targeting sequences include synthetic presequences consisting of only a few different amino acids, a known amphiphilic helix found inside a cytosolic protein, and the presequence of an imported chloroplast protein.Transport of proteins across mitochrondrial membranes requires a membranes requires a membrane potential, ATP, and a 45-kd protein of the mitochondrial outer membrane. The ATP requirement for import is correlated with a stable structure in the imported precursor molecule. We suggest that transmembrane transport of a stably folded precursor requires an ATP-dependent unfolding of the precursor protein.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240360107
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  • 7
    Electronic Resource
    Electronic Resource
    A method for determining dislocation Burgers' vectors in ice (1986)
    New York, NY : Wiley-Blackwell
    Journal of Electron Microscopy Technique 3 (1986), S. 357-358 
    Details
    ISSN: 0741-0581
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: It is shown that the usual method of Burgers' vector analysis in the Transmission Electron Microscope (TEM) using invisibility criteria is unlikely to succeed for ice. A method is outlined using a novel application of computer-simulated imaging which can be used to perform such an analysis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1060030308
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  • 8
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    A family of putative potassium channel genes in Drosophila (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-02-17
    Description: Mutant flies in which the gene coding for the Shaker potassium channel is deleted still have potassium currents similar to those coded by the Shaker gene. This suggests the presence of a family of Shaker-like genes in Drosophila. By using a Shaker complementary DNA probe and low-stringency hybridization, three additional family members have now been isolated, Shab, Shaw, and Shal. The Shaker family genes are not clustered in the genome. The deduced proteins of Shab, Shaw, and Shal have high homology to the Shaker protein; the sequence identity of the integral membrane portions is greater than 50 percent. These genes are organized similarly to Shaker in that only a single homology domain containing six presumed membrane-spanning segments common to all voltage-gated ion channels is coded by each messenger RNA. Thus, potassium channel diversity could result from an extended gene family, as well as from alternate splicing of the Shaker primary transcript.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Butler, A -- Wei, A G -- Baker, K -- Salkoff, L -- 1 RO1 NS24785-01/NS/NINDS NIH HHS/ -- GMO 7200/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1989 Feb 17;243(4893):943-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2493160" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Blotting, Northern ; Carrier Proteins/*genetics ; Drosophila Proteins ; Drosophila melanogaster/*genetics ; *Genes ; Molecular Sequence Data ; *Multigene Family ; Potassium Channels/*physiology ; Protein Conformation ; RNA, Messenger/genetics ; Shab Potassium Channels
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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