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  • Base Sequence  (704)
  • *Ecosystem
  • American Association for the Advancement of Science (AAAS)  (704)
  • American Association of Petroleum Geologists (AAPG)
  • 1990-1994  (704)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (704)
  • American Association of Petroleum Geologists (AAPG)
Years
Year
  • 1
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    CD26 antigen and HIV fusion? (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-05-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Patience, C -- McKnight, A -- Clapham, P R -- Boyd, M T -- Weiss, R A -- Schulz, T F -- G117/547/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 1994 May 20;264(5162):1159-60; author reply 1162-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7909960" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/*physiology ; Antigens, Differentiation, T-Lymphocyte/*physiology ; Base Sequence ; Cats ; Cell Line ; Dipeptidyl Peptidase 4 ; HIV-1/*physiology ; Humans ; Mink ; Molecular Sequence Data
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Microtubule severing by elongation factor 1 alpha (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-14
    Description: An activity that severs stable microtubules is thought to be involved in microtubule reorganization during the cell cycle. Here, a 48-kilodalton microtubule-severing protein was purified from Xenopus eggs and identified as translational elongation factor 1 alpha (EF-1 alpha). Bacterially expressed human EF-1 alpha also displayed microtubule-severing activity in vitro and, when microinjected into fibroblasts, induced rapid and transient fragmentation of cytoplasmic microtubule arrays. Thus, EF-1 alpha, an essential component of the eukaryotic translational apparatus, appears to have a second role as a regulator of cytoskeletal rearrangements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shiina, N -- Gotoh, Y -- Kubomura, N -- Iwamatsu, A -- Nishida, E -- New York, N.Y. -- Science. 1994 Oct 14;266(5183):282-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics and Molecular Biology, Kyoto University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939665" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/pharmacology ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Guanosine Triphosphate/analogs & derivatives/metabolism ; Humans ; Microtubules/drug effects/*metabolism ; Molecular Sequence Data ; Molecular Weight ; Oocytes ; Peptide Elongation Factor 1 ; Peptide Elongation Factors/chemistry/isolation & purification/*physiology ; Rats ; Recombinant Proteins/pharmacology ; Ribonucleoproteins/chemistry/isolation & purification/*physiology ; Sepharose/analogs & derivatives/metabolism ; Xenopus laevis
    Print ISSN: 0036-8075
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  • 3
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    Enhancer point mutation results in a homeotic transformation in Drosophila (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-05-13
    Description: In Drosophila, the misexpression or altered activity of genes from the bithorax complex results in homeotic transformations. One of these genes, abd-A, normally specifies the identity of the second through fourth abdominal segments (A2 to A4). In the dominant Hyperabdominal mutations (Hab), portions of the third thoracic segment (T3) are transformed toward A2 as the result of ectopic abd-A expression. Sequence analysis and deoxyribonuclease I footprinting demonstrate that the misexpression of abd-A in two independent Hab mutations results from the same single base change in a binding site for the gap gene Kruppel protein. These results establish that the spatial limits of the homeotic genes are directly regulated by gap gene products.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shimell, M J -- Simon, J -- Bender, W -- O'Connor, M B -- New York, N.Y. -- Science. 1994 May 13;264(5161):968-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Biochemistry, University of California, Irvine 92717.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7909957" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; DNA-Binding Proteins/genetics/metabolism ; *Drosophila Proteins ; Drosophila melanogaster/embryology/*genetics ; Enhancer Elements, Genetic/*genetics ; Gene Expression Regulation ; *Genes, Homeobox ; Genes, Insect ; Kruppel-Like Transcription Factors ; Molecular Sequence Data ; *Nuclear Proteins ; *Point Mutation ; Proteins/*genetics ; Regulatory Sequences, Nucleic Acid ; *Repressor Proteins ; Transcription Factors/genetics/metabolism
    Print ISSN: 0036-8075
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  • 4
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    Requirement for intron-encoded U22 small nucleolar RNA in 18S ribosomal RNA maturation (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-02
    Description: The nucleoli of vertebrate cells contain a number of small RNAs that are generated by the processing of intron fragments of protein-coding gene transcripts. The host gene (UHG) for intro-encoded human U22 is unusual in that it specifies a polyadenylated but apparently noncoding RNA. Depletion of U22 from Xenopus oocytes by oligonucleotide-directed ribonuclease H targeting prevented the processing of 18S ribosomal RNA (rRNA) at both ends. The appearance of 18S rRNA was restored by injection of in vitro-synthesized U22 RNA. These results identify a cellular function for an intron-encoded small RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tycowski, K T -- Shu, M D -- Steitz, J A -- GM26154/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 2;266(5190):1558-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06536.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7985025" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Blotting, Northern ; Cell Nucleolus/*chemistry ; Humans ; *Introns ; Molecular Sequence Data ; Oligonucleotide Probes ; Oocytes/metabolism ; RNA Precursors/*metabolism ; RNA Processing, Post-Transcriptional ; RNA, Nuclear/chemistry/*genetics/*physiology ; RNA, Ribosomal, 18S/*metabolism ; RNA, Small Nuclear/chemistry/*genetics/*physiology ; Xenopus
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 5
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    Catalytic site components common to both splicing steps of a group II intron (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-25
    Description: The splicing of group II introns occurs in two steps involving substrates with different chemical configurations. The question of whether these two steps are catalyzed by a single or two separate active sites is a matter of debate. Here, certain bases and phosphate oxygen atoms at conserved positions in domain V of a group II self-splicing intron are shown to be required for catalysis of both splicing steps. These results show that the active sites catalyzing the two steps must, at least, share common components, ruling out the existence of two completely distinct active sites in group II introns.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chanfreau, G -- Jacquier, A -- New York, N.Y. -- Science. 1994 Nov 25;266(5189):1383-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Unite de Genetique Moleculaire des Levures, URA 1149 du CNRS, Departement de Biologie Moleculaire, Institut Pasteur, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973729" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Catalysis ; Electron Transport Complex IV/genetics ; Electrophoresis, Polyacrylamide Gel ; Exons ; *Introns ; Molecular Sequence Data ; Nucleic Acid Conformation ; *RNA Splicing ; RNA, Fungal/chemistry/*genetics ; Saccharomyces cerevisiae/enzymology/genetics ; Thionucleotides/genetics
    Print ISSN: 0036-8075
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  • 6
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    Increased recruitment of TATA-binding protein to the promoter by transcriptional activation domains in vivo (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-14
    Description: The rate at which the TATA-binding protein (TBP) interacts with the TATA element and promotes transcription by RNA polymerase II was determined in yeast cells. A TBP derivative with altered TATA-element specificity was rapidly induced, and transcription from promoters with appropriately mutated TATA elements was measured. Without a functional activator protein, basal transcription was observed only after a lag of several hours. In contrast, GCN4-activated transcription occurred rapidly upon induction of the TBP derivative. These results suggest that accessibility of TBP to the chromatin template in vivo is rate limiting and that activation domains increase recruitment of TBP to the promoter.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klein, C -- Struhl, K -- GM30186/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 14;266(5183):280-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939664" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Chromatin/metabolism ; Copper/pharmacology ; DNA-Binding Proteins/*metabolism ; Fungal Proteins/metabolism/pharmacology ; Hydro-Lyases/genetics ; Molecular Sequence Data ; Protein Kinases/metabolism/pharmacology ; *Saccharomyces cerevisiae Proteins ; *TATA Box ; TATA-Box Binding Protein ; Templates, Genetic ; Transcription Factors/*metabolism/pharmacology ; *Transcriptional Activation ; Yeasts/genetics
    Print ISSN: 0036-8075
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  • 7
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    DNA loop repair by human cell extracts (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-04
    Description: An activity in human cell extracts is described that repairs DNA with loops of five or more unpaired bases. Repair is strand-specific and is directed by a nick located 5' or 3' to the loop. This repair is observed in a colorectal cancer cell line that is devoid of a wild-type hMLH1 gene and is deficient in repair of mismatches. However, a cell line with deletions in both hMSH2 alleles is deficient in repair of both loops and mismatches. Defects in loop repair may be relevant to the repetitive-sequence instability observed in cancers and other hereditary diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Umar, A -- Boyer, J C -- Kunkel, T A -- New York, N.Y. -- Science. 1994 Nov 4;266(5186):814-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Genetics, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973637" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Base Composition ; Base Sequence ; Carrier Proteins ; Cell Extracts ; Cell Line ; Colorectal Neoplasms/*genetics ; *DNA Repair ; DNA, Satellite/genetics/metabolism ; *DNA-Binding Proteins ; HeLa Cells ; Humans ; Molecular Sequence Data ; MutS Homolog 2 Protein ; Neoplasm Proteins/*genetics/physiology ; Nuclear Proteins ; Nucleic Acid Heteroduplexes/*metabolism ; Proto-Oncogene Proteins/*genetics/physiology ; Repetitive Sequences, Nucleic Acid ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
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  • 8
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    Delocalization of Vg1 mRNA from the vegetal cortex in Xenopus oocytes after destruction of Xlsirt RNA (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-19
    Description: The Xlsirts are a family of transcribed repeat sequence genes that do not code for protein. Xlsirt RNAs become localized to the vegetal cortex of Xenopus oocytes early in oogenesis, before the localization of the messenger RNA Vg1, which encodes a transforming growth factor-beta-like molecule involved in mesoderm formation, and coincident with the localization of Xcat2 transcripts, which encode a nanos-like molecule. Destruction of the localized Xlsirts by injection of antisense oligodeoxynucleotides into stage 4 oocytes resulted in the release of Vg1 transcripts but not Xcat2 transcripts from the vegetal cortex. Xlsirt RNAs, which may be a structural component of the vegetal cortex, are a crucial part of a genetic pathway necessary for the proper localization of Vg1 that leads to subsequent normal pattern formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kloc, M -- Etkin, L D -- New York, N.Y. -- Science. 1994 Aug 19;265(5175):1101-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, University of Texas, M.D. Anderson Cancer Center, Houston 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7520603" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cells, Cultured ; Glycoproteins/*genetics ; Molecular Sequence Data ; Oligonucleotides, Antisense/pharmacology ; Oogenesis ; RNA/*genetics ; RNA, Messenger/genetics/*metabolism ; RNA-Binding Proteins/genetics ; Repetitive Sequences, Nucleic Acid ; Transforming Growth Factor beta/genetics ; Xenopus ; *Xenopus Proteins ; Zinc Fingers
    Print ISSN: 0036-8075
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  • 9
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    Structures of ternary complexes of rat DNA polymerase beta, a DNA template-primer, and ddCTP (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-24
    Description: Two ternary complexes of rat DNA polymerase beta (pol beta), a DNA template-primer, and dideoxycytidine triphosphate (ddCTP) have been determined at 2.9 A and 3.6 A resolution, respectively. ddCTP is the triphosphate of dideoxycytidine (ddC), a nucleoside analog that targets the reverse transcriptase of human immunodeficiency virus (HIV) and is at present used to treat AIDS. Although crystals of the two complexes belong to different space groups, the structures are similar, suggesting that the polymerase-DNA-ddCTP interactions are not affected by crystal packing forces. In the pol beta active site, the attacking 3'-OH of the elongating primer, the ddCTP phosphates, and two Mg2+ ions are all clustered around Asp190, Asp192, and Asp256. Two of these residues, Asp190 and Asp256, are present in the amino acid sequences of all polymerases so far studied and are also spatially similar in the four polymerases--the Klenow fragment of Escherichia coli DNA polymerase I, HIV-1 reverse transcriptase, T7 RNA polymerase, and rat DNA pol beta--whose crystal structures are now known. A two-metal ion mechanism is described for the nucleotidyl transfer reaction and may apply to all polymerases. In the ternary complex structures analyzed, pol beta binds to the DNA template-primer in a different manner from that recently proposed for other polymerase-DNA models.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pelletier, H -- Sawaya, M R -- Kumar, A -- Wilson, S H -- Kraut, J -- CA17374/CA/NCI NIH HHS/ -- ES06839/ES/NIEHS NIH HHS/ -- GM10928/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jun 24;264(5167):1891-903.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, San Diego 92093-0317.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7516580" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; DNA/chemistry/metabolism ; DNA Polymerase I/*chemistry/metabolism ; DNA Primers/*chemistry/metabolism ; DNA-Directed RNA Polymerases/chemistry/metabolism ; Deoxycytosine Nucleotides/*chemistry/metabolism ; Dideoxynucleotides ; HIV Reverse Transcriptase ; Humans ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; RNA-Directed DNA Polymerase/chemistry/metabolism ; Rats ; Recombinant Proteins ; Templates, Genetic ; Thymine Nucleotides/chemistry/metabolism ; Viral Proteins ; Zidovudine/analogs & derivatives/chemistry/metabolism
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  • 10
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    Attenuation of fungal virulence by synthetic infectious hypovirus transcripts (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-17
    Description: Noninfectious, cytoplasmically transmissible viral double-stranded RNAs of the genus Hypovirus cause reduced virulence (hypovirulence) in the chestnut blight fungus Cryphonectria parasitica, providing the basis for virus-mediated biological control of a fungal disease. Synthetic transcripts corresponding to a full-length hypovirus RNA coding strand are infectious when introduced into fungal spheroplasts by electroporation. Hypovirus infections were readily established in Cryphonectria parasitica and in related fungal species not previously reported to harbor viruses. These results demonstrate the use of a synthetic mycovirus transcript to expand fungal host range, thereby broadening the potential application of virus-mediated hypovirulence to control fungal pathogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, B -- Choi, G H -- Nuss, D L -- New York, N.Y. -- Science. 1994 Jun 17;264(5166):1762-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Roche Institute of Molecular Biology, Roche Research Center, Nutley, NJ 07110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8209256" target="_blank"〉PubMed〈/a〉
    Keywords: Ascomycota/genetics/*pathogenicity/physiology ; Base Sequence ; DNA, Complementary/genetics ; Electroporation ; Molecular Sequence Data ; Phenotype ; Plant Diseases ; RNA Viruses/*genetics/physiology ; RNA, Double-Stranded/*genetics ; RNA, Viral/*genetics ; Spheroplasts ; Transfection ; Virulence ; Virus Replication
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  • 11
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    High-specificity DNA cleavage agent: design and application to kilobase and megabase DNA substrates (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-12
    Description: Strategies to cleave double-stranded DNA at specific DNA sites longer than those of restriction endonucleases (longer than 8 base pairs) have applications in chromosome mapping, chromosome cloning, and chromosome sequencing--provided that the strategies yield high DNA-cleavage efficiency and high DNA-cleavage specificity. In this report, the DNA-cleaving moiety copper:o-phenanthroline was attached to the sequence-specific DNA binding protein catabolite activator protein (CAP) at an amino acid that, because of a difference in DNA bending, is close to DNA in the specific CAP-DNA complex but is not close to DNA in the nonspecific CAP-DNA complex. The resulting CAP derivative, OP26CAP, cleaved kilobase and megabase DNA substrates at a 22-base pair consensus DNA site with high efficiency and exhibited no detectable nonspecific DNA-cleavage activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pendergrast, P S -- Ebright, Y W -- Ebright, R H -- GM41376/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Aug 12;265(5174):959-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Rutgers University, New Brunswick, NJ 08855.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8052855" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cyclic AMP Receptor Protein/*chemistry ; DNA/*chemistry/metabolism ; DNA-Binding Proteins/*chemistry ; Molecular Sequence Data ; Molecular Structure ; Nucleic Acid Conformation ; Phenanthrolines/*chemistry
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  • 12
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    Functional consequences of posttranslational isomerization of Ser46 in a calcium channel toxin (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-11
    Description: The venom of the funnel-web spider Agelenopsis aperta contains several peptides that paralyze prey by blocking voltage-sensitive calcium channels. Two peptides, omega-Aga-IVB (IVB) and omega-Aga-IVC (IVC), have identical amino acid sequences, yet have opposite absolute configurations at serine 46. These toxins had similar selectivities for blocking voltage-sensitive calcium channel subtypes but different potencies for blocking P-type voltage-sensitive calcium channels in rat cerebellar Purkinje cells as well as calcium-45 influx into rat brain synaptosomes. An enzyme purified from venom converts IVC to IVB by isomerizing serine 46, which is present in the carboxyl-terminal tail, from the L to the D configuration. Unlike the carboxyl terminus of IVC, that of IVB was resistant to the major venom protease. These results show enzymatic activities in A. aperta venom being used in an unprecedented strategy for coproduction of necessary neurotoxins that possess enhanced stability and potency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heck, S D -- Siok, C J -- Krapcho, K J -- Kelbaugh, P R -- Thadeio, P F -- Welch, M J -- Williams, R D -- Ganong, A H -- Kelly, M E -- Lanzetti, A J -- New York, N.Y. -- Science. 1994 Nov 11;266(5187):1065-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉NPS Pharmaceuticals Incorporated, Salt Lake City, Utah 84108.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973665" target="_blank"〉PubMed〈/a〉
    Keywords: Agatoxins ; Amino Acid Sequence ; Animals ; Base Sequence ; Calcium/metabolism ; Calcium Channel Blockers/chemistry/*metabolism/toxicity ; Calcium Channels/*metabolism ; Isomerases/metabolism ; Molecular Sequence Data ; *Protein Processing, Post-Translational ; Purkinje Cells/metabolism ; Rats ; Serine/*metabolism ; Spider Venoms/chemistry/enzymology/*metabolism/toxicity ; Stereoisomerism ; Structure-Activity Relationship ; Synaptosomes/metabolism
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  • 13
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    Binding of mismatched microsatellite DNA sequences by the human MSH2 protein (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-25
    Description: Alteration of the human mismatch repair gene hMSH2 has been linked to the microsatellite DNA instability found in hereditary nonpolyposis colon cancer and several sporadic cancers. This microsatellite DNA instability is thought to arise from defective repair of DNA replication errors that create insertion-deletion loop-type (IDL) mismatched nucleotides. Here, it is shown that purified hMSH2 protein efficiently and specifically binds DNA containing IDL mismatches of up to 14 nucleotides. These results support a direct role for hMSH2 in mutation avoidance and microsatellite stability in human cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fishel, R -- Ewel, A -- Lee, S -- Lescoe, M K -- Griffith, J -- CA56542/CA/NCI NIH HHS/ -- GM31819/GM/NIGMS NIH HHS/ -- GM42342/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Nov 25;266(5189):1403-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Markey Center for Molecular Genetics, University of Vermont School of Medicine, Burlington 05405.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973733" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; DNA Repair ; DNA, Satellite/*metabolism ; *DNA-Binding Proteins ; Humans ; Molecular Sequence Data ; MutS Homolog 2 Protein ; Nucleic Acid Conformation ; Nucleic Acid Heteroduplexes/metabolism ; Oligodeoxyribonucleotides/metabolism ; Proto-Oncogene Proteins/*metabolism
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  • 14
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    Engineering poliovirus as a vaccine vector for the expression of diverse antigens (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-02
    Description: As a step toward developing poliovirus as a vaccine vector, poliovirus recombinants were constructed by fusing exogenous peptides (up to 400 amino acids) and an artificial cleavage site for viral protease 3Cpro to the amino terminus of the viral polyprotein. Viral replication proceeded normally. An extended polyprotein was produced in infected cells and proteolytically processed into the complete array of viral proteins plus the foreign peptide, which was excluded from mature virions. The recombinants retained exogenous sequences through successive rounds of replication in culture and in vivo. Infection of animals with recombinants elicited a humoral immune response to the foreign peptides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Andino, R -- Silvera, D -- Suggett, S D -- Achacoso, P L -- Miller, C J -- Baltimore, D -- Feinberg, M B -- AI22346/AI/NIAID NIH HHS/ -- AI35545/AI/NIAID NIH HHS/ -- RR00169/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1994 Sep 2;265(5177):1448-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of California, San Francisco.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8073288" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Bacterial/biosynthesis ; Antibodies, Viral/biosynthesis ; Antigens, Bacterial/genetics/immunology ; Antigens, Viral/genetics/immunology ; Base Sequence ; Cloning, Molecular ; *Genetic Engineering ; Genetic Vectors ; HeLa Cells ; Humans ; Macaca fascicularis ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; Poliovirus/*genetics/immunology/physiology ; Poliovirus Vaccine, Oral/*genetics ; *Protein Biosynthesis ; Proteins/metabolism ; Recombinant Proteins/biosynthesis/metabolism ; Vaccines, Synthetic/genetics/*immunology ; Virus Replication
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 15
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    Hints of a language in junk DNA (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flam, F -- New York, N.Y. -- Science. 1994 Nov 25;266(5189):1320.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973718" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/chemistry/*genetics ; DNA, Fungal/chemistry/genetics ; Genetic Code ; Statistics as Topic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 16
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    Drosophila TAFII150: similarity to yeast gene TSM-1 and specific binding to core promoter DNA (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-05-13
    Description: In Drosophila and human cells, the TATA binding protein (TBP) of the transcription factor IID (TFIID) complex is tightly associated with multiple subunits termed TBP-associated factors (TAFs) that are essential for mediating regulation of RNA polymerase II transcription. The Drosophila TAFII150 has now been molecularly cloned and biochemically characterized. The deduced primary amino acid sequence of dTAFII150 reveals a striking similarity to the essential yeast gene, TSM-1. Furthermore, like dTAFII150, the TSM-1 protein is found associated with the TBP in vivo, thus identifying the first yeast homolog of a TAF associated with TFIID. Both the product of TSM-1 and dTAFII150 bind directly to TBP and dTAFII250, demonstrating a functional similarity between human and yeast TAFs. Surprisingly, DNA binding studies indicate that purified recombinant dTAFII150 binds specifically to DNA sequences overlapping the start site of transcription. The data demonstrate that at least one of the TAFs is a sequence-specific DNA binding protein and that dTAFII150 together with TBP are responsible for TFIID interactions with an extended region of the core promoter.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Verrijzer, C P -- Yokomori, K -- Chen, J L -- Tjian, R -- New York, N.Y. -- Science. 1994 May 13;264(5161):933-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, Berkeley 94720-3202.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8178153" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; DNA/*metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Drosophila ; *Drosophila Proteins ; Genes, Fungal ; Genes, Insect ; Histone Acetyltransferases ; Humans ; Molecular Sequence Data ; Nuclear Proteins/metabolism ; *Promoter Regions, Genetic ; RNA Polymerase II/metabolism ; Recombinant Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; *Saccharomyces cerevisiae Proteins ; Sequence Alignment ; TATA Box ; *TATA-Binding Protein Associated Factors ; TATA-Box Binding Protein ; Transcription Factor TFIID ; Transcription Factors/chemistry/genetics/*metabolism
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  • 17
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    Identification of herpesvirus-like DNA sequences in AIDS-associated Kaposi's sarcoma (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-16
    Description: Representational difference analysis was used to isolate unique sequences present in more than 90 percent of Kaposi's sarcoma (KS) tissues obtained from patients with acquired immunodeficiency syndrome (AIDS). These sequences were not present in tissue DNA from non-AIDS patients, but were present in 15 percent of non-KS tissue DNA samples from AIDS patients. The sequences are homologous to, but distinct from, capsid and tegument protein genes of the Gammaherpesvirinae, herpesvirus saimiri and Epstein-Barr virus. These KS-associated herpesvirus-like (KSHV) sequences appear to define a new human herpesvirus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, Y -- Cesarman, E -- Pessin, M S -- Lee, F -- Culpepper, J -- Knowles, D M -- Moore, P S -- New York, N.Y. -- Science. 1994 Dec 16;266(5192):1865-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, College of Physicians and Surgeons, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7997879" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*complications ; Amino Acid Sequence ; Base Composition ; Base Sequence ; Blotting, Southern ; Cloning, Molecular ; DNA, Viral/*analysis/chemistry/genetics ; Female ; Herpesviridae/*genetics ; Herpesvirus 2, Saimiriine/genetics ; Herpesvirus 4, Human/genetics ; Humans ; Male ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Open Reading Frames ; Polymerase Chain Reaction ; Retrospective Studies ; Sarcoma, Kaposi/etiology/*virology ; Sequence Homology, Amino Acid
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  • 18
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    Induction of mesoderm in Xenopus laevis embryos by translation initiation factor 4E (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-05
    Description: The microinjection of messenger RNA encoding the eukaryotic translation initiation factor 4E (eIF-4E) into early embryos of Xenopus laevis leads to the induction of mesoderm in ectodermal explants. This induction occurs without a stimulation of overall protein synthesis and is blocked by the co-expression of a dominant negative mutant of the proto-oncogene ras or a truncated activin type II receptor. Although other translation factors have been studied in vertebrate and invertebrate embryos, none have been shown to play a direct role in development. The results here suggest a mechanism for relaying and amplifying signals for mesoderm induction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klein, P S -- Melton, D A -- New York, N.Y. -- Science. 1994 Aug 5;265(5173):803-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8047887" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Eukaryotic Initiation Factor-1/physiology ; Eukaryotic Initiation Factor-4E ; Gene Expression Regulation/physiology ; Mesoderm/metabolism/*physiology ; Molecular Sequence Data ; Peptide Initiation Factors/genetics/*physiology ; RNA, Messenger ; Xenopus laevis/*embryology
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  • 19
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    Cooperative display and relatedness among males in a lek-mating bird (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-11-11
    Description: Long-tailed manakins mate in leks and cooperate in multiyear male-male partnerships. An alpha male is responsible for virtually all mating, whereas a beta male assists in the courtship displays. Such altruism by the beta male poses a problem for evolutionary theory because most theoretical treatments and empirical examples of cooperative behavior involve kin selection or reciprocity. Here it is shown that alpha and beta partners are not relatives and that reciprocity is not involved. Instead, direct, though long-delayed benefits to beta males are demonstrated, which include rare copulations, ascension to alpha status, and female lek fidelity. These benefits maintain this unusual form of male-male cooperation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McDonald, D B -- Potts, W K -- New York, N.Y. -- Science. 1994 Nov 11;266(5187):1030-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Archbold Biological Station, Lake Placid, FL 33852-2057.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973654" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Base Sequence ; Birds/genetics/*physiology ; *Cooperative Behavior ; Copulation ; Female ; Heterozygote ; Male ; Molecular Sequence Data ; Polymerase Chain Reaction ; *Sexual Behavior, Animal
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  • 20
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    Receptor and ligand domains for invasion of erythrocytes by Plasmodium falciparum (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-24
    Description: A 175-kilodalton erythrocyte binding protein, EBA-175, of the parasite Plasmodium falciparum mediates the invasion of erythrocytes. The erythrocyte receptor for EBA-175 is dependent on sialic acid. The domain of EBA-175 that binds erythrocytes was identified as region II with the use of truncated portions of EBA-175 expressed on COS cells. Region II, which contains a cysteine-rich motif, and native EBA-175 bind specifically to glycophorin A, but not to glycophorin B, on the erythrocyte membrane. Erythrocyte recognition of EBA-175 requires both sialic acid and the peptide backbone of glycophorin A. The identification of both the receptor and ligand domains may suggest rational designs for receptor blockade and vaccines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sim, B K -- Chitnis, C E -- Wasniowska, K -- Hadley, T J -- Miller, L H -- New York, N.Y. -- Science. 1994 Jun 24;264(5167):1941-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Malaria Research, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8009226" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigens, Protozoan ; Base Sequence ; Binding Sites ; Carrier Proteins/genetics/*metabolism ; Cell Line ; Erythrocytes/metabolism/*parasitology ; Glycopeptides/chemistry/metabolism ; Glycophorin/chemistry/*metabolism ; Molecular Sequence Data ; Plasmodium falciparum/*metabolism ; Protozoan Proteins/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Sialic Acids/*metabolism
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  • 21
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    Protection from Fas-mediated apoptosis by a soluble form of the Fas molecule (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-03-25
    Description: Fas is an apoptosis-signaling receptor molecule on the surface of a number of cell types. Molecular cloning and nucleotide sequence analysis revealed a human Fas messenger RNA variant capable of encoding a soluble Fas molecule lacking the transmembrane domain because of the deletion of an exon encoding this region. The expression of soluble Fas was confirmed by flow cytometry and immunocytochemical analysis. Supernatants from cells transfected with the variant messenger RNA blocked apoptosis induced by the antibody to Fas. Levels of soluble Fas were elevated in patients with systemic lupus erythematosus, and mice injected with soluble Fas displayed autoimmune features.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cheng, J -- Zhou, T -- Liu, C -- Shapiro, J P -- Brauer, M J -- Kiefer, M C -- Barr, P J -- Mountz, J D -- P01 AR03555/AR/NIAMS NIH HHS/ -- P50 AI23694/AI/NIAID NIH HHS/ -- P60 AR20614/AR/NIAMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Mar 25;263(5154):1759-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Alabama at Birmingham.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7510905" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies/immunology ; Antigens, CD95 ; Antigens, Surface/chemistry/genetics/immunology/*physiology ; *Apoptosis ; Arthritis, Rheumatoid/blood ; Base Sequence ; Cell Line ; Cell Membrane/chemistry ; Humans ; Lupus Erythematosus, Systemic/blood ; Mice ; Molecular Sequence Data ; RNA, Messenger/genetics ; Solubility ; T-Lymphocyte Subsets/immunology ; Transfection
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  • 22
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    Determination of intrinsic transcription termination efficiency by RNA polymerase elongation rate (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-04
    Description: Transcription terminators recognized by several RNA polymerases include a DNA segment encoding uridine-rich RNA and, for bacterial RNA polymerase, a hairpin loop located immediately upstream. Here, mutationally altered Escherichia coli RNA polymerase enzymes that have different termination efficiencies were used to show that the extent of transcription through the uridine-rich encoding segment is controlled by the substrate concentration of nucleoside triphosphate. This result implies that the rate of elongation determines the probability of transcript release. Moreover, the position of release sites suggests an important spatial relation between the RNA hairpin and the boundary of the terminator.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McDowell, J C -- Roberts, J W -- Jin, D J -- Gross, C -- New York, N.Y. -- Science. 1994 Nov 4;266(5186):822-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY 14853.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7526463" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA-Directed RNA Polymerases/genetics/*metabolism ; Escherichia coli/enzymology/genetics ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Nucleotides/metabolism ; RNA, Bacterial/*genetics/metabolism ; *Terminator Regions, Genetic ; *Transcription, Genetic ; Uridine Triphosphate/metabolism
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  • 23
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    Molecular evidence that the myxozoan protists are metazoans (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-09-16
    Description: The evolutionary origins of the protistan phylum, Myxozoa, have long been questioned. Although these obligate parasites are like protozoans in many features, several aspects of their ontogeny and morphology have implied a closer relationship to metazoan lineages. Phylogenetic analyses of 18S ribosomal RNA sequences from myxozoans and other eukaryotes, with the use of parsimony, distance, and maximum-likelihood methods, support the hypothesis that myxozoans are closely related to the bilateral animals. These results suggest that the Myxozoa, long considered an assemblage of protozoans, should be considered a metazoan phylum.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smothers, J F -- von Dohlen, C D -- Smith, L H Jr -- Spall, R D -- New York, N.Y. -- Science. 1994 Sep 16;265(5179):1719-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Idaho State University, Pocatello 83209.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8085160" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Biological Evolution ; Eukaryota/*classification/genetics ; Likelihood Functions ; Molecular Sequence Data ; Parasites/*classification/genetics ; Phylogeny ; Probability ; RNA, Protozoan/genetics ; RNA, Ribosomal, 18S/*genetics
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  • 24
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    Formation of nascent intercalated disks between grafted fetal cardiomyocytes and host myocardium (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-01
    Description: Fetal cardiomyocytes isolated from transgenic mice carrying a fusion gene of the alpha-cardiac myosin heavy chain promoter with a beta-galactosidase reporter were examined for their ability to form stable intracardiac grafts. Embryonic day 15 transgenic cardiomyocytes delivered directly into the myocardium of syngeneic hosts formed stable grafts, as identified by nuclear beta-galactosidase activity. Grafted cardiomyocytes were observed as long as 2 months after implantation, the latest date assayed. Intracardiac graft formation did not induce overtly negative effects on the host myocardium and was not associated with chronic immune rejection. Electron microscopy revealed the presence of nascent intercalated disks connecting the engrafted fetal cardiomyocytes and the host myocardium. These results suggest that intracardiac grafting might provide a useful approach for myocardial repair, provided that the grafted cells can contribute to myocardial function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Soonpaa, M H -- Koh, G Y -- Klug, M G -- Field, L J -- HL45453/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1994 Apr 1;264(5155):98-101.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Krannert Institute of Cardiology, Indiana University School of Medicine, Indianapolis 46202-4800.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8140423" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Communication ; Cell Differentiation ; Cell Nucleus/metabolism ; *Cell Transplantation ; DNA/biosynthesis ; DNA Primers ; Electrocardiography ; Fetal Heart/*cytology ; *Fetal Tissue Transplantation ; Gap Junctions/physiology/ultrastructure ; Genetic Markers ; Heart/physiology ; Intercellular Junctions/physiology/*ultrastructure ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; Myocardium/*cytology/ultrastructure ; beta-Galactosidase/analysis
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  • 25
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    Expanding the scope of RNA catalysis (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-06-24
    Description: The basic notions of transition state theory have been exploited in the past to generate highly selective catalysts from the vast library of antibody molecules in the immune system. These same ideas were used to isolate an RNA molecule, from a large library of RNAs, that catalyzes the isomerization of a bridged biphenyl. The RNA-catalyzed reaction displays Michaelis-Menten kinetics with a catalytic rate constant (kcat) of 2.8 x 10(-5) per minute and a Michaelis constant (Km) of 542 microM; the reaction is competitively inhibited by the planar transition state analog with an inhibition constant (Ki) value of approximately 7 microM. This approach may provide a general strategy for expanding the scope of RNA catalysis beyond those reactions in which the substrates are nucleic acids or nucleic acid derivatives.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Prudent, J R -- Uno, T -- Schultz, P G -- GM08352A/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jun 24;264(5167):1924-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8009223" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Biphenyl Compounds/chemistry/metabolism ; Catalysis ; Kinetics ; Molecular Sequence Data ; Nucleic Acid Conformation ; Nucleic Acid Denaturation ; Polymerase Chain Reaction ; RNA, Catalytic/chemistry/*metabolism ; Stereoisomerism ; Temperature
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  • 26
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    Potential role of human cytomegalovirus and p53 interaction in coronary restenosis (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-15
    Description: A subset of patients who have undergone coronary angioplasty develop restenosis, a vessel renarrowing characterized by excessive proliferation of smooth muscle cells (SMCs). Of 60 human restenosis lesions examined, 23 (38 percent) were found to have accumulated high amounts of the tumor suppressor protein p53, and this correlated with the presence of human cytomegalovirus (HCMV) in the lesions. SMCs grown from the lesions expressed HCMV protein IE84 and high amounts of p53. HCMV infection of cultured SMCs enhanced p53 accumulation, which correlated temporally with IE84 expression. IE84 also bound to p53 and abolished its ability to transcriptionally activate a reporter gene. Thus, HCMV, and IE84-mediated inhibition of p53 function, may contribute to the development of restenosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Speir, E -- Modali, R -- Huang, E S -- Leon, M B -- Shawl, F -- Finkel, T -- Epstein, S E -- New York, N.Y. -- Science. 1994 Jul 15;265(5170):391-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cardiology Branch, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8023160" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Aged ; Aged, 80 and over ; *Angioplasty, Balloon ; Antigens, Viral/*metabolism ; Atherectomy, Coronary ; Base Sequence ; Cells, Cultured ; Coronary Disease/*etiology/pathology/therapy ; Coronary Vessels/cytology/metabolism/microbiology ; Cytomegalovirus/*physiology ; Genes, p53 ; Humans ; Immediate-Early Proteins/*metabolism ; Middle Aged ; Molecular Sequence Data ; Muscle, Smooth, Vascular/cytology/metabolism/microbiology ; Recurrence ; Transcriptional Activation ; Transfection ; Tumor Suppressor Protein p53/genetics/*metabolism
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  • 27
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    Specific cleavage of model recombination and repair intermediates by the yeast Rad1-Rad10 DNA endonuclease (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-30
    Description: The RAD1 and RAD10 genes of Saccharomyces cerevisiae are required for both nucleotide excision repair and certain mitotic recombination events. Here, model recombination and repair intermediates were used to show that Rad1-Rad10-mediated cleavage occurs at duplex-single-strand junctions. Moreover, cleavage occurs only on the strand containing the 3' single-stranded tail. Thus, both biochemical and genetic evidence indicate a role for the Rad1-Rad10 complex in the cleavage of specific recombination intermediates. Furthermore, these data suggest that Rad1-Rad10 endonuclease incises DNA 5' to damaged bases during nucleotide excision repair.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bardwell, A J -- Bardwell, L -- Tomkinson, A E -- Friedberg, E C -- CA12428/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Sep 30;265(5181):2082-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Pathology, University of Texas Southwestern Medical Center at Dallas 75235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8091230" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *DNA Repair ; DNA Repair Enzymes ; DNA, Fungal/genetics/*metabolism ; DNA, Single-Stranded/metabolism ; *DNA-Binding Proteins ; Endodeoxyribonucleases/*metabolism ; *Endonucleases ; Fungal Proteins/*metabolism ; Molecular Sequence Data ; Oligodeoxyribonucleotides/metabolism ; *Recombination, Genetic ; Saccharomyces cerevisiae/*genetics/metabolism ; *Saccharomyces cerevisiae Proteins ; Single-Strand Specific DNA and RNA Endonucleases
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    Genetic control of programmed cell death in Drosophila (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-29
    Description: A gene, reaper (rpr), that appears to play a central control function for the initiation of programmed cell death (apoptosis) in Drosophila was identified. Virtually all programmed cell death that normally occurs during Drosophila embryogenesis was blocked in embryos homozygous for a small deletion that includes the reaper gene. Mutant embryos contained many extra cells and failed to hatch, but many other aspects of development appeared quite normal. Deletions that include reaper also protected embryos from apoptosis caused by x-irradiation and developmental defects. However, high doses of x-rays induced some apoptosis in mutant embryos, and the resulting corpses were phagocytosed by macrophages. These data suggest that the basic cell death program is intact although it was not activated in mutant embryos. The DNA encompassed by the deletion was cloned and the reaper gene was identified on the basis of the ability of cloned DNA to restore apoptosis to cell death defective embryos in germ line transformation experiments. The reaper gene appears to encode a small peptide that shows no homology to known proteins, and reaper messenger RNA is expressed in cells destined to undergo apoptosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉White, K -- Grether, M E -- Abrams, J M -- Young, L -- Farrell, K -- Steller, H -- 5 F32 NS08536/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1994 Apr 29;264(5159):677-83.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Brain and Cognitive Sciences, Cambridge, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8171319" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Apoptosis/*genetics ; Base Sequence ; Cloning, Molecular ; DNA Primers ; Drosophila/cytology/embryology/*genetics ; *Drosophila Proteins ; Embryo, Nonmammalian/cytology ; *Genes, Insect ; Models, Genetic ; Molecular Sequence Data ; Mutation ; Nervous System/cytology ; Neurons/cytology ; Peptides/chemistry/*genetics/physiology
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    Differential regulation of RNA polymerases I, II, and III by the TBP-binding repressor Dr1 (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-21
    Description: RNA polymerases I, II, and III each use the TATA-binding protein (TBP). Regulators that target this shared factor may therefore provide a means to coordinate the activities of the three nuclear RNA polymerases. The repressor Dr1 binds to TBP and blocks the interaction of TBP with polymerase II- and polymerase III-specific factors. This enables Dr1 to coordinately regulate transcription by RNA polymerases II and III. Under the same conditions, Dr1 does not inhibit polymerase I transcription. By selectively repressing polymerases II and III, Dr1 may shift the physiological balance of transcriptional output in favor of polymerase I.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉White, R J -- Khoo, B C -- Inostroza, J A -- Reinberg, D -- Jackson, S P -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1994 Oct 21;266(5184):448-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome/CRC Institute, University of Cambridge, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939686" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA-Binding Proteins/metabolism ; HeLa Cells ; Humans ; Molecular Sequence Data ; Phosphoproteins/metabolism/*pharmacology ; RNA Polymerase I/*metabolism ; RNA Polymerase II/*metabolism ; RNA Polymerase III/*metabolism ; Saccharomyces cerevisiae Proteins ; TATA Box ; TATA-Binding Protein Associated Factors ; TATA-Box Binding Protein ; Transcription Factor TFIIB ; Transcription Factor TFIIIB ; Transcription Factors/metabolism/*pharmacology ; *Transcription Factors, TFIII ; Transcription, Genetic/*drug effects
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    [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-22
    Description: A cytoplasmically inherited element, [URE3], allows yeast to use ureidosuccinate in the presence of ammonium ion. Chromosomal mutations in the URE2 gene produce the same phenotype. [URE3] depends for its propagation on the URE2 product (Ure2p), a negative regulator of enzymes of nitrogen metabolism. Saccharomyces cerevisiae strains cured of [URE3] with guanidium chloride were shown to return to the [URE3]-carrying state without its introduction from other cells. Overproduction of Ure2p increased the frequency with which a strain became [URE3] by 100-fold. In analogy to mammalian prions, [URE3] may be an altered form of Ure2p that is inactive for its normal function but can convert normal Ure2p to the altered form. The genetic evidence presented here suggests that protein-based inheritance, involving a protein unrelated to the mammalian prion protein, can occur in a microorganism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wickner, R B -- New York, N.Y. -- Science. 1994 Apr 22;264(5158):566-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section on Genetics of Simple Eukaryotes, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7909170" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartic Acid/analogs & derivatives/metabolism ; Base Sequence ; Crosses, Genetic ; Fungal Proteins/chemistry/*genetics/metabolism ; Genes, Dominant ; Genes, Fungal ; Genes, Recessive ; Glutathione Peroxidase ; Guanidine ; Guanidines/pharmacology ; Molecular Sequence Data ; Mutation ; Phenotype ; Plasmids ; PrPSc Proteins ; Prions/chemistry/genetics/metabolism ; Saccharomyces cerevisiae/*genetics/metabolism ; *Saccharomyces cerevisiae Proteins
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    BRCA1 mutations in primary breast and ovarian carcinomas (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-10-07
    Description: Loss of heterozygosity data from familial tumors suggest that BRCA1, a gene that confers susceptibility to ovarian and early-onset breast cancer, encodes a tumor suppressor. The BRCA1 region is also subject to allelic loss in sporadic breast and ovarian cancers, an indication that BRCA1 mutations may occur somatically in these tumors. The BRCA1 coding region was examined for mutations in primary breast and ovarian tumors that show allele loss at the BRCA1 locus. Mutations were detected in 3 of 32 breast and 1 of 12 ovarian carcinomas; all four mutations were germline alterations and occurred in early-onset cancers. These results suggest that mutation of BRCA1 may not be critical in the development of the majority of breast and ovarian cancers that arise in the absence of a mutant germline allele.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Futreal, P A -- Liu, Q -- Shattuck-Eidens, D -- Cochran, C -- Harshman, K -- Tavtigian, S -- Bennett, L M -- Haugen-Strano, A -- Swensen, J -- Miki, Y -- CA48711/CA/NCI NIH HHS/ -- CA55914/CA/NCI NIH HHS/ -- CA56749/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Oct 7;266(5182):120-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Carcinogenesis, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939630" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Age of Onset ; Alleles ; BRCA1 Protein ; Base Sequence ; Breast Neoplasms/*genetics ; Chromosomes, Human, Pair 17 ; Female ; *Genes, Tumor Suppressor ; Genetic Predisposition to Disease ; *Germ-Line Mutation ; Heterozygote ; Humans ; Middle Aged ; Molecular Sequence Data ; Neoplasm Proteins/*genetics ; Ovarian Neoplasms/*genetics ; Transcription Factors/*genetics
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    Targeting of G alpha i2 to the Golgi by alternative spliced carboxyl-terminal region (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-01-07
    Description: Heterotrimeric guanosine triphosphate (GTP)-binding proteins (G proteins) may participate in membrane traffic events. A complementary DNA (cDNA) was isolated from a mouse pituitary cDNA library that corresponded to an alternatively spliced form of the gene encoding the G protein alpha subunit G alpha i2. The cDNA was identical to that encoding G alpha i2 except that the region encoding for the carboxyl-terminal 24 amino acids was replaced by a longer region encoding 35 amino acids that have no sequence similarity with G alpha i2 or other members of the G protein family. This alternative spliced product and the corresponding protein (sGi2) were present in several tissues. Specific antibodies revealed that sGi2 was localized in the Golgi apparatus, suggesting a role in membrane transport. Thus, alternative splicing may generate from a single gene two G protein alpha subunits with differential cellular localization and function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Montmayeur, J P -- Borrelli, E -- New York, N.Y. -- Science. 1994 Jan 7;263(5143):95-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Genetique Moleculaire des Eucaryotes, CNRS, INSERM U184, Faculte de Medecine, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8272874" target="_blank"〉PubMed〈/a〉
    Keywords: *Alternative Splicing ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cell Membrane/metabolism ; Coatomer Protein ; DNA, Complementary/genetics ; GTP-Binding Protein alpha Subunit, Gi2 ; *GTP-Binding Protein alpha Subunits, Gi-Go ; GTP-Binding Proteins/analysis/chemistry/genetics/*metabolism ; Golgi Apparatus/chemistry/*metabolism ; Mice ; Microtubule-Associated Proteins/analysis ; Molecular Sequence Data ; Oncogene Proteins/analysis/chemistry/genetics/*metabolism ; *Proto-Oncogene Proteins
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    RNAs with dual specificity and dual RNAs with similar specificity (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-05-20
    Description: The biological role of RNA is delimited by its possible reactions, which can be explored by selection. A comparison of selected RNAs that bind one ligand with those that bind two related ligands suggests that a single nucleotide substitution can expand binding specificity. An RNA site with dual (joint) specificity has adenine and cytosine bases whose pKa's appear shifted upward, thereby mimicking an efficient general acid-base catalyst. The joint site also contains two conserved, looped arginine-coding triplets implicated in arginine site formation. Two selected joint RNAs are identical in some regions and distinct in others. The distinct regions, like some peptides, seem to function similarly without being similar in primary structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Connell, G J -- Yarus, M -- New York, N.Y. -- Science. 1994 May 20;264(5162):1137-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder 80309-0347.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7513905" target="_blank"〉PubMed〈/a〉
    Keywords: Arginine/*metabolism ; Base Sequence ; Binding Sites ; Chromatography, Affinity ; Consensus Sequence ; Guanosine/*metabolism ; Hydrogen-Ion Concentration ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA/chemistry/*metabolism ; RNA, Catalytic/chemistry/metabolism
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    DNA sequence from Cretaceous period bone fragments (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-18
    Description: DNA was extracted from 80-million-year-old bone fragments found in strata of the Upper Cretaceous Blackhawk Formation in the roof of an underground coal mine in eastern Utah. This DNA was used as the template in a polymerase chain reaction that amplified and sequenced a portion of the gene encoding mitochondrial cytochrome b. These sequences differ from all other cytochrome b sequences investigated, including those in the GenBank and European Molecular Biology Laboratory databases. DNA isolated from these bone fragments and the resulting gene sequences demonstrate that small fragments of DNA may survive in bone for millions of years.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Woodward, S R -- Weyand, N J -- Bunnell, M -- New York, N.Y. -- Science. 1994 Nov 18;266(5188):1229-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Brigham Young University, Provo, UT 84602.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973705" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Bone and Bones/*chemistry ; Consensus Sequence ; Cytochrome b Group/*genetics ; DNA, Mitochondrial/chemistry/*genetics/isolation & purification ; Databases, Factual ; History, Ancient ; Molecular Sequence Data ; *Paleontology ; Polymerase Chain Reaction ; Sequence Analysis, DNA ; Sequence Homology, Nucleic Acid ; Utah
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    The Drosophila saxophone gene: a serine-threonine kinase receptor of the TGF-beta superfamily (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-03-25
    Description: The Drosophila decapentaplegic (dpp) gene encodes a transforming growth factor-beta (TGF-beta)-like protein that plays a key role in several aspects of development. Transduction of the DPP signal was investigated by cloning of serine-threonine kinase transmembrane receptors from Drosophila because this type of receptor is specific for the TGF-beta-like ligands. Here evidence is provided demonstrating that the Drosophila saxophone (sax) gene, a previously identified female sterile locus, encodes a TGF-beta-like type I receptor. Embryos from sax mothers and dpp embryos exhibit similar mutant phenotypes during early gastrulation, and these two loci exhibit genetic interactions, which suggest that they are utilized in the same pathway. These data suggest that sax encodes a receptor for dpp.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xie, T -- Finelli, A L -- Padgett, R W -- New York, N.Y. -- Science. 1994 Mar 25;263(5154):1756-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Waksman Institute, Rutgers University, Piscataway, NJ 08855-0759.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8134837" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; Drosophila/embryology/*genetics/metabolism ; *Drosophila Proteins ; Embryo, Nonmammalian/metabolism ; Female ; *Genes, Insect ; Insect Hormones/genetics/*metabolism ; Male ; Molecular Sequence Data ; Mutation ; Protein-Serine-Threonine Kinases/chemistry/*genetics/metabolism ; Receptors, Transforming Growth Factor beta/chemistry/*genetics/metabolism ; Signal Transduction ; Transforming Growth Factor beta/genetics/*metabolism
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    Coding of hemolysins within the ribosomal RNA repeat on a plasmid in Entamoeba histolytica (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-03-11
    Description: The pathogenesis of amoebic dysentery is a result of cytolysis of the colonic mucosa by the parasitic protozoan Entamoeba histolytica. The cytolysis results in extensive local ulceration and allows the amoeba to penetrate and metastasize to distant sites. Factors involved in this process were defined with three clones that express hemolytic activities in Escherichia coli. These potential amoebic virulence determinants were also toxic to human colonic epithelial cells, the primary cellular targets in amoebal invasion of the large intestine. The coding sequences for the hemolysins were close to each other on a 2.6-kilobase segment of a 25-kilobase extrachromosomal DNA element. The structural genes for the hemolysins were within inverted repeats that encode ribosomal RNAs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jansson, A -- Gillin, F -- Kagardt, U -- Hagblom, P -- New York, N.Y. -- Science. 1994 Mar 11;263(5152):1440-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Uppsala University, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8128227" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Survival/drug effects ; Cloning, Molecular ; Entamoeba histolytica/*genetics/pathogenicity ; Escherichia coli/genetics ; *Genes, Protozoan ; Hemolysin Proteins/*genetics/toxicity ; Molecular Sequence Data ; Open Reading Frames ; *Plasmids ; RNA, Protozoan/genetics ; RNA, Ribosomal/*genetics ; Repetitive Sequences, Nucleic Acid ; Tumor Cells, Cultured ; Virulence
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    Transcriptional activation modulated by homopolymeric glutamine and proline stretches (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-02-11
    Description: Many transcription factors contain proline- or glutamine-rich activation domains. Here it is shown that simple homopolymeric stretches of these amino acids can activate transcription when fused to the DNA binding domain of GAL4 factor. In vitro, activity increased with polymer length, whereas in cell transfection assays maximal activity was achieved by 10 to 30 glutamines or about 10 prolines. Similar results were obtained when glutamine stretches were placed within a [GAL4]-VP16 chimeric protein. Because these stretches are encoded by rapidly evolving triplet repeats (microsatellites), they may be the main cause for modulation of transcription factor activity and thus result in subtle or overt genomic effects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gerber, H P -- Seipel, K -- Georgiev, O -- Hofferer, M -- Hug, M -- Rusconi, S -- Schaffner, W -- New York, N.Y. -- Science. 1994 Feb 11;263(5148):808-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Molekularbiologie II der Universitat Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8303297" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Glutamine/*chemistry/pharmacology ; HeLa Cells ; Humans ; Molecular Sequence Data ; Peptides/*chemistry/pharmacology ; Recombinant Fusion Proteins/pharmacology ; Repetitive Sequences, Nucleic Acid ; Transcription Factors/*chemistry/pharmacology ; *Transcriptional Activation ; Transfection
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  • 38
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    Specification of C/EBP function during Drosophila development by the bZIP basic region (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-16
    Description: The biologically relevant interactions of a transcription factor are those that are important for function in the organism. Here, a transgenic rescue assay was used to determine which molecular functions of Drosophila CCAAT/enhancer binding protein (C/EBP), a basic region-leucine zipper transcription factor, are required for it to fulfill its essential role during development. Chimeric proteins that contain the Drosophila C/EBP (DmC/EBP) basic region, a heterologous zipper, and a heterologous activation domain could functionally substitute for DmC/EBP. Mammalian C/EBPs were also functional in Drosophila. In contrast, 9 of 25 single amino acid substitutions in the basic region disrupted biological function. Thus, the conserved basic region specifies DmC/EBP activity in the organism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rorth, P -- New York, N.Y. -- Science. 1994 Dec 16;266(5192):1878-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Embryology, Carnegie Institution of Washington, Baltimore, MD 21210.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7997882" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Base Sequence ; Basic-Leucine Zipper Transcription Factors ; CCAAT-Enhancer-Binding Proteins ; DNA/metabolism ; DNA-Binding Proteins/chemistry/genetics/*physiology ; Drosophila/genetics/*growth & development ; Female ; G-Box Binding Factors ; *Leucine Zippers ; Male ; Molecular Sequence Data ; Nuclear Proteins/chemistry/genetics/*physiology ; Recombinant Fusion Proteins ; Transcription Factors/chemistry/genetics/*physiology ; Transcriptional Activation
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    Fusion of a kinase gene, ALK, to a nucleolar protein gene, NPM, in non-Hodgkin's lymphoma (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-03-04
    Description: The 2;5 chromosomal translocation occurs in most anaplastic large-cell non-Hodgkin's lymphomas arising from activated T lymphocytes. This rearrangement was shown to fuse the NPM nucleolar phosphoprotein gene on chromosome 5q35 to a previously unidentified protein tyrosine kinase gene, ALK, on chromosome 2p23. In the predicted hybrid protein, the amino terminus of nucleophosmin (NPM) is linked to the catalytic domain of anaplastic lymphoma kinase (ALK). Expressed in the small intestine, testis, and brain but not in normal lymphoid cells, ALK shows greatest sequence similarity to the insulin receptor subfamily of kinases. Unscheduled expression of the truncated ALK may contribute to malignant transformation in these lymphomas.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morris, S W -- Kirstein, M N -- Valentine, M B -- Dittmer, K G -- Shapiro, D N -- Saltman, D L -- Look, A T -- CA 21765/CA/NCI NIH HHS/ -- KO8 CA 01702/CA/NCI NIH HHS/ -- P01 CA 20180/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Mar 4;263(5151):1281-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Experimental Oncology, St. Jude Children's Research Hospital, Memphis, TN 38105.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8122112" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Brain/enzymology ; Cell Transformation, Neoplastic ; Chromosome Walking ; Chromosomes, Human, Pair 2 ; Chromosomes, Human, Pair 5 ; Cloning, Molecular ; Gene Expression Regulation, Neoplastic ; Humans ; Intestine, Small/enzymology ; Lymphoma, Large-Cell, Anaplastic/chemistry/enzymology/*genetics ; Male ; Molecular Sequence Data ; Nuclear Proteins/chemistry/*genetics ; Phosphoproteins/chemistry/*genetics ; Promoter Regions, Genetic ; Protein-Tyrosine Kinases/chemistry/*genetics ; RNA, Messenger/genetics/metabolism ; Receptor Protein-Tyrosine Kinases ; Sequence Alignment ; Signal Transduction ; Testis/enzymology ; *Translocation, Genetic ; Tumor Cells, Cultured
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    SecA homolog in protein transport within chloroplasts: evidence for endosymbiont-derived sorting (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-04
    Description: The SecA protein is an essential, azide-sensitive component of the bacterial protein translocation machinery. A SecA protein homolog (CPSecA) now identified in pea chloroplasts was purified to homogeneity. CPSecA supported protein transport into thylakoids, the chloroplast internal membrane network, in an azide-sensitive fashion. Only one of three pathways for protein transport into thylakoids uses the CPSecA mechanism. The use of a bacteria-homologous mechanism in intrachloroplast protein transport provides evidence for conservative sorting of proteins within chloroplasts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yuan, J -- Henry, R -- McCaffery, M -- Cline, K -- 1 R01 GM46951/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Nov 4;266(5186):796-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Plant Molecular and Cellular Biology Program, University of Florida, Gainesville 32611.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973633" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/metabolism ; Azides/pharmacology ; Bacterial Proteins/metabolism ; Base Sequence ; Biological Transport/drug effects ; Carrier Proteins/chemistry/isolation & purification/*metabolism ; Chloroplast Proteins ; Chloroplasts/*metabolism ; *Escherichia coli Proteins ; Intracellular Membranes/metabolism ; *Membrane Proteins ; *Membrane Transport Proteins ; Molecular Sequence Data ; Peas ; Photosynthetic Reaction Center Complex Proteins/*metabolism ; *Photosystem II Protein Complex ; Plant Proteins/chemistry/isolation & purification/*metabolism ; Plastocyanin/*metabolism ; Sodium Azide ; Symbiosis
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    Possible dino DNA find is greeted with skepticism (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, A -- New York, N.Y. -- Science. 1994 Nov 18;266(5188):1159.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973693" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Bone and Bones/*chemistry ; Cytochrome b Group/*genetics ; DNA, Mitochondrial/chemistry/*genetics/isolation & purification ; History, Ancient ; *Paleontology ; Polymerase Chain Reaction ; Utah
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    A lymphotoxin-beta-specific receptor (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-04-29
    Description: Tumor necrosis factor (TNF) and lymphotoxin-alpha (LT-alpha) are members of a family of secreted and cell surface cytokines that participate in the regulation of immune and inflammatory responses. The cell surface form of LT-alpha is assembled during biosynthesis as a heteromeric complex with lymphotoxin-beta (LT-beta), a type II transmembrane protein that is another member of the TNF ligand family. Secreted LT-alpha is a homotrimer that binds to distinct TNF receptors of 60 and 80 kilodaltons; however, these receptors do not recognize the major cell surface LT-alpha-LT-beta complex. A receptor specific for human LT-beta was identified, which suggests that cell surface LT may have functions that are distinct from those of secreted LT-alpha.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Crowe, P D -- VanArsdale, T L -- Walter, B N -- Ware, C F -- Hession, C -- Ehrenfels, B -- Browning, J L -- Din, W S -- Goodwin, R G -- Smith, C A -- New York, N.Y. -- Science. 1994 Apr 29;264(5159):707-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biomedical Sciences, University of California, Riverside 92521.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8171323" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Cysteine/chemistry ; Humans ; Hybridomas ; Ligands ; Lymphotoxin beta Receptor ; Lymphotoxin-alpha/*metabolism ; Molecular Sequence Data ; Receptors, Tumor Necrosis Factor/chemistry/*metabolism ; Recombinant Fusion Proteins/metabolism ; T-Lymphocytes/immunology ; Tetradecanoylphorbol Acetate/pharmacology ; Tumor Necrosis Factor-alpha/*metabolism
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    Correction of lethal intestinal defect in a mouse model of cystic fibrosis by human CFTR (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-09
    Description: Cystic fibrosis (CF) is caused by mutations in the gene encoding the cystic fibrosis transmembrane conductance regulator (CFTR). A potential animal model of CF, the CFTR-/- mouse, has had limited utility because most mice die from intestinal obstruction during the first month of life. Human CFTR (hCFTR) was expressed in CFTR-/- mice under the control of the rat intestinal fatty acid-binding protein gene promoter. The mice survived and showed functional correction of ileal goblet cell and crypt cell hyperplasia and cyclic adenosine monophosphate-stimulated chloride secretion. These results support the concept that transfer of the hCFTR gene may be a useful strategy for correcting physiologic defects in patients with CF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, L -- Dey, C R -- Wert, S E -- DuVall, M D -- Frizzell, R A -- Whitsett, J A -- DK38518/DK/NIDDK NIH HHS/ -- HL49004/HL/NHLBI NIH HHS/ -- HL51832/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 9;266(5191):1705-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Children's Hospital Medical Center, Division of Pulmonary Biology, Cincinnati, OH 45229-3039.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7527588" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Carrier Proteins/genetics ; Chlorides/metabolism ; Colforsin/pharmacology ; Colon/chemistry/pathology ; Cystic Fibrosis/genetics/metabolism/pathology/*therapy ; Cystic Fibrosis Transmembrane Conductance Regulator ; Disease Models, Animal ; Fatty Acid-Binding Proteins ; Gene Expression ; *Genetic Therapy ; Humans ; Intestinal Mucosa/chemistry/*pathology/secretion ; Intestine, Small/chemistry/pathology ; Membrane Proteins/analysis/*genetics/physiology ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; *Neoplasm Proteins ; *Nerve Tissue Proteins ; Promoter Regions, Genetic ; RNA, Messenger/analysis/genetics ; Rats ; Recombinant Proteins/biosynthesis ; *Tumor Suppressor Proteins
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    Requirement for the yeast gene LON in intramitochondrial proteolysis and maintenance of respiration (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-08
    Description: The role of protein degradation in mitochondrial homeostasis was explored by cloning of a gene from Saccharomyces cerevisiae that encodes a protein resembling the adenosine triphosphate (ATP)-dependent bacterial protease Lon. The predicted yeast protein has a typical mitochondrial matrix-targeting sequence at its amino terminus. Yeast cells lacking a functional LON gene contained a nonfunctional mitochondrial genome, were respiratory-deficient, and lacked an ATP-dependent proteolytic activity present in the mitochondria of Lon+ cells. Lon- cells were also impaired in their ability to catalyze the energy-dependent degradation of several mitochondrial matrix proteins and they accumulated electron-dense inclusions in their mitochondrial matrix.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Suzuki, C K -- Suda, K -- Wang, N -- Schatz, G -- New York, N.Y. -- Science. 1994 Apr 8;264(5156):273-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biozentrum der Universitat Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8146662" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Dependent Proteases ; Adenosine Triphosphatases/genetics/metabolism ; Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Fungal Proteins/metabolism ; *Genes, Fungal ; Heat-Shock Proteins/*genetics/metabolism ; Microscopy, Electron ; Mitochondria/*metabolism/ultrastructure ; Molecular Sequence Data ; *Oxygen Consumption ; Saccharomyces cerevisiae/*genetics/metabolism ; Serine Endopeptidases/*genetics/metabolism
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    A truncated erythropoietin receptor and cell death: a reanalysis (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-04-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakamura, Y -- Nakauchi, H -- New York, N.Y. -- Science. 1994 Apr 22;264(5158):588-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8160019" target="_blank"〉PubMed〈/a〉
    Keywords: *Apoptosis ; Base Sequence ; Cell Division ; Cell Line ; Erythropoietin/pharmacology ; Hematopoietic Stem Cells/cytology/*metabolism ; Humans ; Molecular Sequence Data ; Receptors, Erythropoietin/chemistry/genetics/*physiology ; Signal Transduction ; Transfection
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  • 46
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    Implications of FRA16A structure for the mechanism of chromosomal fragile site genesis (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-06-24
    Description: Fragile sites are chemically induced nonstaining gaps in chromosomes. Different fragile sites vary in frequency in the population and in the chemistry of their induction. DNA sequences encompassing and including the rare, autosomal, folate-sensitive fragile site, FRA16A, were isolated by positional cloning. The molecular basis of FRA16A was found to be expansion of a normally polymorphic p(CCG)n repeat. This repeat was adjacent to a CpG island that was methylated in fragile site-expressing individuals. The FRA16A locus in individuals who do not express the fragile site is not a site of DNA methylation (imprinting), which suggests that the methylation associated with fragile sites may be a consequence and not a cause of their genesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nancarrow, J K -- Kremer, E -- Holman, K -- Eyre, H -- Doggett, N A -- Le Paslier, D -- Callen, D F -- Sutherland, G R -- Richards, R I -- New York, N.Y. -- Science. 1994 Jun 24;264(5167):1938-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cytogenetics and Molecular Genetics, Women's and Children's Hospital, North Adelaide, South Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8009225" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Chromosome Fragile Sites ; *Chromosome Fragility ; Chromosomes, Artificial, Yeast ; *Chromosomes, Human, Pair 16 ; Dinucleoside Phosphates/metabolism ; Female ; Fragile X Syndrome/genetics ; Humans ; Male ; Methylation ; Molecular Sequence Data ; Pedigree ; Polymerase Chain Reaction ; Repetitive Sequences, Nucleic Acid
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  • 47
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    Control of kinetic properties of AMPA receptor channels by nuclear RNA editing (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-12-09
    Description: AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor channels mediate the fast component of excitatory postsynaptic currents in the central nervous system. Site-selective nuclear RNA editing controls the calcium permeability of these channels, and RNA editing at a second site is shown here to affect the kinetic aspects of these channels in rat brain. In three of the four AMPA receptor subunits (GluR-B, -C, and -D), intronic elements determine a codon switch (AGA, arginine, to GGA, glycine) in the primary transcripts in a position termed the R/G site, which immediately precedes the alternatively spliced modules "flip" and "flop." The extent of editing at this site progresses with brain development in a manner specific for subunit and splice form, and edited channels possess faster recovery rates from desensitization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lomeli, H -- Mosbacher, J -- Melcher, T -- Hoger, T -- Geiger, J R -- Kuner, T -- Monyer, H -- Higuchi, M -- Bach, A -- Seeburg, P H -- New York, N.Y. -- Science. 1994 Dec 9;266(5191):1709-13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Neuroendocrinology, University of Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7992055" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing ; Amino Acid Sequence ; Animals ; Base Sequence ; Brain/embryology/*metabolism ; Cell Nucleus/metabolism ; Exons ; Glutamic Acid/pharmacology ; Glycine/genetics ; Introns ; Kinetics ; Membrane Potentials ; Molecular Sequence Data ; Oocytes ; PC12 Cells ; Patch-Clamp Techniques ; *RNA Editing ; Rats ; Rats, Wistar ; Receptors, AMPA/*genetics/*metabolism ; Recombinant Proteins/metabolism ; Xenopus
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  • 48
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    Rescue of T cell-specific V(D)J recombination in SCID mice by DNA-damaging agents (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-21
    Description: Assembly of antigen receptor V (variable), D (diversity), and J (joining) gene segments requires lymphocyte-specific genes and ubiquitous DNA repair activities. Severe combined immunodeficient (SCID) mice are defective in general double-strand (ds) DNA break repair and V(D)J coding joint formation, resulting in arrested lymphocyte development. A single treatment of newborn SCID mice with DNA-damaging agents restored functional, diverse, T cell receptor beta chain coding joints, as well as development and expansion of thymocytes expressing both CD4 and CD8 coreceptors, but did not promote B cell development. Thymic lymphoma developed in all mice treated with DNA-damaging agents, suggesting an interrelation between V(D)J recombination, dsDNA break repair, and lymphomagenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Danska, J S -- Pflumio, F -- Williams, C J -- Huner, O -- Dick, J E -- Guidos, C J -- New York, N.Y. -- Science. 1994 Oct 21;266(5184):450-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Surgical Research, Hospital for Sick Children Research Institute, Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7524150" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; B-Lymphocytes/cytology/immunology ; Base Sequence ; Bleomycin/pharmacology ; Cell Transformation, Neoplastic ; *DNA Damage ; DNA Repair ; Gamma Rays ; *Gene Rearrangement ; Hematopoietic Stem Cells/cytology/immunology ; Lymphoma/etiology/pathology ; Mice ; Mice, SCID ; Molecular Sequence Data ; Receptors, Antigen, T-Cell, alpha-beta/*genetics ; T-Lymphocyte Subsets/cytology/immunology ; T-Lymphocytes/cytology/*immunology ; Thymus Neoplasms/etiology/pathology
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    Mesodermal patterning by a gradient of the vertebrate homeobox gene goosecoid (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-02-11
    Description: Amphibian mesoderm arises from the marginal zone of the early gastrula and generates various tissues such as notochord, muscle, kidney, and blood. Small changes (twofold) in the amount of microinjected messenger RNA encoding the goosecoid (gsc) homeodomain protein resulted in marked changes in the differentiation of mesoderm in Xenopus laevis. At least three thresholds were observed, which were sufficient to specify four mesodermal cell states. Endogenous gsc messenger RNA was expressed in the marginal zone in a graded fashion that is congruent with a role for this gene in dorso-ventral patterning of mesoderm at the early gastrula stage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Niehrs, C -- Steinbeisser, H -- De Robertis, E M -- HD21502-08/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1994 Feb 11;263(5148):817-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Institute, University of California, Los Angeles 90024-1737.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7905664" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Differentiation ; Culture Techniques ; DNA-Binding Proteins/*genetics ; Gastrula/*cytology/metabolism ; Gene Expression ; *Genes, Homeobox ; Goosecoid Protein ; *Homeodomain Proteins ; Mesoderm/*cytology ; Microinjections ; Molecular Sequence Data ; RNA, Messenger/genetics/metabolism ; *Repressor Proteins ; *Transcription Factors ; Xenopus laevis
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    Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-06-03
    Description: Through the study of transcriptional activation in response to interferon alpha (IFN-alpha) and interferon gamma (IFN-gamma), a previously unrecognized direct signal transduction pathway to the nucleus has been uncovered: IFN-receptor interaction at the cell surface leads to the activation of kinases of the Jak family that then phosphorylate substrate proteins called STATs (signal transducers and activators of transcription). The phosphorylated STAT proteins move to the nucleus, bind specific DNA elements, and direct transcription. Recognition of the molecules involved in the IFN-alpha and IFN-gamma pathway has led to discoveries that a number of STAT family members exist and that other polypeptide ligands also use the Jak-STAT molecules in signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Darnell, J E Jr -- Kerr, I M -- Stark, G R -- New York, N.Y. -- Science. 1994 Jun 3;264(5164):1415-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Cell Biology, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8197455" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; DNA-Binding Proteins/*metabolism ; Genes ; Genetic Complementation Test ; Humans ; Interferon-Stimulated Gene Factor 3 ; Interferon-Stimulated Gene Factor 3, gamma Subunit ; Interferon-alpha/*pharmacology ; Interferon-gamma/*pharmacology ; Molecular Sequence Data ; Mutation ; Protein-Tyrosine Kinases/metabolism ; Regulatory Sequences, Nucleic Acid ; *Signal Transduction ; Transcription Factors/*metabolism ; *Transcriptional Activation
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    Modulation of epithelial cell growth by intraepithelial gamma delta T cells (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-11-18
    Description: The role played in immune surveillance by gamma delta T cells residing in various epithelia has not been clear. It is shown here that activated gamma delta T cells obtained from skin and intestine express the epithelial cell mitogen keratinocyte growth factor (KGF). In contrast, intraepithelial alpha beta T cells, as well as all lymphoid alpha beta and gamma delta T cell populations tested, did not produce KGF or promote the growth of cultured epithelial cells. These results suggest that intraepithelial gamma delta T cells function in surveillance and in repair of damaged epithelial tissues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boismenu, R -- Havran, W L -- AI32751/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1994 Nov 18;266(5188):1253-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973709" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Division ; Cell Line ; Cells, Cultured ; Cloning, Molecular ; Dendritic Cells/*physiology ; Epithelial Cells ; Fibroblast Growth Factor 10 ; Fibroblast Growth Factor 7 ; *Fibroblast Growth Factors ; Growth Substances/*biosynthesis/genetics ; Keratinocytes/*cytology ; Lymphocyte Activation ; Mice ; Molecular Sequence Data ; *Receptors, Antigen, T-Cell, gamma-delta ; T-Lymphocyte Subsets/immunology/metabolism/*physiology
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    Padlock probes: circularizing oligonucleotides for localized DNA detection (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-30
    Description: Nucleotide sequence information derived from DNA segments of the human and other genomes is accumulating rapidly. However, it frequently proves difficult to use such short DNA segments to identify clones in genomic libraries or fragments in blots of the whole genome or for in situ analysis of chromosomes. Oligonucleotide probes, consisting of two target-complementary segments, connected by a linker sequence, were designed. Upon recognition of the specific nucleic acid molecule the ends of the probes were joined through the action of a ligase, creating circular DNA molecules catenated to the target sequence. These probes thus provide highly specific detection with minimal background.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nilsson, M -- Malmgren, H -- Samiotaki, M -- Kwiatkowski, M -- Chowdhary, B P -- Landegren, U -- New York, N.Y. -- Science. 1994 Sep 30;265(5181):2085-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Beijer Laboratory, Department of Medical Genetics, Biomedical Center, Uppsala, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7522346" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cells, Cultured ; Chromosomes, Human, Pair 12 ; Cystic Fibrosis Transmembrane Conductance Regulator ; DNA/*analysis ; DNA, Circular/*analysis ; Genetic Vectors ; Humans ; In Situ Hybridization ; Lymphocytes ; Membrane Proteins/genetics ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; *Oligonucleotide Probes/chemistry ; Repetitive Sequences, Nucleic Acid ; Templates, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Digenic retinitis pigmentosa due to mutations at the unlinked peripherin/RDS and ROM1 loci (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-10
    Description: In spite of recent advances in identifying genes causing monogenic human disease, very little is known about the genes involved in polygenic disease. Three families were identified with mutations in the unlinked photoreceptor-specific genes ROM1 and peripherin/RDS, in which only double heterozygotes develop retinitis pigmentosa (RP). These findings indicate that the allelic and nonallelic heterogeneity known to be a feature of monogenic RP is complicated further by interactions between unlinked mutations causing digenic RP. Recognition of the inheritance pattern exemplified by these three families might facilitate the identification of other examples of digenic inheritance in human disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kajiwara, K -- Berson, E L -- Dryja, T P -- EY00169/EY/NEI NIH HHS/ -- EY08683/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1994 Jun 10;264(5165):1604-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Berman-Gund Laboratory for the Study of Retinal Degenerations, Harvard Medical School, Massachusetts Eye and Ear Infirmary, Boston 02114.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8202715" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Base Sequence ; Electroretinography ; Eye Proteins/chemistry/*genetics ; Female ; Genes, Dominant ; Genes, Recessive ; Genetic Linkage ; Heterozygote ; Humans ; Intermediate Filament Proteins/chemistry/*genetics ; Male ; *Membrane Glycoproteins ; Membrane Proteins/chemistry/*genetics ; Molecular Sequence Data ; Mutation ; *Nerve Tissue Proteins ; Pedigree ; Peripherins ; Retinitis Pigmentosa/*genetics ; Rod Cell Outer Segment/chemistry ; Tetraspanins
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    Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-01
    Description: Concentration of urine in mammals is regulated by the antidiuretic hormone vasopressin. Binding of vasopressin to its V2 receptor leads to the insertion of water channels in apical membranes of principal cells in collecting ducts. In nephrogenic diabetes insipidus (NDI), the kidney fails to concentrate urine in response to vasopressin. A male patient with an autosomal recessive form of NDI was found to be a compound heterozygote for two mutations in the gene encoding aquaporin-2, a water channel. Functional expression studies in Xenopus oocytes revealed that each mutation resulted in nonfunctional water channel proteins. Thus, aquaporin-2 is essential for vasopressin-dependent concentration of urine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Deen, P M -- Verdijk, M A -- Knoers, N V -- Wieringa, B -- Monnens, L A -- van Os, C H -- van Oost, B A -- New York, N.Y. -- Science. 1994 Apr 1;264(5155):92-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Physiology, University of Nijmegen, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8140421" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Aquaporin 2 ; Aquaporin 6 ; *Aquaporins ; Base Sequence ; Cloning, Molecular ; Deamino Arginine Vasopressin/*pharmacology ; Diabetes Insipidus/*genetics/physiopathology ; Female ; Genes, Recessive ; Heterozygote ; Humans ; Kidney/metabolism/*physiology ; *Kidney Concentrating Ability ; Male ; Membrane Proteins/chemistry/genetics/*physiology ; Molecular Sequence Data ; Oocytes ; Pedigree ; Point Mutation ; Protein Structure, Secondary ; RNA, Complementary/genetics ; Water/metabolism ; Xenopus laevis
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    Activation of the myogenic lineage by MEF2A, a factor that induces and cooperates with MyoD (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-18
    Description: Muscle enhancer factor-2A (MEF2A), a member of the MADS family, induced myogenic development when ectopically expressed in clones of nonmuscle cells of human clones, a function previously limited to the muscle basic helix-loop-helix (bHLH) proteins. During myogenesis, MEF2A and bHLH proteins cooperatively activate skeletal muscle genes and physically interact through the MADS domain of MEF2A and the three myogenic amino acids of the muscle bHLH proteins. Thus, skeletal myogenesis is mediated by two distinct families of mutually inducible and interactive muscle transcription factors, either of which can initiate the developmental cascade.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaushal, S -- Schneider, J W -- Nadal-Ginard, B -- Mahdavi, V -- New York, N.Y. -- Science. 1994 Nov 18;266(5188):1236-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cardiology, Children's Hospital, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973707" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Cell Differentiation ; Cell Line ; DNA/metabolism ; DNA-Binding Proteins/genetics/*metabolism ; *Gene Expression Regulation ; Genes, Reporter ; Haplorhini ; Helix-Loop-Helix Motifs ; Humans ; MADS Domain Proteins ; MEF2 Transcription Factors ; Mice ; Molecular Sequence Data ; Muscle, Skeletal/*cytology/metabolism ; MyoD Protein/biosynthesis/*metabolism ; Myogenic Regulatory Factors ; Myogenin/biosynthesis/genetics/metabolism ; Transcription Factors/genetics/*metabolism ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Recombination between viral RNA and transgenic plant transcripts (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-03-11
    Description: Transformed plants expressing the 3' two-thirds of the cowpea chlorotic mottle virus (CCMV) capsid gene were inoculated with a CCMV deletion mutant lacking the 3' one-third of the capsid gene. Although the deletion inoculum replicates in inoculated cells, systemic infections occur only if recombination restores a functional capsid gene. Four of 125 inoculated transgenic plants, representing three different transgenic lines, became systemically infected. Analysis of viral RNA confirmed that RNA recombination had united the transgenic messenger RNA and the challenging virus through aberrant homologous recombination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Greene, A E -- Allison, R F -- New York, N.Y. -- Science. 1994 Mar 11;263(5152):1423-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Botany and Plant Pathology, Michigan State University, East Lansing 48824-1312.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8128222" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Bromovirus/*genetics/physiology ; Capsid/genetics ; Gene Deletion ; Genes, Viral ; Molecular Sequence Data ; Mutation ; Plants, Genetically Modified/genetics/*microbiology ; Plants, Toxic ; RNA, Messenger/*genetics ; RNA, Viral/*genetics ; *Recombination, Genetic ; Tobacco/genetics/microbiology ; Virus Replication
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Blockage of NF-kappa B signaling by selective ablation of an mRNA target by 2-5A antisense chimeras (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-05
    Description: Activation of 2-5A-dependent ribonuclease by 5'-phosphorylated, 2',5'-linked oligoadenylates, known as 2-5A, is one pathway of interferon action. Unaided uptake into HeLa cells of 2-5A linked to an antisense oligonucleotide resulted in the selective ablation of messenger RNA for the double-stranded RNA (dsRNA)-dependent protein kinase PKR. Similarly, purified, recombinant human 2-5A-dependent ribonuclease was induced to selectively cleave PKR messenger RNA. Cells depleted of PKR activity were unresponsive to activation of nuclear factor-kappa B (NF-kappa B) by the dsRNA poly(I):poly(C), which provides direct evidence that PKR is a transducer for the dsRNA signaling of NF-kappa B.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maran, A -- Maitra, R K -- Kumar, A -- Dong, B -- Xiao, W -- Li, G -- Williams, B R -- Torrence, P F -- Silverman, R H -- AI 28253/AI/NIAID NIH HHS/ -- AI 34039-02/AI/NIAID NIH HHS/ -- CA 44059/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Aug 5;265(5173):789-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Biology, Cleveland Clinic Foundation, OH 44195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7914032" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine Nucleotides/chemical synthesis/*pharmacology ; Base Sequence ; Endoribonucleases/metabolism ; Enzyme Activation ; HeLa Cells ; Humans ; Kinetics ; Molecular Sequence Data ; NF-kappa B/*antagonists & inhibitors ; Oligonucleotides, Antisense/chemical synthesis/*pharmacology ; Oligoribonucleotides/chemical synthesis/*pharmacology ; Protein-Serine-Threonine Kinases/*genetics ; RNA, Messenger/drug effects ; Signal Transduction/*drug effects ; eIF-2 Kinase
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Crystal structure of LacI member, PurR, bound to DNA: minor groove binding by alpha helices (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-04
    Description: The three-dimensional structure of a ternary complex of the purine repressor, PurR, bound to both its corepressor, hypoxanthine, and the 16-base pair purF operator site has been solved at 2.7 A resolution by x-ray crystallography. The bipartite structure of PurR consists of an amino-terminal DNA-binding domain and a larger carboxyl-terminal corepressor binding and dimerization domain that is similar to that of the bacterial periplasmic binding proteins. The DNA-binding domain contains a helix-turn-helix motif that makes base-specific contacts in the major groove of the DNA. Base contacts are also made by residues of symmetry-related alpha helices, the "hinge" helices, which bind deeply in the minor groove. Critical to hinge helix-minor groove binding is the intercalation of the side chains of Leu54 and its symmetry-related mate, Leu54', into the central CpG-base pair step. These residues thereby act as "leucine levers" to pry open the minor groove and kink the purF operator by 45 degrees.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schumacher, M A -- Choi, K Y -- Zalkin, H -- Brennan, R G -- GM 24658/GM/NIGMS NIH HHS/ -- GM 49244/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Nov 4;266(5186):763-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland 97201-3098.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973627" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*chemistry/genetics/metabolism ; Base Sequence ; Binding Sites ; Computer Graphics ; Crystallography, X-Ray ; DNA/chemistry/*metabolism ; DNA-Binding Proteins/*chemistry/genetics/metabolism ; *Escherichia coli Proteins ; Hydrogen Bonding ; Hypoxanthine ; Hypoxanthines/metabolism ; Lac Repressors ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; *Operator Regions, Genetic ; Protein Conformation ; Protein Structure, Secondary ; Repressor Proteins/*chemistry/genetics/metabolism
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    CD26 antigen and HIV fusion? (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-05-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Broder, C C -- Nussbaum, O -- Gutheil, W G -- Bachovchin, W W -- Berger, E A -- New York, N.Y. -- Science. 1994 May 20;264(5162):1156-9; author reply 1162-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7909959" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/*physiology ; Antigens, Differentiation, T-Lymphocyte/*physiology ; Base Sequence ; *Cell Fusion ; Cell Line ; Dipeptidyl Peptidase 4 ; Gene Products, env/*physiology ; Giant Cells/physiology ; HIV-1/*physiology ; Humans ; Hybrid Cells ; Molecular Sequence Data
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    Linkage analysis of IL4 and other chromosome 5q31.1 markers and total serum immunoglobulin E concentrations (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-05-20
    Description: Sib-pair analysis of 170 individuals from 11 Amish families revealed evidence for linkage of five markers in chromosome 5q31.1 with a gene controlling total serum immunoglobulin E (IgE) concentration. No linkage was found between these markers and specific IgE antibody concentrations. Analysis of total IgE within a subset of 128 IgE antibody-negative sib pairs confirmed evidence for linkage to 5q31.1, especially to the interleukin-4 gene (IL4). A combination of segregation and maximum likelihood analyses provided further evidence for this linkage. These analyses suggest that IL4 or a nearby gene in 5q31.1 regulates IgE production in a nonantigen-specific (noncognate) fashion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marsh, D G -- Neely, J D -- Breazeale, D R -- Ghosh, B -- Freidhoff, L R -- Ehrlich-Kautzky, E -- Schou, C -- Krishnaswamy, G -- Beaty, T H -- 1 P41 RR03655/RR/NCRR NIH HHS/ -- AI20059/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1994 May 20;264(5162):1152-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Johns Hopkins Asthma and Allergy Center, School of Medicine, Baltimore, MD 21224.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8178175" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Aged ; Allergens/immunology ; Base Sequence ; Child ; Child, Preschool ; *Chromosomes, Human, Pair 5 ; Female ; Genes, MHC Class II ; *Genetic Linkage ; Genetic Markers ; Humans ; Hypersensitivity, Immediate/genetics ; Immunoglobulin E/*blood ; Interleukin-4/*genetics ; Likelihood Functions ; Lod Score ; Male ; Middle Aged ; Molecular Sequence Data
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    Gene for familial psoriasis susceptibility mapped to the distal end of human chromosome 17q (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-05-20
    Description: A gene involved in psoriasis susceptibility was localized to the distal region of human chromosome 17q as a result of a genome-wide linkage analysis with polymorphic microsatellites and eight multiply affected psoriasis kindreds. In the family which showed the strongest evidence for linkage, the recombination fraction between a psoriasis susceptibility locus and D17S784 was 0.04 with a maximum two-point lod score of 5.33. There was also evidence for genetic heterogeneity and although none of the linked families showed any association with HLA-Cw6, two unlinked families showed weak levels of association. This study demonstrates that in some families, psoriasis susceptibility is due to variation at a single major genetic locus other than the human lymphocyte antigen locus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tomfohrde, J -- Silverman, A -- Barnes, R -- Fernandez-Vina, M A -- Young, M -- Lory, D -- Morris, L -- Wuepper, K D -- Stastny, P -- Menter, A -- P01-AI2327/AI/NIAID NIH HHS/ -- R01 HL47145/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1994 May 20;264(5162):1141-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, University of Texas Southwestern Medical Center, Dallas 75235-8591.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8178173" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Chromosome Mapping ; *Chromosomes, Human, Pair 17 ; DNA Primers ; DNA, Satellite/genetics ; Disease Susceptibility ; Female ; Genetic Linkage ; Genetic Markers ; HLA-C Antigens/genetics ; Haplotypes ; Humans ; Lod Score ; Male ; Molecular Sequence Data ; Pedigree ; Polymorphism, Genetic ; Psoriasis/*genetics ; Software
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    Long-term behavioral recovery in parkinsonian rats by an HSV vector expressing tyrosine hydroxylase (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-11-25
    Description: One therapeutic approach to treating Parkinson's disease is to convert endogenous striatal cells into levo-3,4-dihydroxyphenylalanine (L-dopa)-producing cells. A defective herpes simplex virus type 1 vector expressing human tyrosine hydroxylase was delivered into the partially denervated striatum of 6-hydroxydopamine-lesioned rats, used as a model of Parkinson's disease. Efficient behavioral and biochemical recovery was maintained for 1 year after gene transfer. Biochemical recovery included increases in both striatal tyrosine hydroxylase enzyme activity and in extracellular dopamine concentrations. Persistence of human tyrosine hydroxylase was revealed by expression of RNA and immunoreactivity.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2638002/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2638002/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉During, M J -- Naegele, J R -- O'Malley, K L -- Geller, A I -- EY09749/EY/NEI NIH HHS/ -- NS06208/NS/NINDS NIH HHS/ -- NS28227/NS/NINDS NIH HHS/ -- R01 NS034025/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Nov 25;266(5189):1399-403.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Surgery, Yale University School of Medicine, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7669103" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Corpus Striatum/*enzymology/metabolism ; Denervation ; Disease Models, Animal ; Dopamine/metabolism ; Gene Transfer Techniques ; *Genetic Therapy ; Genetic Vectors ; Humans ; Levodopa/metabolism ; Male ; Molecular Sequence Data ; *Motor Activity ; Neurons/enzymology ; Parkinson Disease/metabolism/*therapy ; Rats ; Rats, Sprague-Dawley ; Simplexvirus/*genetics ; Tyrosine 3-Monooxygenase/*genetics/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Noradrenergic regulation of cholinergic differentiation (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-06-10
    Description: When the sympathetic nerves that innervate rat sweat glands reach their targets, they are induced to switch from using norepinephrine as their neurotransmitter to acetylcholine. Catecholamines (such as norepinephrine) released by nerves growing to the sweat gland induce this phenotypic conversion by stimulating production of a cholinergic differentiation factor [sweat gland factor (SGF)] by gland cells. Here, culture of gland cells with sympathetic, but not sensory, neurons induced SGF production. Blockage of alpha 1- or beta-adrenergic receptors prevented acquisition of the cholinergic phenotype in sympathetic neurons co-cultured with sweat glands, and sweat glands from sympathectomized animals lacked SGF. Thus, reciprocal instructive interactions, mediated in part by small molecule neurotransmitters, direct the development of this synapse.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Habecker, B A -- Landis, S C -- NS-023678/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jun 10;264(5165):1602-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurosciences, Case Western Reserve University School of Medicine, Cleveland, OH 44106-4975.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8202714" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; Base Sequence ; Cell Differentiation ; Cells, Cultured ; Culture Media, Conditioned ; Glycoproteins/*biosynthesis ; Molecular Sequence Data ; Neuregulins ; Neurons/cytology/physiology ; Neurons, Afferent/cytology/physiology ; Parasympathetic Nervous System/cytology/*physiology ; Phenotype ; Rats ; Receptors, Adrenergic/*physiology ; Sweat Glands/cytology/*innervation/metabolism ; Sympathectomy ; Sympathetic Nervous System/cytology/*physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    RNA editing: transfer of genetic information from gRNA to precursor mRNA in vitro (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-07
    Description: RNA editing in the mitochondrion of Trypanosoma brucei extensively alters the adenosine triphosphate synthase (ATPase) subunit 6 precursor messenger RNA (pre-mRNA) by addition of 447 uridines and removal of 28 uridines. In vivo, the guide RNA gA6[14] is thought to specify the deletion of two uridines from the editing site closest to the 3' end. In this study, an in vitro system was developed that accurately removed uridines from this editing site in synthetic ATPase 6 pre-mRNA when gA6[14] and ATP were added. Mutations in both the guide RNA and the pre-mRNA editing site suggest that base-pairing interactions control the number of uridines deleted in vitro. Thus, guide RNAs are required for RNA editing and for the transfer of genetic information to pre-mRNAs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seiwert, S D -- Stuart, K -- GM 42188/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 7;266(5182):114-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06536-0182.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7524149" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/genetics ; Adenosine Triphosphate/metabolism ; Animals ; Base Composition ; Base Sequence ; Mitochondria/genetics ; Molecular Sequence Data ; Mutation ; RNA/chemistry/*genetics/metabolism ; *RNA Editing ; RNA Precursors/chemistry/*genetics/metabolism ; RNA, Guide/chemistry/*genetics/metabolism ; RNA, Protozoan/chemistry/genetics/metabolism ; Trypanosoma brucei brucei/*genetics/metabolism ; Uridine/metabolism
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    Human severe combined immunodeficiency due to a defect in ZAP-70, a T cell tyrosine kinase (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-10
    Description: A homozygous mutation in the kinase domain of ZAP-70, a T cell receptor-associated protein tyrosine kinase, produced a distinctive form of human severe combined immunodeficiency. Manifestations of this disorder included profound immunodeficiency, absence of peripheral CD8+ T cells, and abundant peripheral CD4+ T cells that were refractory to T cell receptor-mediated activation. These findings demonstrate that ZAP-70 is essential for human T cell function and suggest that CD4+ and CD8+ T cells depend on different intracellular signaling pathways to support their development or survival.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Elder, M E -- Lin, D -- Clever, J -- Chan, A C -- Hope, T J -- Weiss, A -- Parslow, T G -- AI29313/AI/NIAID NIH HHS/ -- GM43574/GM/NIGMS NIH HHS/ -- RR01271/RR/NCRR NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Jun 10;264(5165):1596-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, University of California, San Francisco 94143-0110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8202712" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cloning, Molecular ; Female ; Frameshift Mutation ; Gene Deletion ; Homozygote ; Humans ; Infant ; Male ; Molecular Sequence Data ; Polymerase Chain Reaction ; Protein-Tyrosine Kinases/*genetics/metabolism ; Receptors, Antigen, T-Cell/*metabolism ; Severe Combined Immunodeficiency/*genetics/immunology ; Signal Transduction ; T-Lymphocyte Subsets/*immunology ; Transfection ; Tumor Cells, Cultured ; ZAP-70 Protein-Tyrosine Kinase
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    The stereochemical course of group II intron self-splicing (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-09
    Description: The stereochemical specificities and reaction courses for both self-splicing steps of a group II intron have been determined by phosphorothioate substitution at the 5' and 3' splice site phosphodiester bonds. Both steps of the splicing reaction proceeded with a phosphorothioate in the Sp configuration but were blocked by the Rp diastereomer. Both steps also proceeded with inversion of stereochemical configuration around phosphorus, consistent with a concerted transesterification reaction. These results are identical to those found for nuclear precursor mRNA (pre-mRNA) splicing and provide support for the hypothesis that group II introns and nuclear pre-mRNA introns share a common evolutionary history.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Padgett, R A -- Podar, M -- Boulanger, S C -- Perlman, P S -- GM31480/GM/NIGMS NIH HHS/ -- GM45371/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 9;266(5191):1685-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas 75235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7527587" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Exons ; *Introns ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Oligoribonucleotides/chemistry ; Oxygen/chemistry ; Phosphorus/chemistry ; RNA/*chemistry/genetics ; *RNA Splicing ; Sulfur/chemistry ; Thionucleotides/chemistry
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    MHC class I expression in mice lacking the proteasome subunit LMP-7 (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-26
    Description: Proteasomes degrade endogenous proteins. Two subunits, LMP-2 and LMP-7, are encoded in a region of the major histocompatibility complex (MHC) that is critical for class I-restricted antigen presentation. Mice with a targeted deletion of the gene encoding LMP-7 have reduced levels of MHC class I cell-surface expression and present the endogenous antigen HY inefficiently; addition of peptides to splenocytes deficient in LMP-7 restores wild-type class I expression levels. This demonstrates the involvement of LMP-7 in the MHC class I presentation pathway and suggests that LMP-7 functions as an integral part of the peptide supply machinery.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fehling, H J -- Swat, W -- Laplace, C -- Kuhn, R -- Rajewsky, K -- Muller, U -- von Boehmer, H -- New York, N.Y. -- Science. 1994 Aug 26;265(5176):1234-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Basel Institute for Immunology, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8066463" target="_blank"〉PubMed〈/a〉
    Keywords: *ATP-Binding Cassette Transporters ; Amino Acid Sequence ; Animals ; Antigen Presentation ; Antigen-Presenting Cells/immunology ; Base Sequence ; Carrier Proteins/genetics ; *Cysteine Endopeptidases ; Female ; Gene Deletion ; H-2 Antigens/*biosynthesis/immunology ; H-Y Antigen/immunology ; Lymphocytes/immunology ; Male ; Mice ; Mice, Knockout ; Molecular Sequence Data ; *Multienzyme Complexes ; Proteasome Endopeptidase Complex ; Proteins/genetics/*physiology
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    Molecular basis of mammalian sexual determination: activation of Mullerian inhibiting substance gene expression by SRY (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-02
    Description: The pathway of male sexual development in mammals is initiated by SRY, a gene on the short arm of the Y chromosome. Its expression in the differentiating gonadal ridge directs testicular morphogenesis, characterized by elaboration of Mullerian inhibiting substance (MIS) and testosterone. SRY and MIS each belong to conserved gene families that function in the control of growth and differentiation. Structural and biochemical studies of the DNA binding domain of SRY (the HMG box) revealed a protein-DNA interaction consisting of partial side chain intercalation into a widened minor groove. Functional studies of SRY in a cell line from embryonic gonadal ridge demonstrated activation of a gene-regulatory pathway leading to expression of MIS. SRY molecules containing mutations associated with human sex reversal have altered structural interactions with DNA and failed to induce transcription of MIS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haqq, C M -- King, C Y -- Ukiyama, E -- Falsafi, S -- Haqq, T N -- Donahoe, P K -- Weiss, M A -- GM51558/GM/NIGMS NIH HHS/ -- HD30812/HD/NICHD NIH HHS/ -- P30HD28138/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 2;266(5190):1494-500.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pediatric Surgical Research Laboratory, Massachusetts General Hospital, Boston 02114.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7985018" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Anti-Mullerian Hormone ; Base Sequence ; Cell Line ; DNA/metabolism ; DNA-Binding Proteins/chemistry/*genetics/metabolism ; Female ; *Gene Expression Regulation, Developmental ; Genitalia, Male/*embryology ; *Glycoproteins ; Growth Inhibitors/biosynthesis/*genetics ; Humans ; Male ; Models, Biological ; Models, Molecular ; Molecular Sequence Data ; Mullerian Ducts ; *Nuclear Proteins ; Sex Differentiation/*genetics ; Sex-Determining Region Y Protein ; Testicular Hormones/biosynthesis/*genetics ; Transcription Factors/chemistry/*genetics/metabolism
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    Identification of two GTP-binding proteins in the chloroplast protein import machinery (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-11-11
    Description: Two of four proteins that associated with translocation intermediates during protein import across the outer chloroplast envelope membrane were identified as guanosine triphosphate (GTP)-binding proteins. Both proteins are integral membrane proteins of the outer chloroplast membrane, and both are partially exposed on the chloroplast surface where they were accessible to thermolysin digestion. Engagement of the outer membrane's import machinery by an import substrate was inhibited by slowly hydrolyzable or non-hydrolyzable GTP analogs. Thus, these GTP-binding proteins may function in protein import into chloroplasts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kessler, F -- Blobel, G -- Patel, H A -- Schnell, D J -- New York, N.Y. -- Science. 1994 Nov 11;266(5187):1035-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973656" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Base Sequence ; Biological Transport ; Chloroplasts/chemistry/*metabolism ; GTP-Binding Proteins/analysis/chemistry/*metabolism ; Guanosine Triphosphate/metabolism ; Intracellular Membranes/chemistry/*metabolism ; Membrane Proteins/analysis/chemistry/*metabolism ; Molecular Sequence Data ; *Monomeric GTP-Binding Proteins ; Plant Proteins/chemistry/*metabolism ; Sequence Alignment
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    Mutation of a mutL homolog in hereditary colon cancer (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-03-18
    Description: Some cases of hereditary nonpolyposis colorectal cancer (HNPCC) are due to alterations in a mutS-related mismatch repair gene. A search of a large database of expressed sequence tags derived from random complementary DNA clones revealed three additional human mismatch repair genes, all related to the bacterial mutL gene. One of these genes (hMLH1) resides on chromosome 3p21, within 1 centimorgan of markers previously linked to cancer susceptibility in HNPCC kindreds. Mutations of hMLH1 that would disrupt the gene product were identified in such kindreds, demonstrating that this gene is responsible for the disease. These results suggest that defects in any of several mismatch repair genes can cause HNPCC.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Papadopoulos, N -- Nicolaides, N C -- Wei, Y F -- Ruben, S M -- Carter, K C -- Rosen, C A -- Haseltine, W A -- Fleischmann, R D -- Fraser, C M -- Adams, M D -- CA35494/CA/NCI NIH HHS/ -- CA47527/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Mar 18;263(5153):1625-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Johns Hopkins Oncology Center, Baltimore, MD 21231.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8128251" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; *Adenosine Triphosphatases ; Amino Acid Sequence ; Bacterial Proteins/chemistry/*genetics ; Base Sequence ; Carrier Proteins ; Chromosome Mapping ; *Chromosomes, Human, Pair 3 ; Codon ; Colorectal Neoplasms, Hereditary Nonpolyposis/*genetics ; *DNA Repair ; *DNA-Binding Proteins ; *Escherichia coli Proteins ; Female ; Frameshift Mutation ; *Genes ; Genetic Markers ; Humans ; Male ; Molecular Sequence Data ; MutS Homolog 2 Protein ; Mutation ; Neoplasm Proteins/chemistry/*genetics ; Nuclear Proteins ; Open Reading Frames ; Polymerase Chain Reaction ; Proto-Oncogene Proteins/genetics ; Sequence Deletion ; Tumor Cells, Cultured
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    DNA targets for certain bZIP proteins distinguished by an intrinsic bend (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-05-20
    Description: In spite of the large amount of sequence conservation among the DNA binding segments of basic region leucine zipper (bZIP) proteins, these proteins can discriminate differently between target sequences that differ in half-site spacing. Here it is shown that the half-site spacing preferences of bZIP proteins are the result of (i) the differential intrinsic curvature in target binding sites that differ by insertion or deletion of a single base pair and (ii) the ability of some bZIP proteins to overcome this intrinsic curvature through a mechanism dependent on basic segment residues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Paolella, D N -- Palmer, C R -- Schepartz, A -- New York, N.Y. -- Science. 1994 May 20;264(5162):1130-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Yale University, New Haven, CT 06511.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8178171" target="_blank"〉PubMed〈/a〉
    Keywords: Activating Transcription Factor 2 ; Amino Acid Sequence ; Base Sequence ; Basic-Leucine Zipper Transcription Factors ; Binding Sites ; Cyclic AMP Response Element-Binding Protein/chemistry/*metabolism ; DNA/chemistry/*metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Fungal Proteins/chemistry/*metabolism ; G-Box Binding Factors ; *Leucine Zippers ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/chemistry/metabolism ; Protein Kinases/chemistry/*metabolism ; Proto-Oncogene Proteins c-jun/chemistry/metabolism ; *Saccharomyces cerevisiae Proteins ; *Transcription Factors
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    ZAP-70 deficiency in an autosomal recessive form of severe combined immunodeficiency (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-10
    Description: Protein tyrosine kinases (PTKs) play an integral role in T cell activation and differentiation. Defects in the Src-family PTKs in mice and in T cell lines have resulted in variable defects in thymic development and in T cell antigen receptor (TCR) signal transduction. Here, three siblings are described with an autosomal recessive form of severe combined immunodeficiency disease (SCID) in which ZAP-70, a non-Src PTK, is absent as a result of mutations in the ZAP-70 gene. This absence is associated with defects in TCR signal transduction, suggesting an important functional role for ZAP-70.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, A C -- Kadlecek, T A -- Elder, M E -- Filipovich, A H -- Kuo, W L -- Iwashima, M -- Parslow, T G -- Weiss, A -- AR-20684/AR/NIAMS NIH HHS/ -- GM39553/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jun 10;264(5165):1599-601.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Medicine, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8202713" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Calcium/metabolism ; Cell Line ; Child ; Female ; Gene Deletion ; *Genes, Recessive ; Humans ; Lymphocyte Activation ; Male ; Molecular Sequence Data ; Mutation ; Point Mutation ; Protein-Tyrosine Kinases/deficiency/*genetics/metabolism ; Receptors, Antigen, T-Cell/*metabolism ; Severe Combined Immunodeficiency/*genetics/immunology ; *Signal Transduction ; T-Lymphocyte Subsets/immunology ; ZAP-70 Protein-Tyrosine Kinase
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    Mediation of Epstein-Barr virus EBNA2 transactivation by recombination signal-binding protein J kappa (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-07-01
    Description: The Epstein-Barr virus (EBV) transactivator protein, termed Epstein-Barr virus nuclear antigen 2 (EBNA2), plays a critical role in the regulation of latent viral transcription and in the immortalization of EBV-infected B cells. Unlike most transcription factors, EBNA2 does not bind directly to its cis-responsive DNA element but requires a cellular factor, termed C-promoter binding factor 1 (CBF1). Here, CBF1 was purified and was found to directly interact with EBNA2. CBF1 is identical to a protein thought to be involved in immunoglobulin gene rearrangement, RBPJ kappa. Contrary to previous reports, CBF1-RBPJ kappa did not bind to the recombination signal sequences but instead bound to sites in the EBV C-promoter and in the CD23 promoter.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Henkel, T -- Ling, P D -- Hayward, S D -- Peterson, M G -- CA42245/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Jul 1;265(5168):92-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tularik Inc, South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8016657" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Viral/*genetics ; Base Sequence ; Binding Sites ; DNA-Binding Proteins/chemistry/*genetics/isolation & purification/*metabolism ; Epstein-Barr Virus Nuclear Antigens ; HeLa Cells ; Herpesvirus 4, Human/*genetics/immunology ; Humans ; Immunoglobulin J Recombination Signal Sequence-Binding Protein ; Molecular Sequence Data ; *Nuclear Proteins ; *Promoter Regions, Genetic ; Receptors, IgE/genetics ; Regulatory Sequences, Nucleic Acid ; *Transcriptional Activation
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    TLC1: template RNA component of Saccharomyces cerevisiae telomerase (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-10-21
    Description: Telomeres, the natural ends of linear eukaryotic chromosomes, are essential for chromosome stability. Because of the nature of DNA replication, telomeres require a specialized mechanism to ensure their complete duplication. Telomeres are also capable of silencing the transcription of genes that are located near them. In order to identify genes in the budding yeast Saccharomyces cerevisiae that are important for telomere function, a screen was conducted for genes that, when expressed in high amounts, would suppress telomeric silencing. This screen lead to the identification of the gene TLC1 (telomerase component 1). TLC1 encodes the template RNA of telomerase, a ribonucleoprotein required for telomere replication in a variety of organisms. The discovery of TLC1 confirms the existence of telomerase in S. cerevisiae and may facilitate both the analysis of this enzyme and an understanding of telomere structure and function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Singer, M S -- Gottschling, D E -- CA 14599/CA/NCI NIH HHS/ -- GM43893/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 21;266(5184):404-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Cell Biology, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7545955" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosomes, Fungal/genetics/metabolism ; DNA Nucleotidylexotransferase/chemistry/*genetics/metabolism ; Gene Expression Regulation, Fungal ; *Genes, Fungal ; Molecular Sequence Data ; RNA, Fungal/chemistry/*genetics/metabolism ; Saccharomyces cerevisiae/*enzymology/genetics ; Suppression, Genetic ; Telomere/genetics/metabolism ; Templates, Genetic
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    Protein-DNA recognition: new perspectives and underlying themes (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-02-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉von Hippel, P H -- GM-15792/GM/NIGMS NIH HHS/ -- GM-29158/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Feb 11;263(5148):769-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, University of Oregon, Eugene 97403.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8303292" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; Crystallography, X-Ray ; DNA/chemistry/*metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Models, Molecular ; Protein Binding ; Protein Conformation ; Thermodynamics
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    Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-09-09
    Description: The gene aquaporin-1 encodes channel-forming integral protein (CHIP), a member of a large family of water transporters found throughout nature. Three rare individuals were identified who do not express CHIP-associated Colton blood group antigens and whose red cells exhibit low osmotic water permeabilities. Genomic DNA analyses demonstrated that two individuals were homozygous for different nonsense mutations (exon deletion or frameshift), and the third had a missense mutation encoding a nonfunctioning CHIP molecule. Surprisingly, none of the three suffers any apparent clinical consequence, which raises questions about the physiological importance of CHIP and implies that other mechanisms may compensate for its absence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Preston, G M -- Smith, B L -- Zeidel, M L -- Moulds, J J -- Agre, P -- DK32753/DK/NIDDK NIH HHS/ -- HL33991/HL/NHLBI NIH HHS/ -- HL48268/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Sep 9;265(5178):1585-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7521540" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aquaporin 1 ; *Aquaporins ; Base Sequence ; Blood Group Antigens ; Cell Membrane Permeability ; Erythrocyte Membrane/chemistry/physiology ; Exons ; Female ; Homozygote ; Humans ; Ion Channels/blood/*genetics/urine ; Kidney Tubules/chemistry ; Molecular Sequence Data ; Mutation ; Oocytes ; Phenotype ; Polymerase Chain Reaction ; Xenopus
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    High-resolution structure of the oligomerization domain of p53 by multidimensional NMR (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-15
    Description: The three-dimensional structure of the oligomerization domain (residues 319 to 360) of the tumor suppressor p53 has been solved by multidimensional heteronuclear magnetic resonance (NMR) spectroscopy. The domain forms a 20-kilodalton symmetric tetramer with a topology made up from a dimer of dimers. The two primary dimers each comprise two antiparallel helices linked by an antiparallel beta sheet. One beta strand and one helix are contributed from each monomer. The interface between the two dimers forming the tetramer is mediated solely by helix-helix contacts. The overall result is a symmetric, four-helix bundle with adjacent helices oriented antiparallel to each other and with the two antiparallel beta sheets located on opposing faces of the molecule. The tetramer is stabilized not only by hydrophobic interactions within the protein core but also by a number of electrostatic interactions. The implications of the structure of the tetramer for the biological function of p53 are discussed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clore, G M -- Omichinski, J G -- Sakaguchi, K -- Zambrano, N -- Sakamoto, H -- Appella, E -- Gronenborn, A M -- New York, N.Y. -- Science. 1994 Jul 15;265(5170):386-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8023159" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Computer Graphics ; DNA/chemistry/metabolism ; Genes, p53 ; Macromolecular Substances ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Mutation ; *Protein Conformation ; Protein Structure, Secondary ; Tumor Suppressor Protein p53/*chemistry/genetics/metabolism
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  • 78
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    Naturally occurring variation in bristle number and DNA polymorphisms at the scabrous locus of Drosophila melanogaster (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-09
    Description: The association between quantitative genetic variation in bristle number and molecular variation at a candidate neurogenic locus, scabrous, was examined in Drosophila melanogaster. Approximately 32 percent of the genetic variation in abdominal bristle number (21 percent for sternopleural bristle number) among 47 second chromosomes from a natural population was correlated with DNA sequence polymorphisms at this locus. Several polymorphic sites associated with large phenotypic effects occurred at intermediate frequency. Quantitative genetic variation in natural populations caused by alleles that have large effects at a few loci and that segregate at intermediate frequencies conflicts with the classical infinitesimal model of the genetic basis of quantitative variation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lai, C -- Lyman, R F -- Long, A D -- Langley, C H -- Mackay, T F -- GM45146/GM/NIGMS NIH HHS/ -- GM45344/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 9;266(5191):1697-702.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Population Biology, University of California at Davis 95616.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7992053" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Base Sequence ; DNA/genetics ; *Drosophila Proteins ; Drosophila melanogaster/anatomy & histology/*genetics ; Female ; *Genes, Insect ; *Genetic Variation ; *Glycoproteins ; Haplotypes ; Linkage Disequilibrium ; Male ; Molecular Sequence Data ; Phenotype ; *Polymorphism, Genetic ; Proteins/*genetics ; Restriction Mapping ; Sense Organs/anatomy & histology
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  • 79
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    Coupling of local folding to site-specific binding of proteins to DNA (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-02-11
    Description: Thermodynamic studies have demonstrated the central importance of a large negative heat capacity change (delta C degree assoc) in site-specific protein-DNA recognition. Dissection of the large negative delta C degree assoc and the entropy change of protein-ligand and protein-DNA complexation provide a thermodynamic signature identifying processes in which local folding is coupled to binding. Estimates of the number of residues that fold on binding obtained from this analysis agree with structural data. Structural comparisons indicate that these local folding transitions create key parts of the protein-DNA interface. The energetic implications of this "induced fit" model for DNA site recognition are considered.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Spolar, R S -- Record, M T Jr -- GM23467/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Feb 11;263(5148):777-84.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Wisconsin-Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8303294" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Crystallography, X-Ray ; DNA/chemistry/*metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Models, Molecular ; Nucleic Acid Conformation ; Protein Conformation ; *Protein Folding ; Thermodynamics
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  • 80
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    Adaptive reversion of a frameshift mutation in Escherichia coli by simple base deletions in homopolymeric runs (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-15
    Description: Spontaneous mutations are thought to occur primarily in growing cells. However, spontaneous mutations also arise in nutritionally deprived cells, and in some cases this process appears to be adaptive. Here it is reported that when a Lac- strain of Escherichia coli is under selection for lactose use, the spectrum of Lac+ mutations that arises is different, and simpler, than that arising without selection. Mutations appearing during selection were mainly one-base deletions in runs of iterated bases. Similar mutations occurring in repetitive DNA elements are associated with a variety of human hereditary diseases and are increased in cells that cannot correct heteroduplex DNA.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2990682/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2990682/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Foster, P L -- Trimarchi, J M -- R01 GM054084/GM/NIGMS NIH HHS/ -- R01 GM054084-02/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jul 15;265(5170):407-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Environmental Health, Boston University School of Public Health, MA 02118.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8023164" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Escherichia coli/*genetics/growth & development/metabolism ; Frameshift Mutation ; Lac Operon ; Lactose/metabolism ; Molecular Sequence Data ; *Mutation ; Recombination, Genetic ; *Selection, Genetic ; *Sequence Deletion ; beta-Galactosidase/metabolism
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  • 81
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    Retention of unassembled components of integral membrane proteins by calnexin (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-01-21
    Description: Quality control mechanisms prevent the cell surface expression of incompletely assembled multisubunit receptors such as the T cell receptor (TCR). The molecular chaperone function of calnexin (IP90, p88), a 90-kilodalton protein that resides in the endoplasmic reticulum (ER), in the retention of representative chains of the TCR-CD3 complex in the ER was tested. Truncation mutants of calnexin, when transiently expressed in COS cells, were exported from the ER and either accumulated in the Golgi or progressed to the cell surface. CD3 epsilon chains cotransfected with the forms of calnexin that were not retained in the ER exited the ER and colocalized with calnexin. Since engineered calnexin determined the intracellular localization of the proteins associated with it, it is concluded that calnexin interacts with incompletely assembled TCR components and retains them in the ER.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rajagopalan, S -- Xu, Y -- Brenner, M B -- New York, N.Y. -- Science. 1994 Jan 21;263(5145):387-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Rheumatology and Immunology, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8278814" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD3/*metabolism ; Base Sequence ; Calcium-Binding Proteins/analysis/chemistry/*metabolism ; Calnexin ; Cell Line ; Cell Membrane/metabolism ; Endoplasmic Reticulum/*metabolism ; Golgi Apparatus/metabolism ; Histocompatibility Antigens Class I/metabolism ; Lysosomes/metabolism ; Membrane Proteins/analysis/chemistry/*metabolism ; Molecular Sequence Data ; Nuclear Envelope/metabolism ; Receptor-CD3 Complex, Antigen, T-Cell/*metabolism ; Recombinant Proteins/metabolism ; Transfection
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  • 82
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    An interleukin-4-induced transcription factor: IL-4 Stat (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-16
    Description: Interleukin-4 (IL-4) is an immunomodulatory cytokine secreted by activated T lymphocytes, basophils, and mast cells. It plays an important role in modulating the balance of T helper (Th) cell subsets, favoring expansion of the Th2 lineage relative to Th1. Imbalance of these T lymphocyte subsets has been implicated in immunological diseases including allergy, inflammation, and autoimmune disease. IL-4 may mediate its biological effects, at least in part, by activating a tyrosine-phosphorylated DNA binding protein. This protein has now been purified and its encoding gene cloned. Examination of the primary amino acid sequence of this protein indicates that it is a member of the signal transducers and activators of transcription (Stat) family of DNA binding proteins, hereby designated IL-4 Stat. Study of the inhibitory activities of phosphotyrosine-containing peptides derived from the intracellular domain of the IL-4 receptor provided evidence for direct coupling of receptor and transcription factor during the IL-4 Stat activation cycle. Such observations indicate that IL-4 Stat has the same functional domain for both receptor coupling and dimerization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hou, J -- Schindler, U -- Henzel, W J -- Ho, T C -- Brasseur, M -- McKnight, S L -- New York, N.Y. -- Science. 1994 Sep 16;265(5179):1701-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tularik, Inc., South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8085155" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; Cloning, Molecular ; Cross-Linking Reagents ; DNA/metabolism ; DNA-Binding Proteins/chemistry/genetics/isolation & purification/*metabolism ; Humans ; Interleukin-4/*pharmacology ; Interleukin-4 Receptor alpha Subunit ; Models, Biological ; Molecular Sequence Data ; Monocytes/metabolism ; Phosphopeptides/metabolism/pharmacology ; Phosphorylation ; Polymers ; Receptors, Cell Surface ; Receptors, Interleukin-4 ; Receptors, Mitogen/*metabolism ; STAT6 Transcription Factor ; Trans-Activators/chemistry/genetics/isolation & purification/*metabolism ; Transcription Factors/chemistry/genetics/*metabolism
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  • 83
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    Reconstitution of transcription factor SL1: exclusive binding of TBP by SL1 or TFIID subunits (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-23
    Description: RNA polymerase I and II transcription factors SL1 and TFIID, respectively, are composed of the TATA-binding protein (TBP) and a set of TBP-associated factors (TAFs) responsible for promoter recognition. How the universal transcription factor TBP becomes committed to a TFIID or SL1 complex has not been known. Complementary DNAs encoding each of the three TAFIs that are integral components of SL1 have not been isolated. Analysis of subunit interactions indicated that the three TAFIs can bind individually and specifically to TBP. In addition, these TAFIs interact with each other to form a stable TBP-TAF complex. When TBP was bound first by either TAFI110, 63, or 48, subunits of TFIID such as TAFII250 and 150 did not bind TBP. Conversely, if TBP first formed a complex with TAFII250 or 150, the subunits of SL1 did not bind TBP. These results suggest that a mutually exclusive binding specificity for TBP intrinsic to SL1 and TFIID subunits directs the formation of promoter- and RNA polymerase-selective TBP-TAF complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Comai, L -- Zomerdijk, J C -- Beckmann, H -- Zhou, S -- Admon, A -- Tjian, R -- New York, N.Y. -- Science. 1994 Dec 23;266(5193):1966-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular and Cell Biology, University of California at Berkeley 94720-3204.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7801123" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding, Competitive ; Cloning, Molecular ; DNA, Complementary/genetics ; DNA-Binding Proteins/chemistry/genetics/isolation & purification/*metabolism ; HeLa Cells ; Humans ; Molecular Sequence Data ; *Pol1 Transcription Initiation Complex Proteins ; Promoter Regions, Genetic ; Protein Binding ; RNA Polymerase I/metabolism ; TATA Box ; *TATA-Binding Protein Associated Factors ; TATA-Box Binding Protein ; Transcription Factor TFIID ; Transcription Factors/chemistry/genetics/isolation & purification/*metabolism ; Transcription, Genetic
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  • 84
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    Association of poly(CA).poly(TG) DNA fragments into four-stranded complexes bound by HMG1 and 2 (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-15
    Description: The tandemly repeated DNA sequence poly(CA).poly(TG) is found in tracts up to 60 base pairs long, dispersed at thousands of sites throughout the genomes of eukaryotes. Double-stranded DNA fragments containing such sequences associated spontaneously with each other in vitro, in the absence of protein, forming stable four-stranded structures that were detected by gel electrophoresis and electron microscopy. These structures were recognized specifically by the nuclear nonhistone high mobility group (HMG) proteins 1 and 2 as evidenced by gel retardation. Such sequence-specific complexes might be involved in vivo in recombination or other processes requiring specific association of two double-stranded DNA molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gaillard, C -- Strauss, F -- New York, N.Y. -- Science. 1994 Apr 15;264(5157):433-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut Jacques Monod, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8153633" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/*chemistry/metabolism ; Electrophoresis, Polyacrylamide Gel ; High Mobility Group Proteins/chemistry/*metabolism ; Microscopy, Electron ; Molecular Sequence Data ; Nucleic Acid Conformation ; Polydeoxyribonucleotides/*chemistry/metabolism ; *Repetitive Sequences, Nucleic Acid
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  • 85
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    Catalytic activity of an RNA domain derived from the U6-U4 RNA complex (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-01-07
    Description: U6 RNA contains two regions that are essential for proper splicing of nuclear precursor messenger RNA (pre-mRNA). A comparison of putative secondary structures of the U6-U4 RNA complexes from different phyla revealed a conserved domain that is similar to the catalytic hammerhead RNA motif. Although no catalytic activity was detected in the mammalian U6-U4 RNA complexes, two nucleotide changes in U6 RNA and one in U4 RNA conferred cleavage activity to the complex. Furthermore, the highly conserved domain of the wild-type complex, without the accompanying flanking regions, cleaved an RNA substrate and exhibited other characteristics of the hammerhead ribozyme. The possible involvement of this structure in pre-mRNA splicing is also discussed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, J H -- Cedergren, R -- Nadal-Ginard, B -- R01 AR36865-08/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jan 7;263(5143):77-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Cellular and Molecular Physiology, Harvard Medical School, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8272868" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Humans ; Introns ; Magnesium/metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA Splicing ; RNA, Catalytic/chemistry/*metabolism ; RNA, Small Nuclear/chemistry/*metabolism ; Yeasts/genetics
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  • 86
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    Design of a G.C-specific DNA minor groove-binding peptide (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-28
    Description: A four-ring tripeptide containing alternating imidazole and pyrrole carboxamides specifically binds six-base pair 5'-(A,T)GCGC(A,T)-3' sites in the minor groove of DNA. The designed peptide has a specificity completely reversed from that of the tripyrrole distamycin, which binds A,T sequences. Structural studies with nuclear magnetic resonance revealed that two peptides bound side-by-side and in an antiparallel orientation in the minor groove. Each of the four imidazoles in the 2:1 ligand-DNA complex recognized a specific guanine amino group in the GCGC core through a hydrogen bond. Targeting a designated four-base pair G.C tract by this synthetic ligand supports the generality of the 2:1 peptide-DNA motif for sequence-specific minor groove recognition of DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Geierstanger, B H -- Mrksich, M -- Dervan, P B -- Wemmer, D E -- GM-27681/GM/NIGMS NIH HHS/ -- GM-43129/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 28;266(5185):646-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate Group in Biophysics, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939719" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; Computer Graphics ; DNA/chemistry/*metabolism ; Drug Design ; Hydrogen Bonding ; Imidazoles/chemical synthesis/*chemistry/metabolism ; Ligands ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/chemistry/metabolism ; Oligopeptides/chemical synthesis/*chemistry/metabolism ; Protein Conformation ; Pyrroles/chemical synthesis/*chemistry/metabolism
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  • 87
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    Target of the transcriptional activation function of phage lambda cI protein (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-01-07
    Description: Activation of transcription initiation by the cI protein of phage lambda is thought to be mediated by a direct interaction between cl and RNA polymerase at the PRM promoter. Two negatively charged amino acid residues in the DNA binding domain of cI play a key role in activation, suggesting that these residues contact RNA polymerase. The subunit of RNA polymerase involved was identified by selecting polymerase mutants that restored the activation function of a mutant form of cI protein. Although previous studies suggest that several activators interact with the alpha subunit of RNA polymerase, the results here suggest that cI interacts with the sigma subunit. An arginine to histidine change near the carboxyl terminus of sigma specifically suppresses an aspartic acid to asparagine change in the activation region of cI. This finding supports the direct-contact model and suggests that a cluster of positively charged residues near the carboxyl terminus of sigma is the target of the negatively charged activation region of cI.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, M -- Moyle, H -- Susskind, M M -- GM36811/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jan 7;263(5143):75-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Southern California, Los Angeles 90089-1340.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8272867" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage P22/genetics ; Bacteriophage lambda/*genetics ; Base Sequence ; *DNA-Binding Proteins ; DNA-Directed RNA Polymerases/genetics/metabolism ; Models, Genetic ; Molecular Sequence Data ; Promoter Regions, Genetic ; Repressor Proteins/chemistry/*genetics/metabolism ; Sigma Factor/chemistry/*genetics/metabolism ; Suppression, Genetic ; Transcription Factors/chemistry/*genetics/metabolism ; *Transcriptional Activation ; Viral Proteins ; Viral Regulatory and Accessory Proteins
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  • 88
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    Kin selection, social structure, gene flow, and the evolution of chimpanzees (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-26
    Description: Hypotheses about chimpanzee social behavior, phylogeography, and evolution were evaluated by noninvasive genotyping of free-ranging individuals from 20 African sites. Degrees of relatedness among individuals in one community were inferred from allele-sharing at eight nuclear simple sequence repeat (SSR) loci. Males are related on the order of half-siblings, and homozygosity is significantly increased at several SSR loci compared to Hardy-Weinberg expectations. These data support the kin-selection hypothesis for the evolution of cooperation among males. Sequence variation patterns at two mitochondrial loci indicate historically high long-distance gene flow and clarify the relationships among three allopatric subspecies. The unexpectedly large genetic distance between the western subspecies, Pan troglodytes verus, and the other two subspecies suggests a divergence time of about 1.58 million years. This result, if confirmed at nuclear loci and supported by eco-behavioral data, implies that P. t. verus should be elevated to full species rank.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morin, P A -- Moore, J J -- Chakraborty, R -- Jin, L -- Goodall, J -- Woodruff, D S -- 1T32 HG00005-02/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1994 Aug 26;265(5176):1193-201.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, San Diego, La Jolla 92093-0116.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7915048" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Alleles ; Animals ; Base Sequence ; *Biological Evolution ; DNA/analysis/genetics ; Female ; *Genetic Variation ; Hair/chemistry ; Male ; Molecular Sequence Data ; Pan troglodytes/classification/*genetics/psychology ; Phylogeny ; Polymerase Chain Reaction ; Polymorphism, Restriction Fragment Length ; Repetitive Sequences, Nucleic Acid ; *Social Behavior ; Tanzania
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  • 89
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    Suppression of hyphal formation in Candida albicans by mutation of a STE12 homolog (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-09
    Description: A Candida albicans gene (CPH1) was cloned that encodes a protein homologous to Saccharomyces cerevisiae Ste12p, a transcription factor that is the target of the pheromone response mitogen-activated protein kinase cascade. CPH1 complements both the mating defect of ste12 haploids and the filamentous growth defect of ste12/ste12 diploids. Candida albicans strains without a functional CPH1 gene (cph1/cph1) show suppressed hyphal formation on solid medium. However, cph1/cph1 strains can still form hyphae in liquid culture and in response to serum. Thus, filamentous growth may be activated in C. albicans by the same signaling kinase cascade that activates Ste12p in S. cerevisiae; however, alternative pathways may exist in C. albicans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, H -- Kohler, J -- Fink, G R -- GM402661/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 9;266(5191):1723-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7992058" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Candida albicans/cytology/genetics/*growth & development ; Cloning, Molecular ; Culture Media ; Fungal Proteins/chemistry/*genetics/physiology ; *Genes, Fungal ; Genetic Complementation Test ; Molecular Sequence Data ; Mutation ; Saccharomyces cerevisiae/cytology/genetics/growth & development ; *Saccharomyces cerevisiae Proteins ; Transcription Factors/chemistry/*genetics/physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 90
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    High-resolution molecular discrimination by RNA (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-03-11
    Description: Species of RNA that bind with high affinity and specificity to the bronchodilator theophylline were identified by selection from an oligonucleotide library. One RNA molecule binds to theophylline with a dissociation constant Kd of 0.1 microM. This binding affinity is 10,000-fold greater than the RNA molecule's affinity for caffeine, which differs from theophylline only by a methyl group at nitrogen atom N-7. Analysis by nuclear magnetic resonance indicates that this RNA molecule undergoes a significant change in its conformation or dynamics upon theophylline binding. Binding studies of compounds chemically related to theophylline have revealed structural features required for the observed binding specificity. These results demonstrate the ability of RNA molecules to exhibit an extremely high degree of ligand recognition and discrimination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jenison, R D -- Gill, S C -- Pardi, A -- Polisky, B -- AI01051/AI/NIAID NIH HHS/ -- AI33098/AI/NIAID NIH HHS/ -- RR03283/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1994 Mar 11;263(5152):1425-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉NeXagen, Inc., Boulder, CO 80301.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7510417" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Binding, Competitive ; DNA, Complementary/chemistry ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Molecular Structure ; Nucleic Acid Conformation ; RNA/chemistry/*metabolism ; Sequence Analysis, DNA ; Theophylline/chemistry/*metabolism ; Xanthines/chemistry/metabolism
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  • 91
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    Stat3: a STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6 (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-01
    Description: The STAT family of proteins carries out a dual function: signal transduction and activation of transcription. A new family member, Stat3, becomes activated through phosphorylation on tyrosine as a DNA binding protein in response to epidermal growth factor (EGF) and interleukin-6 (IL-6) but not interferon gamma (IFN-gamma). It is likely that this phosphoprotein forms homodimers as well as heterodimers with the first described member of the STAT family, Stat91 (renamed Stat1 alpha), which is activated by the IFNs and EGF. Differential activation of different STAT proteins in response to different ligands should help to explain specificity in nuclear signaling from the cell surface.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhong, Z -- Wen, Z -- Darnell, J E Jr -- AI32489/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1994 Apr 1;264(5155):95-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Cell Biology, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8140422" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; DNA/metabolism ; DNA-Binding Proteins/chemistry/genetics/isolation & purification/*metabolism ; Epidermal Growth Factor/*pharmacology ; Humans ; Interferon-gamma ; Interleukin-6/*pharmacology ; Mice ; Molecular Sequence Data ; Phosphorylation ; Regulatory Sequences, Nucleic Acid ; STAT1 Transcription Factor ; STAT3 Transcription Factor ; Sequence Alignment ; Trans-Activators/metabolism ; Transfection ; Tumor Cells, Cultured ; Tyrosine/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 92
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    DNA bending by asymmetric phosphate neutralization (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-16
    Description: DNA is often bent when complexed with proteins. Understanding the forces responsible for DNA bending would be of fundamental value in exploring the interplay of these macromolecules. A series of experiments was devised to test the hypothesis that proteins with cationic surfaces can induce substantial DNA bending by neutralizing phosphates on one DNA face. Repulsions between phosphates in the remaining anionic helix are predicted to result in an unbalanced compression force acting to deform the DNA toward the protein. This hypothesis is supported by the results of electrophoretic experiments in which DNA spontaneously bends when one helical face is partially modified by incorporation of neutral phosphate analogs. Phasing with respect to a site of intrinsic DNA curvature (hexadeoxyadenylate tract) permits estimation of the electrostatic bend angle, and demonstrates that such modified DNAs are deformed toward the neutralized surface, as predicted. Similar model systems may be useful in exploring the extent to which phosphate neutralization can account for DNA bending by particular proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Strauss, J K -- Maher, L J 3rd -- GM47814/GM/NIGMS NIH HHS/ -- P30 CA36727-08/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 16;266(5192):1829-34.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha 68198-6805.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7997878" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cations/chemistry ; DNA/*chemistry ; DNA-Binding Proteins/chemistry ; Electrochemistry ; Electrophoresis, Polyacrylamide Gel ; Models, Molecular ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Nucleosomes/chemistry ; Oligodeoxyribonucleotides ; Organophosphorus Compounds/chemistry ; Phosphates/*chemistry ; Thermodynamics
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  • 93
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    The TATA-binding protein: a general transcription factor in eukaryotes and archaebacteria (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-05-27
    Description: The TATA-binding protein TBP appears to be essential for all transcription in eukaryotic cell nuclei, which suggests that its function was established early in evolution. Archaebacteria constitute a kingdom of organisms distinct from eukaryotes and eubacteria. Archaebacterial gene regulatory sequences often map to TATA box-like motifs. Here it is shown that the archaebacterium Pyrococcus woesei expresses a protein with structural and functional similarity to eukaryotic TBP molecules. This suggests that TBP's role in transcription was established before the archaebacterial and eukaryotic lineages diverged and that the transcription systems of archaebacteria and eukaryotes are fundamentally homologous.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rowlands, T -- Baumann, P -- Jackson, S P -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1994 May 27;264(5163):1326-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome/CRC Institute, Cambridge, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8191287" target="_blank"〉PubMed〈/a〉
    Keywords: Adenovirus E1A Proteins/genetics ; Amino Acid Sequence ; Arabidopsis/genetics ; Archaea/chemistry/*genetics/metabolism ; Base Sequence ; *Biological Evolution ; Cloning, Molecular ; DNA-Binding Proteins/chemistry/*genetics/metabolism ; Eukaryotic Cells/*metabolism ; Genes, Bacterial ; Molecular Sequence Data ; Polymerase Chain Reaction ; Recombinant Fusion Proteins ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins ; *TATA Box ; TATA-Box Binding Protein ; Transcription Factor TFIIB ; *Transcription Factor TFIIIB ; Transcription Factors/chemistry/*genetics/metabolism ; Transcription, Genetic ; Tumor Suppressor Protein p53/genetics
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  • 94
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    Coaxially stacked RNA helices in the catalytic center of the Tetrahymena ribozyme (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-16
    Description: Coaxial stacking of helical elements is a determinant of three-dimensional structure in RNA. In the catalytic center of the Tetrahymena group I intron, helices P4 and P6 are part of a tertiary structural domain that folds independently of the remainder of the intron. When P4 and P6 were fused with a phosphodiester linkage, the resulting RNA retained the detailed tertiary interactions characteristic of the native P4-P6 domain and even required lower magnesium ion concentrations for folding. These results indicate that P4 and P6 are coaxial in the P4-P6 domain and, therefore, in the native ribozyme. Helix fusion could provide a general method for identifying pairs of coaxially stacked helices in biological RNA molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murphy, F L -- Wang, Y H -- Griffith, J D -- Cech, T R -- GM31819/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Sep 16;265(5179):1709-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8085157" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Edetic Acid ; Electrophoresis, Polyacrylamide Gel ; Ferrous Compounds ; Introns ; Magnesium/pharmacology ; Molecular Sequence Data ; *Nucleic Acid Conformation ; RNA, Catalytic/*chemistry/ultrastructure ; RNA, Protozoan/*chemistry/ultrastructure ; Tetrahymena/*genetics
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  • 95
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    Role of a conserved retinoic acid response element in rhombomere restriction of Hoxb-1 (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-16
    Description: After activation in mesoderm and neuroectoderm, expression of the Hoxb-1 gene is progressively restricted to rhombomere (r) 4 in the hindbrain. Analysis of the chick and mouse Hoxb-1 genes identified positive and negative regulatory regions that cooperate to mediate segment-restricted expression during rhombomere formation. An enhancer generates expression extending into r3 and r5, and a repressor limits this domain to r4. The repressor contains a conserved retinoic acid response element, point mutations in which allow expression to spread into adjacent rhombomeres. Retinoids and their nuclear receptors may therefore participate in sharpening segment-restricted expression of Hoxb-1 during rhombomere boundary formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Studer, M -- Popperl, H -- Marshall, H -- Kuroiwa, A -- Krumlauf, R -- New York, N.Y. -- Science. 1994 Sep 16;265(5179):1728-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lab of Developmental Neurobiology, National Institute for Medical Research, Mill Hill, London, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7916164" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chick Embryo ; Enhancer Elements, Genetic ; Gene Expression Regulation ; *Genes, Homeobox ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; Neural Crest/metabolism ; Oligonucleotides/metabolism ; Point Mutation ; Receptors, Cytoplasmic and Nuclear/metabolism ; Receptors, Retinoic Acid/metabolism ; *Regulatory Sequences, Nucleic Acid ; Retinoid X Receptors ; Rhombencephalon/*embryology/metabolism ; *Transcription Factors ; Tretinoin/*pharmacology
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  • 96
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    Analysis and expression of a cloned pre-T cell receptor gene (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-18
    Description: The T cell antigen receptor (TCR) beta chain regulates early T cell development in the absence of the TCR alpha chain. The developmentally controlled gene described here encodes the pre-TCR alpha (pT alpha) chain, which covalently associates with TCR beta and with the CD3 proteins forms a pre-TCR complex that transduces signals in immature thymocytes. Unlike the lambda 5 pre-B cell receptor protein, the pT alpha chain is a type I transmembrane protein whose cytoplasmic tail contains two potential phosphorylation sites and a Src homology 3 (SH3)-domain binding sequence. Pre-TCR alpha transfection experiments indicated that surface expression of the pre-TCR is controlled by additional developmentally regulated proteins. Identification of the pT alpha gene represents an essential step in the structure-function analysis of the pre-TCR complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saint-Ruf, C -- Ungewiss, K -- Groettrup, M -- Bruno, L -- Fehling, H J -- von Boehmer, H -- New York, N.Y. -- Science. 1994 Nov 18;266(5188):1208-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Unite INSERM 373, Institut Necker, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973703" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD3/metabolism ; Base Sequence ; Cell Line ; *Cloning, Molecular ; DNA, Complementary/genetics ; *Gene Expression Regulation, Developmental ; Gene Rearrangement ; Membrane Glycoproteins/chemistry/*genetics/metabolism ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Open Reading Frames ; Phosphorylation ; Polymerase Chain Reaction ; Rabbits ; Receptors, Antigen, T-Cell, alpha-beta/chemistry/*genetics/metabolism ; Signal Transduction ; T-Lymphocytes/*immunology ; Transfection
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  • 97
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    Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-30
    Description: The complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII reveals that it contains 269 predicted or known genes (300 base pairs or larger). Fifty-nine of these genes (22 percent) were previously identified. Of the 210 novel genes, 65 are predicted to encode proteins that are similar to other proteins of known or predicted function. Sixteen genes appear to be relatively recently duplicated. On average, there is one gene approximately every 2 kilobases. Although the coding density and base composition across the chromosome are not uniform, no regular pattern of variation is apparent.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnston, M -- Andrews, S -- Brinkman, R -- Cooper, J -- Ding, H -- Dover, J -- Du, Z -- Favello, A -- Fulton, L -- Gattung, S -- New York, N.Y. -- Science. 1994 Sep 30;265(5181):2077-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, 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/8091229" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; Chromosome Mapping ; *Chromosomes, Fungal ; DNA, Fungal/genetics ; *Genes, Fungal ; Introns ; Multigene Family ; Open Reading Frames ; RNA, Fungal/genetics ; RNA, Transfer/genetics ; Saccharomyces cerevisiae/*genetics
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  • 98
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    DNA fingerprinting (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lovell, W S -- New York, N.Y. -- Science. 1994 Oct 14;266(5183):201-2; author reply 202-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939647" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Dna ; DNA Fingerprinting/*statistics & numerical data ; Gene Frequency ; Humans ; Jurisprudence ; Probability
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 99
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    Coordinate initiation of Drosophila development by regulated polyadenylation of maternal messenger RNAs (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-23
    Description: Pattern formation in Drosophila depends initially on the translational activation of maternal messenger RNAs (mRNAs) whose protein products determine cell fate. Three mRNAs that dictate anterior, dorsoventral, and terminal specification--bicoid, Toll, and torso, respectively--showed increases in polyadenylate [poly(A)] tail length concomitant with translation. In contrast, posteriorly localized nanos mRNA, although also translationally activated, was not regulated by poly(A) status. These results implicate at least two mechanisms of mRNA activation in flies. Studies with bicoid mRNA showed that cytoplasmic polyadenylation is necessary for translation, establishing this pathway as essential for embryogenesis. Combined, these experiments identify a regulatory pathway that can coordinate initiation of maternal pattern formation systems in Drosophila.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Salles, F J -- Lieberfarb, M E -- Wreden, C -- Gergen, J P -- Strickland, S -- GM51584/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 23;266(5193):1996-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University Medical Center at Stony Brook, NY 11794-8651.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7801127" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cytoplasm/metabolism ; Drosophila/*embryology/genetics ; *Drosophila Proteins ; Embryonic Development ; Female ; *Homeodomain Proteins ; Insect Hormones/genetics ; Membrane Glycoproteins/genetics ; Molecular Sequence Data ; Morphogenesis ; Ovary/metabolism ; Poly A/*metabolism ; *Protein Biosynthesis ; Protein-Tyrosine Kinases/genetics ; RNA, Messenger/genetics/*metabolism ; *RNA-Binding Proteins ; *Receptor Protein-Tyrosine Kinases ; *Receptors, Cell Surface ; Toll-Like Receptors ; *Trans-Activators
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  • 100
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    Mapping the lectin-like activity of tumor necrosis factor (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-02-11
    Description: Tumor necrosis factor (TNF), but not lymphotoxin (LT), is directly trypanolytic for salivarian trypanosomes. This activity was not blocked by soluble 55-kilodalton and 75-kilodalton TNF receptors, but was potently inhibited by N,N'-diacetylchitobiose, an oligosaccharide that binds TNF. Comparative sequence analysis of TNF and LT localized the trypanocidal region, and synthetic peptides were trypanolytic. TNF molecules in which the trypanocidal region was mutated or deleted retained tumoricidal activity. Thus, trypanosome-TNF interactions occur via a TNF domain, probably with lectin-like affinity, which is functionally and spatially distinct from the mammalian TNF receptor binding sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lucas, R -- Magez, S -- De Leys, R -- Fransen, L -- Scheerlinck, J P -- Rampelberg, M -- Sablon, E -- De Baetselier, P -- New York, N.Y. -- Science. 1994 Feb 11;263(5148):814-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular Immunology, University of Brussels, Sint-Genesius-Rode, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8303299" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; *Disaccharides ; Glucans/metabolism/pharmacology ; L Cells (Cell Line) ; Lectins/chemistry/metabolism/*pharmacology ; Lymphotoxin-alpha/pharmacology ; Mice ; Molecular Sequence Data ; Mutation ; Peptide Fragments/chemistry/pharmacology ; Receptors, Tumor Necrosis Factor/metabolism ; Trypanosoma brucei brucei/*drug effects ; Tumor Necrosis Factor-alpha/chemistry/genetics/metabolism/*pharmacology
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