Showing papers in "Annual Review of Biochemistry in 1980"
TL;DR: Inhibitors 0/ Carboxyl, Metallo and Sulfhydryl Proteinases 599 Inhibitors0/ Serine Proteinases 601 The Standard Mechanism 601 The nature of the reactive site 604 Multiple reactive sites on a single polypeptide chain 608 The Inhibitor Families
Abstract: PERSPECTIVES AND SUMMARY 593 INTRODUCTION 595 Limited Knowledge 0/ Physiological Function 595 Nomenclature Problems 596 0.2 MACROGLOBULINS 598 INHIBITORS WITH CLASS-SPECIFIC REACTIVE SITES 599 Inhibitors 0/ Carboxyl, Metallo and Sulfhydryl Proteinases 599 Inhibitors 0/ Serine Proteinases 601 The Standard Mechanism 601 The nature of the reactive site 604 Multiple reactive sites on a single polypeptide chain 608 The Inhibitor Families 610 The pancreatic trypsin inhibitor (Kunitzj family 610 Pancreatic secretory trypsin inhibitor (Kazal) family 613 Streptomyces subtilisin inhibitor family 616 Bowman-Berk inhibitor family : 616 Soybean trypsin inhibitor (Kunitzj family 617 Other inhibitor families 618 Inhibitors in mammalian blood plasma 619
2,139 citations
TL;DR: The role of Exogenous Fatly Acids in the Control of Ketogenesis and Applications of the Model are examined.
Abstract: PERSPECTIVES AND SUMMARY . ENZYMES OF KETONE BODY SYNTHESIS AND UTILIZATION .. fIti!t::r% n\":::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::: REQUIREMENTS FOR KETOGENESIS . LOCALIZATION OF THE REGULATORY SITE IN KETOGENESIS .. Relative Importance of Generation Versus Utilization of Acetyl-CoA .. Utilization of acetyl-CoA . Genemtion of acetyl-CoA . The Role of Camitine Acyltransferase .. HORMONAL CONTROL OF THE REGULATORY SITE IN KETOGENESIS ...... . RESPONSE TO HORMONAL SIGNALS AT THE REGULATORY SITE ...... .. Relationship Between Camitine, Glycogen, and Ketogenesis . The Role of Malonyl-CoA in the Regulation of Ketogenesis .. The Role of Exogenous Fatly Acids in the Control of Ketogenesis .. Applications of the Model . PHYSIOLOGICAL OVERVIEW . CONCLUSION .
1,316 citations
TL;DR: A large number of the ribosomal genes affected by the bobbed locus mutation in Drosophila belong to the TSP class, which has been associated with central giant cell reprograming.
Abstract: PERSPECTIVES AND SUMMARY ,. '728 RIBOSOMAL RNA GENES 729 Introduction 729 Ribosomal Gene Redundancy 730 Chromosomal Location of Ribosomal Genes 730 Structure of Ribosomal Genes 735 Integrated tandemly repeated ribosomal genes 738 Extrachromosomal rDNA 741 Changes in Redundancy of Ribosomal Genes 741 Amplification of ribosomal genes 742 Mutants of the bobbed locus in Drosophila 743 THE GENES FOR 5S RIBOSOMAL RNA 745 tRNA GENES 748 PROPERTIES OF SPACERS 749 GENE FAMILIES WITH VARIANT REPETITION 751 Globin genes 751 Actin genes 751 Immunoglobulin genes 752 Vitel/ogenin genes 753 Ovalbumin and genes X and Y 753 Chorion protein genes 753
1,286 citations
TL;DR: The iron binding affinities of the sites, and the two-domain hypothesis of tronsfemn structure, are described.
Abstract: INTRODUCTION AND PERSPECTIVES 358 THE TRANSFERRINS 359 Definition, Nomenclature. and Evolution 359 Fundamental Properties 360 Physicochemical characteristics •......••••...• •••••......• •......•...•..•......•..•.••.. 360 Corbohydrate evntent 360 X-roy crystallography .•••.....•.•.••.••.......•........••.•.• ••••.....•..•.•....•..•.•.••.•..•.•• 362 The Two-Sited Nature of the Transferrins 362 Phenomenology of iron binding ..•••••• •.•••.••.•........•.....•...•••••••......•....•....•..••••••. 362 Iron binding affinities of the sites 362 The binding of iron to transfemn .•.. .•... •••••. •.... .•... .••.••..... .•. .•...... .•..••••••.. ••... .•.•. .•.•. .••. 364 The two-domain hypothesis of tronsfemn structure 364 Spectroscopic studies ... .•.•••• ••••... .••. .•....•••• ••. .•. .•...... .•.••••••.. .••...... .•.... .•.•••• ••. .•.•. .•.•. .•.•• 365 The Anion-Binding Site 366 The anion-binding requirement of tronsfemn ••••• ••••• ••••• 366 Binding site ligands •.•..•.•.••••.•.•.•••......••••..•.....•....•..••..•••••.....•.....•..•..••••••..•.•..•.•.••.•.• 368 Binding and Release 0/ Iron by Trans/errin 368 Iron binding ••••••••••.•..•.•..•..••••••••••• •••.•••....•..•..••••••••.•.....•..•.•....•..••••••••••••.• 368 Iron release ... 369
1,134 citations
1,109 citations
TL;DR: This paper presents a meta-analyses of six classes of enzyme involving reactions at phosphorus and some of the mechanisms leading to these reactions are described.
Abstract: PERSPECTIVES AND SUMMARY ... 877 Classes of enzyme involving reactions at phosphorus 878 COVALENT REACTION INTERMEDIATES, CRYPTIC AND OTHERWISE 879 Reactions of Phosphoric Monoesters ..... 879 Phosphatoses ..... ..... 879 Phosphokinases • •..•.....• • 881 Phosphomutases 886 Reactions of Phosphoric Diesters 890 REACTION ENERGETICS 892 "Off" Rates 893 Internal Thermodynamics ... .. ... ..... ...... ...... ... 896 THE NATURE OF THE ELEMENTARY STEP ....... ...... 898 Associative versus Diss ociative Pathways 898 Stereochemistry . .. ......... . ... 902 Prochiral substrate ..... prochiral product ... 902 Prochira/ substrate ..... pro-prochira/ product :.... ...... 903 Pro-prochiral substrate ..... pro-prochira/ product .. ........ ...... ........ ...... 905 Metal Ions 907 Cation-dependent diastereoisomer preference 908 Substitution-inert complexes of nucleotides 909 Catalysis ......... 911
1,035 citations
1,027 citations
TL;DR: Susceptibility to Vertebrate Collagenases, Susceptability to Other Proteases, and Solubility and Purification are studied.
Abstract: PERSPECTIVES AND SUMMARy . NOMENCLATURE .... . . . . . . . . . . . . . ........ . CHEMICAL CHARACTERIZATION . . . . . . . . . . . . . . Solubility and Purification .. . ......... ... . Structural Characteristics of Procollagen Chains .. Amino Acid and Carbohydrate Composition .. Comparative Peptide Mapping . Segment-Long-Spacing (SLS) Aggregates . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. . . . . . . . . . . . . . . . Susceptibility to Vertebrate Collagenases .. Sus�epti!'i!ity to Other Proteases . Antlgenlclty . Physical-Chemical Studies .
998 citations
TL;DR: A comparative study on the structure of CYTOCHROME P-450 at the HemeLocus and theMechanism of OXYGEN-SUPPORTED HYDROXYLATION REACfIONS and substrate Binding and first-Electron Transfer are presented.
Abstract: PERSPECfIVES AND SUMMARY . STRUCTURE OF CYTOCHROME P-450 AT THE HEME LOCUS .. CATALYTIC CYCLE FOR CYTOCHROME P-450-DEPENDENT HYDROXYLATION REACfIONS . MECHANISM OF OXYGEN-SUPPORTED HYDROXYLATION REACfIONS . Substrate Binding . First-Electron Transfer .
970 citations
949 citations
TL;DR: Detailed analysis of triglycerideRich Lipoproteins: VLDL and Chylomicrons and the effect of substrate composition, regulation of LPL, and other effectors are presented.
Abstract: PERSPECTIVES AND SUMMARY 668 OUTLINE OF LIPOPROTEIN METABOLISM 669 TriglycerideRich Lipoproteins: VLDL and Chylomicrons .... . . ..... ..... ....... .. .... .. 670 High-Density Lipoproteins ..... . . ... ..... ....... ...... ... . . .. . . 672 LIPOPROTEIN LIPASE (LPL) 673 Comparison of LPL f rom Diff erent Sources . . ... 673 Physio.logic�l Rol� of L.PL .... ... : 675 Trtglyceride assimilatI On ..... ...... .. ...... ..... . . ....... 675 Lipoprotein transformations .... .. . . ..... .. . . ......... ....... 677 Regulation of LPL .. . . . . .... ...... . . ...... ..... . . .. .. ... 679 Passive modulation of triglyceride removal 679 Active regulation of LPL activity ....... . . .. ......... ... .... . . ... .... .... ...... 681 Effect of substrate composition ........ . . .. ......... .. . . 684 Other effectors 685 HEPATIC LIPASE 686 LECITHIN CHOLESTEROL ACYL TRANSFERASE (LCAT) 688
TL;DR: In this paper, the authors discuss the role of genes and proteins in the development and regulation of MP BIOSYNTHESIS, including regulation by metabolites, regulation by Orotic Acid and Orotidine Accumulation.
Abstract: PERSPECfIVES AND SUMMARY 253 INTRODUCfION 256 GENES AND PROTEIN PRODUCfS 257 Drosophila 257 Mammals 258 Multienzyme pyr1-3 258 DBO dehydrogenase 260 Multienzyme pyrj,6 260 CHARACfERlSTICS OF DHOdeHase AND MULTIENZYMES pyrI-3 AND pyrS,6 262 Activities of Multienzyme pyrl-3 262 Carbamyl phosphate synthetase 262 Aspartate transcarbamylase 263 Dihydroorotase 263 Dihydroorotate Dehydrogenase 266 Activities of Multienzyme pyrS,6 266 REGULATION OF UMP BIOSYNTHESIS 269 Regulation by Metabolites 269 Regulation by Orotic Acid and Orotidine Accumulation 273 Channeling of CA�P, CAasp, and aMP 275
TL;DR: Biosynthesis of Phosphatidylglycerol and Cardiolipin 474 Biosynthetic pathways for bis-Monoacylglyc erol-P 474 PHOSPHOGLYCERIDE MODIFICATION REACfIONS 475 Base Exchange Re reactions 475 Reacyiation Reactions 475
Abstract: INTRODUCfION AND PERSPECfIVES ... ... 460 FATTY ACID ACTIVATION . . . . ..... . .. . . . . . . . . . . .. . .. . . . . . . . .. . .. .. . .. . 463 BIOSYNTHESIS OF PHOSPHATIDIC ACID .... ......... 464 Acylation of Glycerol-P • 464 Acylation of Lysophosphatidic Acid 465 Dihydroxyacetone-P Pathway 466 Diacylglycerol Kinase 467 BIOSYNTHESIS OF DIACYLGLYCEROL 468 BIOSYNTHESIS OF TRIACYLGL YCEROL ......... 469 BIOSYNTHESIS OF PHOSPHATIDYLCHOLINE AND . PHOSPHATIDYLETHANOLAMINE.... . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 470 Choline and Ethanolamine Kinases 470 Choline-P and Ethanolamine-P Cytidyltransferases 470 Cholineand Ethanoiaminephosphotransferases 471 Phosphatidylethanolamine N-methyltransferases 472 BIOSYNTHESIS OF CDP-DIACYLGL YCEROL AND THE ANIONIC PHOSPHOGLYCERIDES .... . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. . .. . .. ... . . . . . . 473 Biosynthesis of Phosphatidylglycerol and Cardiolipin 474 Biosynthesis of Phosphatidylinositol 474 Biosynthesis of bis-Monoacylglyc erol-P 474 PHOSPHOGLYCERIDE MODIFICATION REACfIONS 475 Base Exchange Reactions 475 Reacyiation Reactions 475
TL;DR: Proline Biosynthesis: The Glutamate Pathway and Proline Degradation: The Om Pathway.
Abstract: PERSPECTIVES AND SUMMARY 1006 INTRODUCTION 1007 PROLINE 1008 Proline Biosynthesis: The Glutamate Pathway 1008 Proline Biosynthesis: The Om Pathway 1015 Proline Degradation: The P5C Pathway 1018 Proline Degradation: Reguiation 1020 Proline Degradation: Other Pathways 1023 4-HYDROXYPROLlNE 1024 Natural Occurrence 1024 Metabolism General Features 1025 Catabolism of Free 4-Hyp 1034 3-HYDROXYPROLINE 1041 Metabolism 1042 3,4-DIHYDROXYPROLINE 1044
TL;DR: The information currently available on the properties and catalytic functions of the four known selenium-dependent enzymes is summarized and formate dehydrogenases of Escherichia coli and several anaerobic bacteria, clostridial glycine reductase, mammalian and avian glutathione peroxidase, and nicotinic acid hydroxylase of Clostridium barkeri are mentioned.
Abstract: Selenium, molecular weight 78.96, resembles sulfur in many of its chemical properties and occurs in inorganic forms as H2Se, H2Se2O3, H2SeO3, and H2SeO4 which are the analogues of hydrogen sulfide, thiosulfate, sulfite, and sulfate, respectively. The commonly available radionuclide, 75Se, is a gamma emitter (half-life 122 days) that is used extensively as a tracer in biochemical studies and as a radiopharmaceutical agent for diagnostic purposes. Organoselenium compounds, in general, are less stable and more reactive than the corresponding sulfur analogues and these properties may account for the toxicity of selenium when it is incorporated indiscriminately in place of sulfur in cellular constituents. On the other hand living systems may have exploited the greater reactivity of certain types of organoselenium compounds in those instances where selenium is specifically required as a component of an enzyme or other macromolecule. Several enzymic processes that do not distinguish selenium from sulfur and therefore may be important in selenium toxicity were discussed in some detail in two earlier reviews on selenium biochemistry (1, 2) and this aspect of the problem is not treated here. Rather, the information currently available on the properties and catalytic functions of the four known selenium-dependent enzymes is summarized. These enzymes are formate dehydrogenases of Escherichia coli and several anaerobic bacteria, clostridial glycine reductase, mammalian and avian glutathione peroxidase, and nicotinic acid hydroxylase of Clostridium barkeri. Additional selenoproteins whose catalytic activities are as yet unidentified are mentioned.
TL;DR: Three new monocyclic Cascade systems are reported to have been developed that combine 3-Hydroxy-3-Methylglutaryl CoA Reductase Cascade with Glycogen Phosphorylase-Glycogen Synthase System.
Abstract: MONOCYCLIC CASCADE SYSTEMS . Mammalian Pyruvate Dehydrogenase . ADP-Ribosylation . Other Monocyclic Cascade Systems . MULTICYCLIC CASCADE SYSTEMS . Coordinated Glycogen Phosphorylase-Glycogen Synthase System .. 3-Hydroxy-3-Methylglutaryl CoA Reductase Cascade .. Glutamine Synthetase Cascade .
TL;DR: RNA-PRIMED SYNTHESIS of Nascent DNA FRAGments in VARIOUS ORGANISMS in V Variety of Organisms is studied.
Abstract: PERSPECTIVES AND SUMMARY ...... . . .. . . . . . . . . . .. . . . .. . ... ... . . . . . . . . . . . . . .. ... . . .. . . . . . . . . . NASCENT DNA FRAGMENT: A UNIT OF DNA REPLICATION . CHAIN INITIATION OF NASCENT DNA . METHODS USED FOR DETECTION OF PRIMER RNA . Buoyant Density Shift . Phosphate Transfer from Deoxyribonucleotides to Neighboring Ribonucleotides . The Spleen Exonuclease Assay . The Polynucleotide Kinase Assay . Liberation of Radioactive Primer RNA by DNase Digestion . In Vivo Sealing of Nascent Chains . RNA-PRIMED SYNTHESIS OF NASCENT DNA FRAGMENTS IN VARIOUS ORGANISMS . Bacteriophage T7 .
TL;DR: The Three-DIMENSIONAL STRUCTURE of PHOSPHORYLASE is presented, highlighting the importance of the three components of the structure and their role in the synthesis and regulation in the regulation of activity.
Abstract: PERSPECTIVES AND SUMMARY .. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . HISTORICAL INTRODUCTION .. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . Physiological Role and Metabolic Regulation of Activity . . . .... ... . . .... . . .. . . .. .. . . .. . Subunit Relationships . Chemical Studies . Kinetics and Mechanism . ..... . . . . . . .. .. . .. . . . . . . . . . . . .. . . .. . . .. .. .. . . . . .. . . .. . . . Allosteric Conformational Transitions and Physicochemical Probes .. Amino Acid Sequences . THE PRIMARY STRUCTURE OF PHOSPHORYLASE . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . Strategic Approach to the Research Problem ..... . ...... ...... . The Amino Acid Sequence and Location of Special Residues ......... . . . . . .. . . .. ... . . . . Sequence Homologies . . . . . .. . . .. . . . . .... . . . . ....... .... . ....... . THE THREE-DIMENSIONAL STRUCTURE OF PHOSPHORYLASE a . X-ray and Electron Microscope Studies of Quaternary Structure and Subunit Shape .... . Crystal Forms of Phosphorylase . ... . . . . . . . ..... . . . . . . . . . ....... . . . . . . . . . ..... . . . Description of the Molecule . . . . . . .. . . . . . . .. .. .. . . . . ........ . . . . . . . . . . . . . . Pyridoxal Phosphate . . . . . . . . . ..... . .... . . . .... .... . ... . ... . . . Ser-14 Phosphate . FUNCTIONAL AND BIOLOGICAL SIGNIFICANCE OF THE STRUCTURE Ligand Binding Sites .... . . Glycogen binding . . . . . . . . . .. . . .. ... . . . . .. . . . . . . . . . . . .. . . . . . . . . . . . . . . . . . . . . . . . . . +12034
TL;DR: A comparison study of the Nucleated Polymerization Model and its applications in the assembly process finds that T and HMW-MAPs specijic is a viable alternative for HMW fraction fractionation.
Abstract: PERSPECTIVES AND SUMMARY . METHODOLOGY .... : . . EQUILIBRIA IN THE ASSEMBLY PROCESS . Nucleated Polymerization Model . Is Tubulin Competent to Assemble? ; . . . . . ... . . . . . ... . . . . . . . . . . . . . .. CHEMICAL CHARACTERISTICS OF THE MICROTUBULE ASSEMBLY PROCESS .. . . . . . . . . ..... . . . . . . . . . . . . . . ........ . . . . . . . . . . . . . . . . . . ..... . . . . . . . .. . . . . . . . . . . . ......... .. . Role of Solvent Components . Role of Nontubulin Proteins . T factor : ..... ......... ....... . . ..... . Map or HMW fraction .. Are T and HMW-MAPs specijic? . Role of Nucleotides . Involvement of GTP . Mechanism of GTP action . GTPase Activity of tubulin ..... ........ . . . . ... ..... . . . . ..... . . . . .... . . . . . . ... . . . ... . . . . . . . . . ... . . ... . . . . . ... ..... . Role of Covalent Modifications of Tubulin . . Phosphorylation and kinase activity . SH groups . Tyroslation ... . MECHANISM OF MICROTUBULE ASSEMBLy .. Initiation .
TL;DR: The present work presents a meta-analysis of yeast chromosomol genes that highlights the importance of knowing the carrier and removal status of canine coronavirus, as a source of infection for other animals.
Abstract: PROSPECTIVES AND SUMMARY 845 GENETIC ANALYSIS IN yEAST 846 Tetrad Analysis 846 New Advances in Genetic Analysis 850 Construction of recombinant DNA molecules 850 Identification of cloned genes 850 Yeast transformation 854 ORGANIZATION AND REPLICATION OF THE YEAST CHROMOSOMES 856 Chromosome Structure 858 Chromosome Replication 860 Structure of replicating nuclear DNA molecules 860 Control of DNA synthesis 862 Yeast DNA polymerases .. ... ... ........ ... ..... 864 ANALYSIS OF SPECIFIC CLASSES OF CHROMOSOMAL GENES 864 Structural Analysis of Single-Copy Genes 865 Repeating Chromosomal Genes 866 Yeast ribosomal DNA genes 866 Structure of yeast tRNA genes 867 Other repeating yeast chromosomol genes 868 STRUCTURE AND REPLICATION OF THE 2p.m PLASMIDS 869 CONCLUSIONS AND FUTURE PROSPECTS 871
TL;DR: The 4Fe-4S Cluster and Cluster Oxidation States have shown the ability to modify the geometry of the chiral stationary phase of the EPR to change the intensity of the response of the H2O/O2 molecule.
Abstract: PERSPECTIVES AND SUMMARY 140 SPECTRAL PROPERTIES ... .... ....... ...... ..... ........ ... 142 Optical 142 Magnetic .. ..... .. ... 143 EPR 143 NMR 146 Spectral Identification of Cluster Type 149 THE NATURE OF THE 4Fe-4S CLUSTER ..... 149 The (4Fe-4S}2+ Cluster .. 150 The (4Fe-4Sr Cluster 150 The (4Fe-4S)1+ Cluster 151 THE INFLUENCE OF THE POLYPEPTIDE CHAIN ON THE REDUCTION POTENTIAL ...... ... .. .. .... : 152 Selection of the Functioning Cluster Oxidation States . . . . . . .. . . . . . . .. . . . . . . . . . . . . . . . 152 Variation of the Reduction Potential Between a Selected Pair of Cluster Oxidation States .... .. . ......... ..... ......... ......... 154 Magnitude of the influence .. ......... . . . . . . . . . . . . . ....... . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 154 Mechanisms of influence 155 An Overview 158 OTHER FUNCTIONS OF THE POLYPEPTIDE CHAIN ..... 158
TL;DR: The role of the A TPase in Proton Translocation and Photophosphorylation, and the Catalytic Route for both Synthesis and Hydrolysis of A TP, are studied.
Abstract: PERSPECfIVES AND SUMMARY . PROPERTIES OF THE CHLOROPLAST COUPLING FACTOR COMPONENT . Structure and Composition . Catalytic Properties . . . ..... . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . Restoration of Photophosphorylation . OTHER COMPONENTS OF THE ATPase COMPLEX . TIGHTLY BOUND NUCLEOTIDES ON CF, .. Isolated CFI . Membrane Bound CFI . BINDING, DISSOCIATION, AND EXCHANGE OF NUCLEOTIDES .. Latent and Activated Isolated CFI .. Membrane Bound CFI ........ . MECHANISM OF ATP FORMATION . Role of the A TPase in Proton Translocation and Photophosphorylation . Energy-Dependent Conformational Changes of the ATPase Complex .. Sites Invofved in the Catalytic Functions of tlie A TPase Complex . Initial Phosphate Acceptor and the Role of Bound Nue/eotides .. Catalytic Route for both Synthesis and Hydrolysis of A TP .. .12037
TL;DR: Pterin-Dependent Hydraxy/ations at the Oxidation Level of Formaldehyde and Reaction of the One-Carbon Unit at the Methyl Leve/ of Oxidation and Reductases.
Abstract: Perspectives and Summary 227 Structure 228 Reductases 230 One-Carbon Unit Transfer at the Oxidation Level of Formaldehyde ...... 233 One-Carbon Unit Transfer at the Oxidation Level of Formate 240 Reaction of the One-Carbon Unit at the Methyl Leve/ of Oxidation 244 Pterin-Dependent Hydraxy/ations 245
TL;DR: The aim of this monograph is to establish a chronology of Papovavirus infections, their mechanisms, and the role of Sequence Homologies in Expediting Integration.
Abstract: PAPOVAVIRUSES AND THEIR INTEGRATED GENOMES . Biology of Papovavirus Infections . Molecular Characterization of Integrated Papovavirus Genomes . Does Integration Occur During the Lytic, Replicative Cycle? .. Does the Act of Integration Induce Transformation? .. Do Papovavirus Genomes Encode Proteins Responsible for Integration? .. Recombinational Mechanisms of Papovavirus Integration .. Role of Sequence Homologies in Expediting Integration .. Defective Interfering (DI) Particles and Integration . Excision of Integrated Papovavirus Genomes .
TL;DR: One evening in the late nineteen forties my wife and I were at a party given in honor of Otto Loewi and Sir Henry Dale, corecipients of the 1936 Nobel Prize in Medicine for their discovery of the chemical transmission of the nerve impulse.
Abstract: One evening in the late nineteen forties my wife and I were at a party given in honor of Otto Loewi and Sir Henry Dale, corecipients of the 1936 Nobel Prize in Medicine for their discovery of the chemical transmission of the nerve impulse. We were all asked to sign the guest book and state our hobby and I did this as Sir Henry looked over my shoulder. As I put down my hobby as Biochemistry he roared with laughter. At that time I was Professor of Pharmacology and Chairman of the Department at the New York University School of Medicine and Sir Henry said, “now that he is a pharmacologist, he has biochemistry as a hobby.” I tell this story to justify the title of this essay, because in my life biochemistry has been my only and real hobby.