bluuebunny/crossref_metadata_2025_split huggingface dataset:
Hsp70 Chaperones
Authors: Craig Elizabeth A. , Huang Peggy 
Published: March 2008

AbstractOriginally published in: Protein Folding Handbook. Part II. Edited by Johannes Buchner and Thomas Kiefhaber. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30784‐2The sections in this article areIntroduction“Soluble”Hsp70s/J‐proteins Function in General Protein FoldingThe SolubleHsp70 ofE.coli,DnaKSolubleHsp70sof Major Eukaryotic Cellular CompartmentsEukaryotic CytosolMatrix of MitochondriaLumen of the Endoplasmic Reticulum“Tethered”Hsp70s/J‐proteins: Roles in Protein Folding on the Ribosome and in Protein TranslocationMembrane‐tetheredHsp70/J‐proteinRibosome‐associatedHsp70/J‐proteinsModulating of Protein Conformation byHsp70s/J‐proteinsAssembly ofFe/SCentersUncoating of Clathrin‐coated VesiclesRegulation of the Heat Shock ResponseRegulation of Activity ofDNAReplication‐initiator ProteinsCases of a SingleHsp70 Functioning With MultipleJ‐ProteinsHsp70s/J‐proteins – When anHsp70 Maybe Isn't Really a ChaperoneThe Ribosome‐associated “Hsp70”Ssz1MitochondrialHsp70 as the Regulatory Subunit of an EndonucleaseConclusions
Protein Folding in the Endoplasmic Reticulum
Authors: Shen Ying , Chung Kyung Tae , Hendershot Linda M. 
Published: March 2008

AbstractOriginally published in: Protein Folding Handbook. Part II. Edited by Johannes Buchner and Thomas Kiefhaber. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30784‐2The sections in this article areIntroductionBiPInteractions with Unfolded ProteinsER‐localizedDnaJHomologuesER‐localized Nucleotide‐exchange/releasing FactorsOrganization and Relative Levels of Chaperones in theERRegulation ofERChaperone LevelsDisposal of BiP‐associated Proteins That Fail to Fold or AssembleOther Roles ofBiPin theERConclusionsAcknowledgements
Procollagen Biosynthesis in Mammalian Cells
Authors: Tasab Mohammed , Bulleid Neil J. 
Published: March 2008

Abstract
Originally published in: Protein Folding Handbook. Part II. Edited by Johannes Buchner and Thomas Kiefhaber. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30784‐2
The sections in this article are

Introduction

Variety and Complexity of Collagen Proteins

Fibrillar Procollagen

Expression of Fibrillar Collagens

The Procollagen Biosynthetic Process: An Overview

Disulfide Bonding in Procollagen Assembly

The Influence of Primary Amino Acid Sequence on Intracellular Procollagen Folding

Chain Recognition and Type‐specific Assembly

Assembly of Multi‐subunit Proteins

Coordination of Type‐specific Procollagen Assembly and Chain Selection

Hypervariable Motifs: Components of a Recognition Mechanism That Distinguishes Between Procollagen Chains?

Modeling the
C
‐propeptide

Chain Association

Posttranslational Modifications That Affect Procollagen Folding

Hydroxylation and Triple‐helix Stability

Procollagen Chaperones

Prolyl 4‐Hydroxylase

Protein Disulfide Isomerase

Hsp
47

PPI
and
Bi
P

Analysis of Procollagen Folding
The

E
.
coli

Gro
E
Chaperone
Authors: Burston Steven G. , Walter Stefan 
Published: March 2008

Abstract
Originally published in: Protein Folding Handbook. Part II. Edited by Johannes Buchner and Thomas Kiefhaber. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30784‐2
The sections in this article are

Introduction

The Structure of
Gro
EL

The Structure of
Gro
EL
‐
ATP

The Structure of
Gro
ES
and its Interaction with
Gro
EL

The Interaction Between
Gro
EL
and Substrate Polypeptides

Gro
EL
is a Complex Allosteric Macromolecule

The Reaction Cycle of the
Gro
E
Chaperone

The Effect of
Gro
E
on Protein‐folding Pathways

Conclusions

Acknowledgements
TheHsp90 Family of Molecular Chaperones
Authors: Richter Klaus , Meinlschmidt Birgit , Buchner Johannes 
Published: March 2008

AbstractOriginally published in: Protein Folding Handbook. Part II. Edited by Johannes Buchner and Thomas Kiefhaber. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30784‐2The sections in this article areIntroductionTheHsp90 Familyin vivoEvolutionary Relationships within theHsp90 Gene FamilyIn Vivo Functions ofHsp90Regulation ofHsp90 Expression and Posttranscriptional ActivationChemical Inhibition ofHsp90Identification of NaturalHsp90 SubstratesIn Vitro Investigation of the ChaperoneHsp90Hsp90: A Special Kind of ATPaseTheATPaseCycle ofHsp90Interaction ofHsp90 with Model Substrate ProteinsInvestigatingHsp90 Substrate Interactions Using Native SubstratesPartner Proteins: Does Complexity Lead to Specificity?Hop,p23, and PPIases: The Chaperone Cycle ofHsp90Hop/Sti1: Interactions Mediated by TPR Domainsp23/Sba1: Nucleotide‐specific Interaction withHsp90Large PPIases: Conferring Specificity to Substrate Localization?Pp5: Facilitating DephosphorylationCdc37: Building Complexes with KinasesTom70: Chaperoning Mitochondrial ImportCHIPandSgt1: Multiple Connections to Protein DegradationAha1 andHch1: Just Stimulating the ATPase?Cns1,Sgt2, andXap2: Is aTPREnough to Become anHsp90 Partner?ConclusionAcknowledgements
Small Heat Shock Proteins
Authors: Narberhaus Franz , Haslbeck Martin 
Published: March 2008

AbstractOriginally published in: Protein Folding Handbook. Part II. Edited by Johannes Buchner and Thomas Kiefhaber. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30784‐2The sections in this article areIntroductionα‐Crystallins and the Small Heat Shock Protein Family: Diverse Yet SimilarCellular Functions of α‐HspsChaperone Activityin vitroChaperone Functionin vivoOther FunctionsThe Oligomeric Structure of α‐HspsDynamic Structures as Key to Chaperone ActivityAcknowledgements
Transmemebrane Domains in Proteins
Authors: Ridder Anja , Langosch Dieter 
Published: March 2008

AbstractOriginally published in: Protein Folding Handbook. Part II. Edited by Johannes Buchner and Thomas Kiefhaber. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30784‐2The sections in this article areIntroductionStructure of Transmembrane DomainsThe Biosynthetic Route towards Folded and Oligomeric Integral Membrane ProteinsStructure and Stability ofTMSsAmino Acid Composition ofTMSs and Flanking RegionsStability of Transmembrane HelicesThe Nature of Transmembrane Helix‐Helix InteractionsGeneral ConsiderationsAttractive Forces within Lipid BilayersForces between Transmembrane HelicesEntropic Factors Influencing Transmembrane Helix‐Helix InteractionsLessons from Sequence Analyses and High‐resolution StructuresLessons from Bitopic Membrane ProteinsTransmembrane Segments Forming Right‐handed PairsTransmembrane Segments Forming Left‐handed AssembliesSelection of Self‐interactingTMSs from Combinatorial LibrariesRole of Lipids in Packing/Assembly of Membrane ProteinsConformational Flexibility of Transmembrane SegmentsExperimental TechniquesBiochemical and Biophysical TechniquesVisualization of Oligomeric States by Electrophoretic TechniquesHydrodynamic MethodsFluorescence Resonance TransferGenetic AssaysTheToxRSystemOther Genetic AssaysIdentification ofTMS‐TMSInterfaces by Mutational Analysis
The Structures of General Porins
Authors: Schulz Georg E. 
Published: March 2008

Abstract
Originally published in: Bacterial and Eukaryotic Porins. Edited by Roland Benz. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30775‐3
The sections in this article are

Bacterial Outer Membrane Proteins

Construction of General Porins

Trimer Association and Folding

Pore Geometry

Permeation

Conclusion

Acknowledgments
Lipid Bilayers, Translocons and the Shaping of Polypeptide Structure
Authors: White Stephen H. , Hessa Tara , von Heijne Gunnar 
Published: March 2008

AbstractOriginally published in: Protein‐Lipid Interactions. Edited by Lukas K. Tamm. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31151‐4The sections in this article areIntroductionMembrane Proteins: Intrinsic InteractionsPhysical Determinants of Membrane Protein Stability: The Bilayer MilieuPhysical Determinants of Membrane Protein Stability: Energetics of Peptides in BilayersPhysical Determinants of Membrane Protein Stability: Helix‐Helix Interactions in BilayersMembrane Proteins: Formative InteractionsConnecting Translocon‐assisted Folding to Physical Hydrophobicity Scales: The Interfacial ConnectionConnecting Translocon‐assisted Folding to Physical Hydrophobicity Scales: Transmembrane Insertion of HelicesConclusionsAcknowledgments
Expression of Proteins in Isotopically Enriched Form
Authors: Patzelt Heiko , Goto Natalie , Iwai Hideo , Lundstrom Kenneth , Fernholz Erhard 
Published: March 2008

AbstractOriginally published in: BioNMR in Drug Research. Edited by Oliver Zerbe. Copyright © 2002 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30465‐7The sections in this article areIntroductionIsotope‐Labeled Proteins from Hydrolyzates of the Green AlgaScenedesmus obliquusProduction of Isotope‐Labeled Algal HydrolyzatesAdaptation of the Protein Overproducer to the Algal MediumPreparation of Homogenously Isotope‐Labeled Protein by Fermentation on Algal MediaAmino Acid‐Type Specific LabelingMass Spectrometric Analysis of the Labeled Amino AcidsSelective Labeling SchemesReverse‐Labeling SchemesSelective Protonation of Methyl Groups in2H‐Labeled ProteinsStructure Determination of Selectively Methyl Protonated ProteinsIntroducing1H,12CAromatic Residues into Otherwise13CUniformly Labeled ProteinsBackbone‐Labeled ProteinsSelective13CMethyl Group LabelingIntein‐Based Protein Engineering forNMRSpectroscopySegmental Labeling of ProteinsIntein‐Mediated Protein Ligation (IPL)/Expressed Protein Ligation (EPL) using theIMPACTSystemReconstitution of Split InteinsStabilizing Proteins by Intein‐Mediated Backbone CyclizationIn vitroCyclization of ProteinsIn vivoCyclizationStability Enhancement by Backbone CyclizationAlternatives toE. coliExpression SystemsExpression VectorsHalobacteriumsalinarumSaccharomycescerevisiaeSchizosaccharomycespombePichiapastorisBaculovirusTransient Mammalian ExpressionStable Mammalian ExpressionViral VectorsComparison of Expression SystemsIsotope Labeling andNMRTarget ProteinsThe Use of Cell‐Free Protein Expression forNMRAnalysisThe Cell‐Free Protein Expression SystemRTSFromPCRProduct to15N‐Labeled ProteinConclusion
Monocot Expression Systems for Molecular Farming
Authors: Christou Paul , Stoger Eva , Twyman Richard M. 
Published: March 2008

Abstract
Originally published in: Molecular Farming. Edited by Rainer Fischer and Stefan Schillberg. Copyright © 2004 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30786‐9
The sections in this article are

Introduction

Cereal Production Crops

Technical Aspects of Molecular Farming in Cereals

Cereal Transformation

Expression Construct Design

Production Considerations for Cereals

Examples of Recombinant Proteins Produced in Cereals

ProdiGene and Maize

Recombinant Proteins Expressed in Rice

Recombinant Proteins Produced in Wheat

Recombinant Proteins Produced in Barley

Conclusions
Large‐scale Protein Production in Plants: Host Plants, Systems and Expression
Authors: Twyman Richard M. 
Published: March 2008

Abstract
Originally published in: Molecular Farming. Edited by Rainer Fischer and Stefan Schillberg. Copyright © 2004 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30786‐9
The sections in this article are

Introduction

Host Species for Molecular Farming

Leafy Crops

Tobacco (
Nicotiana tabacum
)

Tobacco (
Nicotiana benthamiana
)

Alfalfa (
Medicago sativa
)

White clover (
Trifolium repens
)

Lettuce (
Lactuca sativa
)

Spinach (
Spinacia oleracea
)

Lupin (
Lupinus spp
.)

Dry Seed Crops

Maize (
Zea mays
)

Rice (
Oryza sativa
)

Wheat (
Triticum aestivium
)

Barley (
Hordeum vulgare
)

Soybean (
Glycine max
)

Pea (
Pisum sativum
)

Pigeon pea (
Cajanus cajan
)

Peanut (
Arachis hypogaea
)

Fruit and vegetable crops

Potato (
Solanum tuberosum
)

Tomato (
Lycopersicon esculentum
)

Carrot (
Daucus carota
)

Banana (
Musa
spp.)

Oilcrops

Rapeseed/Canola (
Brassica napus
)

Falseflax (
Camelina sativa
)

Safflower (
Carthamus tinctorius
)

Unicellular Plants and Aquatic Plants Maintained in Bioreactors

Chlamydomonas reinhardtii

Physcomitrella patens

Duckweed (
Lemna minor
)

Non‐cultivated Model Plants

Arabidopsis thaliana

Expression systems for molecular farming

Transgenic plants

Transplastomic plants

Virus‐infected plants

Transiently transformed leaves

Hydroponic cultures

Hairy roots

Shooty teratomas

Suspension cell cultures

Expression strategies and protein yields

Conclusions
Plant Viral Expression Vectors
Authors: Yusibov Vidadi , Rabindran Shailaja 
Published: March 2008

AbstractOriginally published in: Molecular Farming. Edited by Rainer Fischer and Stefan Schillberg. Copyright © 2004 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30786‐9The sections in this article areIntroductionPlant RNA Viruses as Expression VectorsTobacco mosaic virus (TMV)Potato virus X (PVX)Cowpea mosaic virus (CPMV)Alfalfa mosaic virus (AlMV)Biological Activity of Target MoleculesEfficacy of Plant Virus‐produced AntigensVaccine AntigensParticle‐based Vaccine Antigen DeliveryOther Uses of Plant Virus ParticlesPlant Viruses as Gene Function Discovery ToolsNew Approaches to the Development of Viral VectorsConclusion
Foreign Protein Expression Using Plant Cell
Authors: Shadwick Fiona S. , Doran Pauline M. 
Published: March 2008

AbstractOriginally published in: Molecular Farming. Edited by Rainer Fischer and Stefan Schillberg. Copyright © 2004 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30786‐9The sections in this article areForeign Protein Production SystemsProduction of Foreign Proteins Using Plant Tissue CultureSuspended Cell CulturesHairy Root CulturesShooty Teratoma CulturesScale‐up Considerations for Different Forms of Plant Tissue CultureStrategies for Improving Foreign Protein Accumulation and Product Recovery in Plant Tissue CultureExpression SystemsModifications to Existing Expression ConstructsTransient Expression Using Viral VectorsSecretion of Foreign ProteinsForeign Protein StabilityStability Inside the CellsStability Outside the CellsMedium AdditivesMedium PropertiesBioprocess DevelopmentsProduct Recovery from the MediumOxygen Transfer and Dissolved Oxygen ConcentrationConclusions
Functional Expression of Ion Channels in Mammalian Systems
Authors: Clare Jeffrey J. 
Published: March 2008

AbstractOriginally published in: Expression and Analysis of Recombinant Ions Channels. Edited by Jeffrey J. Clare and Derek J. Trezise. Copyright © 2006 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31209‐2The sections in this article areIntroductioncDNACloning and ManipulationChoice of Host Cell BackgroundPost‐translational Processing of Heterologous Expressed Ion ChannelsCytotoxicityTransient Expression SystemsStandard Transient ExpressionViral Expression SystemsStable Expression of Ion ChannelsBicistronic Expression SystemsStable Expression of Multiple SubunitsInducible ExpressionConclusionsAcknowledgements
Production of Recombinant Proteins by In Vitro Folding
Authors: Lange Christian , Rudolph Rainer 
Published: March 2008

AbstractOriginally published in: Protein Folding Handbook. Part II. Edited by Johannes Buchner and Thomas Kiefhaber. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30784‐2The sections in this article areIntroductionThe Inclusion Body ProblemCost and Scale Limitations in Industrial Protein FoldingTreatment of Inclusion BodiesIsolation of Inclusion BodiesSolubilization of Inclusion BodiesRefolding in SolutionProtein Design ConsiderationsOxidative Refolding With Disulfide Bond FormationTransfer of the Unfolded Proteins Into Refolding BufferRefolding AdditivesCofactors in Protein FoldingChaperones and Folding‐helper ProteinsAn Artificial Chaperone SystemPressure‐induced FoldingTemperature‐leap TechniquesRecycling of AggregatesAlternative Refolding TechniquesMatrix‐assisted RefoldingFolding by Gel FiltrationDirect Refolding of Inclusion Body MaterialConclusionsExperimental ProtocolsAcknowledgements
Protein Production inEscherichia coli
Authors: Altenbuchner Josef , Mattes Ralf 
Published: March 2008

AbstractOriginally published in: Production of Recombinant Proteins. Edited by Gerd Gellissen. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31036‐4The sections in this article areIntroductionStrains, Genome, and CultivationExpression VectorsReplication of pMB1‐derived VectorsPlasmid PartitioningGenome EngineeringE. coliPromotersRegulation of Gene ExpressionNegative ControlPositive Controll‐Arabinose Operonl‐Rhamnose OperonTranscription and TranslationTranslation InitiationCodon UsageTranslation TerminationTranscription Termination and mRNA StabilityProtein ProductionInclusion Body FormationChaperones as Facilitators of FoldingFusion Protein TechnologyMethionine ProcessingSecretion into the PeriplasmDisulfide Bond Formation and FoldingTwin Arginine Translocation (TAT) of Folded ProteinsDisulfide Bond Formation in the CytoplasmCell Surface Display and Secretion across the Outer MembraneExamples of Products and ProcessesConclusionsAppendix
Protein Production in
Pseudomonas fluorescens
Authors: Chew Lawrence C. , Ramseier Tom M. , Retallack Diane M. , Schneider Jane C. , Squires Charles H. , Talbot Henry W. 
Published: March 2008

Abstract
Originally published in: Production of Recombinant Proteins. Edited by Gerd Gellissen. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31036‐4
The sections in this article are

Introduction

Biology of
Pseudomonas fluorescens

History and Taxonomy of
Pseudomonas fluorescens
Strain Biovar I MB101

Cultivation

Genomics and Functional Genomics of
P. fluorescens
Strain MB101

Core Expression Platform for Heterologous Proteins

Antibiotic‐free Plasmids using
pyrF
and
proC

Gene Deletion Strategy and Re‐usable Markers

Periplasmic Secretion and Use of Transposomes

Alternative Expression Systems: Anthranilate and Benzoate‐inducible Promoters

Production of Heterologous Proteins in
P. fluorescens

Pharmaceutical Proteins

Industrial Enzymes

Agricultural Proteins

Conclusions

Appendix
Protein Production inStaphylococcus carnosusand other Gram‐Positive Bacteria
Authors: Freudl Roland 
Published: March 2008

AbstractOriginally published in: Production of Recombinant Proteins. Edited by Gerd Gellissen. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31036‐4The sections in this article areIntroductionMajor Protein Export Routes in Gram‐positive BacteriaThe General Secretion (Sec) PathwayThe Twin‐Arginine Translocation (Tat) PathwaySecretion SignalsExtracytosolic Protein FoldingThe Cell Wall as a Barrier for the Secretion of Heterologous ProteinsDegradation of Exported Proteins by Cell‐associated and Secreted ProteasesStaphylococcus carnosusGeneral DescriptionMicrobiological and Molecular Biological ToolsS. carnosusas Host Organism for the Analysis of Staphylococcal‐related Pathogenicity AspectsSecretory Production of Heterologous Proteins byS. carnosusTheStaphylococcus hyicusLipase: Secretory Signals and Heterologous Expression inS. carnosusUse of the Pre‐pro‐part of theS. hyicusLipase for the Secretion of Heterologous Proteins inS. carnosusProcess Development for the Secretory Production of a Human Calcitonin Precursor Fusion Protein byS. carnosusSurface Display onS. carnosusAppendix
Protein Production inHansenulapolymorpha
Authors: Ah Kang Hyun , Gellissen Gerd 
Published: March 2008

AbstractOriginally published in: Production of Recombinant Proteins. Edited by Gerd Gellissen. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31036‐4The sections in this article areHistory, Phylogenetic Position, Basic Genetics and Biochemistry ofH.polymorphaCharacteristics of theH.polymorphaGenomeN‐linked Glycosylation inH.polymorphaTheH.polymorpha‐based Expression PlatformTransformationStrainsPlasmids and Available ElementsProduct and Process ExamplesConclusionLimitations of theH.polymorpha‐based Expression PlatformImpact of Functional Genomics on Development of theH.polymorphaRB11‐based Expression PlatformAppendix
Protein Production inPichia pastoris
Authors: Ilgen Christine , Lin‐Cereghino Joan , Cregg James M. 
Published: March 2008

AbstractOriginally published in: Production of Recombinant Proteins. Edited by Gerd Gellissen. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31036‐4The sections in this article areIntroductionConstruction of Expression StrainsExpression Vector ComponentsAlternative PromotersSelectable MarkersHost StrainsMethanol Utilization PhenotypeProtease‐deficient Host StrainsConstruction of Expression StrainsMulticopy StrainsGrowth in Fermentor CulturesPost‐translational Modification of Secreted ProteinsSecretion SignalsO‐linked GlycosylationN‐linked Glycosylation“Humanization” of N‐linked CarbohydrateConclusionsAcknowledgmentsAppendix
Protein Production inAspergillus sojae
Authors: Heerikhuisen Margreet , van den Hondel Cees , Punt Peter 
Published: March 2008

AbstractOriginally published in: Production of Recombinant Proteins. Edited by Gerd Gellissen. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31036‐4The sections in this article areIntroductionTaxonomyThe Expression PlatformStrain SelectionTransformationProtoplastingDominant Selection MarkersAuxotrophic Selection MarkersRe‐usable Selection MarkerPromoter ElementsAspergillus sojaeas a Cell Factory for Foreign ProteinsProduction of Fungal ProteinsProduction of Non‐fungal ProteinsControlled FermentationStrain DevelopmentProtease‐deficient StrainsUltra‐violet (UV) MutagenesisGene DisruptionControlled Batch FermentationsLow‐viscosity MutantsGene DisruptionControlled FermentationsConclusionAcknowledgmentsAppendix
Antibiotics and the Ribosome
Authors: Hansen Jeffrey L. 
Published: March 2008

AbstractOriginally published in: Protein Crystallography in Drug Discovery. Edited by Robert E. Babine and Sherin S. Abdel‐Meguid. Copyright © 2004 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30678‐7The sections in this article areIntroductionThe RibosomeIntroductionBinding of tRNAPeptidyl Transferase ActivityStructure of the RibosomeAntibioticsIntroductionAntibiotics that Bind to the 50S SubunitMLSBAntibioticsMacrolidesMacrolides, 15‐ and 16‐MemberedBinding Interactions Between the Lactone Ring and the RibosomeSugar Interactions with the RibosomeA Covalent BondMacrolides, 14‐MemberedRational Drug Design of MacrolidesLincosamidesStreptograminsChloramphenicolNucleoside Analogue AntibioticsPuromycinAminoacyl‐4‐aminohexosyl‐cytosine AntibioticsOther Antibiotics that Bind to the 50S SubunitSparsomycinAnisomycinProspects for Rational Drug Design of Antibiotics that Bind to the RibosomeAcknowledgments
Ribosome‐associated Proteins
Authors: Rospert Sabine , Gautschi Matthias , Rakwalska Magdalena , Raue Uta 
Published: March 2008

Abstract
Originally published in: Protein Folding Handbook. Part II. Edited by Johannes Buchner and Thomas Kiefhaber. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30784‐2
The sections in this article are

Introduction

Signal Recognition Particle, Nascent Polypeptide–associated Complex, and Trigger Factor

Signal Recognition Particle

An Interplay between Eukaryotic SRP and Nascent Polypeptide–associated Complex?

Interplay between Bacterial SRP and Trigger Factor?

Functional Redundancy: TF and the Bacterial Hsp70 Homologue DnaK

Chaperones Bound to the Eukaryotic Ribosome: Hsp70 and Hsp40 Systems

Sis1p and Ssa1p: an Hsp70/Hsp40 System Involved in Translation Initiation?

Ssb1/2p, an Hsp70 Homologue Distributed Between Ribosomes and Cytosol

Function of Ssb1/2p in Degradation and Protein Folding

Zuotin and Ssz1p: a Stable Chaperone Complex Bound to the Yeast Ribosome

A Functional Chaperone Triad Consisting of Ssb1/2p, Ssz1p, and Zuotin

Effects of Ribosome‐bound Chaperones on the Yeast Prion [
PSI
+
]

Enzymes Acting on Nascent Polypeptide Chains

Methionine Aminopeptidases

N
α
‐acetyltransferases

A Complex Arrangement at the Yeast Ribosomal Tunnel Exit