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  • Articles  (60)
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  • Latest Papers from Table of Contents or Articles in Press  (60)
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  • 1995-1999  (60)
  • 1995  (60)
  • Science. 267(5194): 108-11.  (1)
  • Science. 267(5194): 74-7.  (1)
  • Science. 267(5195): 249-52.  (1)
  • Science. 267(5197): 455-6.  (1)
  • Science. 267(5197): 518-22.  (1)
  • Science. 267(5198): 707-11.  (1)
  • Science. 267(5199): 899-902.  (1)
  • Science. 267(5203): 1491-4.  (1)
  • Science. 267(5203): 1510-2.  (1)
  • Science. 267(5204): 1658-62.  (1)
  • Science. 267(5206): 2003-6.  (1)
  • Science. 268(5208): 200-1.  (1)
  • Science. 268(5208): 297-300.  (1)
  • Science. 268(5208): 301-4.  (1)
  • Science. 268(5210): 497-8.  (1)
  • Science. 268(5210): 556-9.  (1)
  • Science. 268(5210): 567-9.  (1)
  • Science. 268(5212): 799-800.  (1)
  • Science. 268(5212): 866-9.  (1)
  • Science. 268(5212): 873-6.  (1)
  • 25
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  • Articles  (60)
  • Maps
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  • Latest Papers from Table of Contents or Articles in Press  (60)
Years
  • 1995-1999  (60)
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Journal
  • 1
    Publication Date: 1995-12-22
    Description: Hydrolysis of guanosine triphosphate (GTP) by the small guanosine triphosphatase (GTPase) adenosine diphosphate ribosylation factor-1 (ARF1) depends on a GTPase-activating protein (GAP). A complementary DNA encoding the ARF1 GAP was cloned from rat liver and predicts a protein with a zinc finger motif near the amino terminus. The GAP function required an intact zinc finger and additional amino-terminal residues. The ARF1 GAP was localized to the Golgi complex and was redistributed into a cytosolic pattern when cells were treated with brefeldin A, a drug that prevents ARF1-dependent association of coat proteins with the Golgi. Thus, the GAP is likely to be recruited to the Golgi by an ARF1-dependent mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cukierman, E -- Huber, I -- Rotman, M -- Cassel, D -- New York, N.Y. -- Science. 1995 Dec 22;270(5244):1999-2002.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Technion-Israel Institute of Technology, Haifa, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8533093" target="_blank"〉PubMed〈/a〉
    Keywords: ADP-Ribosylation Factor 1 ; ADP-Ribosylation Factors ; Alternative Splicing ; Amino Acid Sequence ; Animals ; Base Sequence ; Brefeldin A ; Cloning, Molecular ; Cyclopentanes/pharmacology ; Cytosol/metabolism ; DNA, Complementary ; GTP-Binding Proteins/*metabolism ; GTPase-Activating Proteins ; Golgi Apparatus/*metabolism ; Guanosine Triphosphate/metabolism ; Liver/metabolism ; Molecular Sequence Data ; Proteins/chemistry/genetics/isolation & purification/*metabolism ; Rats ; *Zinc Fingers
    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
    Publication Date: 1995-12-22
    Description: The cerebellar cortex is implicated in the learning of complex motor skills. This learning may require synaptic remodeling of Purkinje cell inputs. An extracellular serine protease, tissue plasminogen activator (tPA), is involved in remodeling various nonneural tissues and is associated with developing and regenerating neurons. In situ hybridization showed that expression of tPA messenger RNA was increased in the Purkinje neurons of rats within an hour of their being trained for a complex motor task. Antibody to tPA also showed the induction of tPA protein associated with cerebellar Purkinje cells. Thus, the induction of tPA during motor learning may play a role in activity-dependent synaptic plasticity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seeds, N W -- Williams, B L -- Bickford, P C -- AG-04418/AG/NIA NIH HHS/ -- NS-09818/NS/NINDS NIH HHS/ -- T32-GM 08497/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Dec 22;270(5244):1992-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Neuroscience Program, University of Colorado Health Sciences Center, Denver 80262, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8533091" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cerebellum/enzymology ; Enzyme Induction ; In Situ Hybridization ; Learning/*physiology ; Male ; Motor Skills/*physiology ; Neuronal Plasticity ; Physical Conditioning, Animal ; Psychomotor Performance/*physiology ; Purkinje Cells/*enzymology ; Rats ; Rats, Inbred F344 ; Tissue Plasminogen Activator/*biosynthesis/genetics
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  • 3
    Publication Date: 1995-12-08
    Description: Pineal serotonin N-acetyltransferase (arylalkylamine N-acetyltransferase, or AA-NAT) generates the large circadian rhythm in melatonin, the hormone that coordinates daily and seasonal physiology in some mammals. Complementary DNA encoding ovine AA-NAT was cloned. The abundance of AA-NAT messenger RNA (mRNA) during the day was high in the ovine pineal gland and somewhat lower in retina. AA-NAT mRNA was found unexpectedly in the pituitary gland and in some brain regions. The night-to-day ratio of ovine pineal AA-NAT mRNA is less than 2. In contrast, the ratio exceeds 150 in rats. AA-NAT represents a family within a large superfamily of acetyltransferases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coon, S L -- Roseboom, P H -- Baler, R -- Weller, J L -- Namboodiri, M A -- Koonin, E V -- Klein, D C -- New York, N.Y. -- Science. 1995 Dec 8;270(5242):1681-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section on Neuroendocrinology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502081" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arylamine N-Acetyltransferase/*genetics/metabolism ; Brain/metabolism ; Cell Line ; Circadian Rhythm ; *Cloning, Molecular ; DNA, Complementary/genetics ; Molecular Sequence Data ; Pineal Gland/*enzymology/metabolism ; Pituitary Gland/metabolism ; RNA, Messenger/genetics/metabolism ; Rats ; Retina/metabolism ; Sequence Alignment ; Sheep ; Transfection
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 1995-11-24
    Description: Apoptosis plays an important role during neuronal development, and defects in apoptosis may underlie various neurodegenerative disorders. To characterize molecular mechanisms that regulate neuronal apoptosis, the contributions to cell death of mitogen-activated protein (MAP) kinase family members, including ERK (extracellular signal-regulated kinase), JNK (c-JUN NH2-terminal protein kinase), and p38, were examined after withdrawal of nerve growth factor (NGF) from rat PC-12 pheochromocytoma cells. NGF withdrawal led to sustained activation of the JNK and p38 enzymes and inhibition of ERKs. The effects of dominant-interfering or constitutively activated forms of various components of the JNK-p38 and ERK signaling pathways demonstrated that activation of JNK and p38 and concurrent inhibition of ERK are critical for induction of apoptosis in these cells. Therefore, the dynamic balance between growth factor-activated ERK and stress-activated JNK-p38 pathways may be important in determining whether a cell survives or undergoes apoptosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xia, Z -- Dickens, M -- Raingeaud, J -- Davis, R J -- Greenberg, M E -- CA43855/CA/NCI NIH HHS/ -- CA65861/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 24;270(5240):1326-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Children's Hospital, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481820" target="_blank"〉PubMed〈/a〉
    Keywords: Alkaloids/pharmacology ; Animals ; *Apoptosis ; Calcium-Calmodulin-Dependent Protein Kinases/*antagonists & ; inhibitors/genetics/*metabolism ; Cell Differentiation ; Enzyme Activation ; Genes, jun ; *JNK Mitogen-Activated Protein Kinases ; MAP Kinase Kinase 1 ; MAP Kinase Kinase 3 ; MAP Kinase Kinase 4 ; MAP Kinase Kinase Kinases ; Mitogen-Activated Protein Kinase 1 ; Mitogen-Activated Protein Kinase 3 ; *Mitogen-Activated Protein Kinase Kinases ; *Mitogen-Activated Protein Kinases ; Nerve Growth Factors/pharmacology ; Neurons/*cytology/enzymology ; PC12 Cells ; Protein Kinases/*metabolism ; Protein-Serine-Threonine Kinases/genetics/metabolism ; Protein-Tyrosine Kinases/*antagonists & inhibitors/genetics/metabolism ; Rats ; *Signal Transduction ; Staurosporine ; Sympathetic Nervous System/cytology ; p38 Mitogen-Activated Protein Kinases
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-11-24
    Description: Opioid analgesia, the selective suppression of pain without effects on other sensations, also distinguishes between different types of pain: severe, persistent pain is potently inhibited by opioids, but they fail to cohceal the sensation of a pinprick. The cellular basis for this specificity was analyzed by means of patch-clamp experiments performed on fluorescently labeled nociceptive neurons (nociceptors) that innervate rat tooth pulp. Activation of the mu opioid receptor inhibited calcium channels on almost all small nociceptors but had minimal effect on large nociceptors. Somatostatin had the opposite specificity, preferentially inhibiting calcium channels on the large cells. Because persistent pain is mediated by slow-conducting, small nociceptors, opioids are thus likely to inhibit neurotransmitter release only at those primary synapses specialized for persistent pain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taddese, A -- Nah, S Y -- McCleskey, E W -- New York, N.Y. -- Science. 1995 Nov 24;270(5240):1366-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute, Oregon Health Sciences University, Portland 97201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481826" target="_blank"〉PubMed〈/a〉
    Keywords: Analgesics/*pharmacology ; Animals ; Calcium Channels/drug effects ; Cells, Cultured ; Dental Pulp/innervation ; Enkephalin, Ala(2)-MePhe(4)-Gly(5)- ; Enkephalins/*pharmacology ; Male ; Neurons, Afferent/*drug effects/physiology ; Neurotransmitter Agents/metabolism ; Nociceptors/*drug effects/physiology ; Patch-Clamp Techniques ; Presynaptic Terminals/drug effects/metabolism ; Rats ; Rats, Sprague-Dawley ; Receptors, Opioid, mu/*physiology ; Receptors, Somatostatin/physiology ; Sodium Channel Blockers ; Somatostatin/pharmacology
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  • 6
    Publication Date: 1995-11-17
    Description: A member of the inwardly rectifying potassium channel family was cloned here. The channel, called BIR (Kir6.2), was expressed in large amounts in rat pancreatic islets and glucose-responsive insulin-secreting cell lines. Coexpression with the sulfonylurea receptor SUR reconstituted an inwardly rectifying potassium conductance of 76 picosiemens that was sensitive to adenosine triphosphate (ATP) (IKATP) and was inhibited by sulfonylureas and activated by diazoxide. The data indicate that these pancreatic beta cell potassium channels are a complex composed of at least two subunits--BIR, a member of the inward rectifier potassium channel family, and SUR, a member of the ATP-binding cassette superfamily. Gene mapping data show that these two potassium channel subunit genes are clustered on human chromosome 11 at position 11p15.1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Inagaki, N -- Gonoi, T -- Clement, J P 4th -- Namba, N -- Inazawa, J -- Gonzalez, G -- Aguilar-Bryan, L -- Seino, S -- Bryan, J -- DK44311/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1166-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Medicine, Chiba University School of Medicine, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502040" target="_blank"〉PubMed〈/a〉
    Keywords: *ATP-Binding Cassette Transporters ; Adenosine Triphosphate/pharmacology ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Chromosome Mapping ; Chromosomes, Human, Pair 11 ; Cloning, Molecular ; Cricetinae ; Diazoxide/pharmacology ; Humans ; Islets of Langerhans/metabolism ; KATP Channels ; Mice ; Molecular Sequence Data ; Potassium/*metabolism ; Potassium Channels/*chemistry/genetics/*metabolism ; *Potassium Channels, Inwardly Rectifying ; Rats ; Receptors, Drug/*chemistry/metabolism ; Rubidium/metabolism ; Sulfonylurea Compounds/pharmacology ; Sulfonylurea Receptors
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-10-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fay, F S -- HL14523/HL/NHLBI NIH HHS/ -- HL47530/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1995 Oct 27;270(5236):588-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Massachusetts Medical School, Worchester 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7570016" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood Pressure ; Calcium/*metabolism ; Calcium Channels/metabolism ; Cell Membrane/metabolism ; Cerebral Arteries/physiology ; Membrane Potentials ; Muscle Proteins/metabolism ; *Muscle Relaxation ; Muscle, Smooth, Vascular/metabolism/*physiology ; Potassium Channels/metabolism ; Protein Kinases/metabolism ; Rats ; Ryanodine Receptor Calcium Release Channel ; Sarcoplasmic Reticulum/metabolism ; Vasoconstriction ; Vasodilation
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  • 8
    Publication Date: 1995-10-27
    Description: During stress, the activity of the sympathetic nervous system is changed in a global fashion, leading to an increase in cardiovascular function and a release of adrenal catecholamines. This response is thought to be regulated by a common set of brain neurons that provide a dual input to the sympathetic preganglionic neurons regulating cardiac and adrenal medullary functions. By using a double-virus transneuronal labeling technique, the existence of such a set of central autonomic neurons in the hypothalamus and brainstem was demonstrated. These neurons innervate both of the sympathetic outflow systems and likely function in circumstances where parallel sympathetic processing occurs, such as in the fight-or-flight response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jansen, A S -- Nguyen, X V -- Karpitskiy, V -- Mettenleiter, T C -- Loewy, A D -- HL-25449/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1995 Oct 27;270(5236):644-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7570024" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenal Glands/innervation ; Animals ; Brain Mapping ; Brain Stem/cytology/*physiology ; Catecholamines/metabolism ; Choline O-Acetyltransferase/metabolism ; *Escape Reaction ; Female ; Heart/innervation ; Herpesvirus 1, Suid/physiology ; Hypothalamus/cytology/*physiology ; Male ; Neural Pathways ; Neurons/metabolism/*physiology/virology ; Rats ; Rats, Sprague-Dawley ; Serotonin/metabolism ; Spinal Cord/cytology ; Stellate Ganglion ; Stress, Physiological/physiopathology ; Sympathetic Nervous System/cytology/*physiology
    Print ISSN: 0036-8075
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  • 9
    Publication Date: 1995-10-27
    Description: Local increases in intracellular calcium ion concentration ([Ca2+]i) resulting from activation of the ryanodine-sensitive calcium-release channel in the sarcoplasmic reticulum (SR) of smooth muscle cause arterial dilation. Ryanodine-sensitive, spontaneous local increases in [Ca2+]i (Ca2+ sparks) from the SR were observed just under the surface membrane of single smooth muscle cells from myogenic cerebral arteries. Ryanodine and thapsigargin inhibited Ca2+ sparks and Ca(2+)-dependent potassium (KCa) currents, suggesting that Ca2+ sparks activate KCa channels. Furthermore, KCa channels activated by Ca2+ sparks appeared to hyperpolarize and dilate pressurized myogenic arteries because ryanodine and thapsigargin depolarized and constricted these arteries to an extent similar to that produced by blockers of KCa channels. Ca2+ sparks indirectly cause vasodilation through activation of KCa channels, but have little direct effect on spatially averaged [Ca2+]i, which regulates contraction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nelson, M T -- Cheng, H -- Rubart, M -- Santana, L F -- Bonev, A D -- Knot, H J -- Lederer, W J -- HL25675/HL/NHLBI NIH HHS/ -- HL44455/HL/NHLBI NIH HHS/ -- HL51728/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1995 Oct 27;270(5236):633-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Vermont, Colchester 05446, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7570021" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Pyridinecarboxylic acid, ; 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ; ester/pharmacology ; Animals ; Cadmium/pharmacology ; Calcium/*metabolism ; Calcium Channel Agonists/pharmacology ; Calcium Channels/*metabolism ; Cell Membrane/metabolism ; Cerebral Arteries/physiology ; Membrane Potentials ; Muscle Contraction ; *Muscle Relaxation ; Muscle, Smooth, Vascular/cytology/*physiology ; Peptides/pharmacology ; Potassium Channels/*metabolism ; Rats ; Ryanodine/pharmacology ; Sarcoplasmic Reticulum/metabolism ; Terpenes/pharmacology ; Thapsigargin ; Vasodilation
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-10-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1995 Oct 27;270(5236):581.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7570014" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*cytology ; Brain-Derived Neurotrophic Factor ; Cell Communication ; Cell Survival ; Cells, Cultured ; Models, Neurological ; Nerve Growth Factors/pharmacology/*physiology ; Nerve Tissue Proteins/pharmacology/physiology ; Neural Pathways ; Neurons/*cytology/*physiology ; Rats
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