bluuebunny/crossref_metadata_2025_split huggingface dataset:
Photoproteins as Reporters in Whole‐cell Sensing
Authors: Feliciano Jessika , Pasini Patrizia , Deo Sapna K. , Daunert Sylvia 
Published: March 2008

AbstractOriginally published in: Photoproteins in Bioanalysis. Edited by Sylvia Daunert and Sapna K. Deo. Copyright © 2006 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31016‐6The sections in this article areIntroductionBiosensors Using Intact CellsReporter Genes in Genetically Engineered Whole‐cell SensorsThe LuciferasesBacterial LuciferasesluxABBioreportersluxCDABEBioreportersNaturally Luminescent BioreportersEukaryotic LuciferasesFirefly LuciferaseSea Pansy LuciferaseAequorinFluorescent ProteinsGreen Fluorescent ProteinRed Fluorescent ProteinMultiplexingApplicationsStress Factors and GenotoxicantsEnvironmental PollutantsQuorum‐sensing Signaling MoleculesAntibioticsTechnological AdvancesAcknowledgments
Catalytic Antibody Technology
Authors: Hilvert Donald 
Published: March 2008

AbstractOriginally published in: Catalytic Antibodies. Edited by Ehud Keinan. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30688‐6The sections in this article areIntroductionExploiting Antibodies as CatalystsCatalytic EfficiencyHapten DesignRepresentative Catalytic AntibodiesProximity EffectsSigmatropic RearrangementsCycloadditionsStrainFerrochelatase MimicsOther SystemsElectrostatic CatalysisAcyl Transfer ReactionsFunctional GroupsAldolasesPerspectivesGeneral Lessons from Comparisons of Enzymes and AntibodiesHow efficient does catalysis need to be?Strategies for Optimizing EfficiencyBetter HaptensScreeningEngineeringSelectionOther ScaffoldsConclusionsAcknowledgements
Structure and Function of Catalytic Antibodies
Authors: Larsen Nicholas A. , Wilson Ian A. 
Published: March 2008

AbstractOriginally published in: Catalytic Antibodies. Edited by Ehud Keinan. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30688‐6The sections in this article areIntroductionElectrostatic ComplementarityAnionic Binding Motifs and Ester HydrolysisStructural MotifsMechanistic ConsiderationsMechanistic PitfallsStructural and Functional Considerations for Hapten DesignAnionic Binding Motifs and Control of the Microenvironment in DecarboxylationAnionic Binding Motifs and the Periodate Cofactor in Sulfide OxygenationCation Stabilization and Allylic IsomerizationShape Complementarity and ApproximationUnimolecular RearrangementsAntibody 1F7Antibody AZ‐28Bimolecular Rearrangements and the Diels‐Alder ReactionRetro‐Diels‐Alder ReactionDisfavoredexoDiels‐Alder ReactionEndoDiels‐Alder ReactionsShape Complementarity and Control of the Reaction CoordinateSyn‐EliminationDisfavored Ring ClosureSelective Control of a Reactive Carbocation: Antibodies 4C6 and 19A4Shape Complementarity and Substrate StrainReactive Amino Acids and the Possibility of Covalent CatalysisConclusions
N‐terminal Ubiquitination
Authors: Ciechanover Aaron 
Published: March 2008

Abstract
Originally published in: Protein Degradation, Volume 1. Edited by R. John Mayer, Aaron Ciechanover and Martin Rechsteiner. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30837‐7

The ubiquitin–proteasome system (UPS) is involved in selective targeting of innumerable cellular proteins via a complex pathway that plays important roles in a broad array of processes. An important step in the proteolytic cascade is specific recognition of the substrate by one of many ubiquitin ligases, E3s, that is followed by generation of the polyubiquitin degradation signal. For most substrates, it is believed, though it has not been shown directly, that the first ubiquitin moiety is conjugated, via its C‐terminal Gly
76
residue, to an ɛ‐NH
2
group of an internal lysine residue. Recent findings indicate that for an increasing number of proteins, the first ubiquitin moiety is fused linearly to the α‐NH
2
group of the N‐terminal residue. An important biological question relates to the evolutionary requirement for an alternative mode of ubiquitination.
The COP9 Signalosome and Its Role in the Ubiquitin System
Authors: Bech‐Otschir Dawadschargal , Kapelari Barbara , Dubiel Wolfgang 
Published: March 2008

Abstract
Originally published in: Protein Degradation, Volume 1. Edited by R. John Mayer, Aaron Ciechanover and Martin Rechsteiner. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30837‐8
The sections in this article are

Introduction

Discovery of the CSN

Architecture of the CSN

CSN Subunit–Subunit Interactions

CSN‐subunit Interactions With Other Proteins

PCI and MPN

Biochemical Activities Associated With the CSN

Deneddylation Activity

Protein Kinases

Associated Protein Kinases

Deubiquitinating Enzymes

Ubiquitin Ligases

Association of the CSN With Other Protein Complexes

The eIF3 Complex

The Proteasome

Biological Functions of the CSN

Regulation of Ubiquitin Conjugate Formation

Cell‐cycle and Checkpoint Control

DNA Repair

Developmental Processes

Tumor Angiogenesis

Conclusions

Acknowledgment
Molecular Chaperones and the Ubiquitin–Proteasome System
Authors: Patterson Cam , Höhfeld Jörg 
Published: March 2008

AbstractOriginally published in: Protein Degradation, Volume 2. Edited by R. John Mayer, Aaron Ciechanover and Martin Rechsteiner. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31130‐0A role for the ubiquitin–proteasome system in the removal of misfolded and abnormal proteins is well established. Nevertheless, very little is known about how abnormal proteins are recognized for degradation by the proteasome. Recent advances suggest that substrate recognition and processing require a close cooperation of the ubiquitin–proteasome system with molecular chaperones. Chaperones are defined by their ability to recognize nonnative conformations of other proteins and are therefore ideally suited to distinguish between native and abnormal proteins during substrate selection. Here we discuss molecular mechanisms that underlie the cooperation of molecular chaperones with the ubiquitin–proteasome system. Advancing our knowledge about such mechanisms may open up opportunities to modulate chaperone–proteasome cooperation in human diseases.The sections in this article areIntroductionA Biomedical PerspectiveMolecular Chaperones: Mode of Action and Cellular FunctionsThe Hsp70 FamilyThe Hsp90 FamilyThe Small Heat Shock ProteinsChaperoninsChaperones: Central Players During Protein Quality ControlChaperones and Protein DegradationThe CHIP Ubiquitin Ligase: A Link Between Folding and Degradation SystemsOther Proteins That May Influence the Balance Between Chaperone‐assisted Folding and DegradationFurther ConsiderationsConclusions
Ubiquitin‐conjugating Enzymes
Authors: Eddins Michael J. , Pickart Cecile M. 
Published: March 2008

AbstractOriginally published in: Protein Degradation, Volume 1. Edited by R. John Mayer, Aaron Ciechanover and Martin Rechsteiner. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30837‐8The sections in this article areIntroductionHistorical BackgroundWhat is an E2?Functional Diversity of Ubiquitin‐conjugating EnzymesFunctions Related to Proteasome ProteolysisEndocytosis and TraffickingNon‐proteolytic FunctionsE2s of Uncertain FunctionE2 Enzymes and DiseaseE2 Enzymes Dedicated to Ubiquitin‐like Proteins (UbLs)The Biochemistry of E2 EnzymesE1 InteractionInteractions with Thiol‐linked UbiquitinE3 InteractionsRING E3/E2 InteractionsU‐box E3/E2 InteractionsHECT E3/E2 InteractionsE2/Substrate InteractionsE2 Catalysis MechanismFunctional Diversification of the E2 FoldConclusions
The Deubiquitinating Enzymes
Authors: Russell Nathaniel S. , Wilkinson Keith D. 
Published: March 2008

Abstract
Originally published in: Protein Degradation, Volume 1. Edited by R. John Mayer, Aaron Ciechanover and Martin Rechsteiner. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30837‐8
The sections in this article are

Introduction

Structure and
In Vitro
Specificity of DUB Families

Ubiquitin C‐terminal Hydrolases (UCH)

Ubiquitin‐specific Processing Proteases (UBP/USP)

Ubiquitin‐like Specific Proteases (ULP)

OTU DUBs

JAMM Isopeptidases

DUB Specificity

Recognition of the Ub‐like Domain

Recognition of the gly–gly Linkage

Recognition of the Leaving Group

Substrate‐induced Conformational Changes

Localization of DUBs

Probable Physiological Roles for DUBs

Proprotein Processing

Salvage Pathways: Recovering Mono‐ubiquitin Adducts and Recycling Polyubiquitin

Regulation of Mono‐ubiquitination

Processing of Proteasome‐bound Polyubiquitin

Finding Substrates and Roles for DUBs

Roles of DUBs Revealed in Disease

NF‐κB Pathway

Neural Function

New Tools for DUB Analysis

Active‐site‐directed Irreversible Inhibitors and Substrates

Non‐hydrolyzable Polyubiquitin Analogs

Conclusion
The 26S Proteasome
Authors: Rechsteiner Martin 
Published: March 2008

Abstract
The 26S proteasome is a large ATP‐dependent protease composed of more than 30 different polypeptide chains. Like the ribosome, the 26S proteasome is assembled from two “subunits”, the 19S regulatory complex and the 20S proteasome. The 19S regulatory complex confers the ability to recognize and unfold protein substrates, and the 20S proteasome provides the proteolytic activities needed to degrade the substrates. The 26S proteasome is the only enzyme known to degrade ubiquitylated proteins, and it also degrades intracellular proteins that have not been marked by ubiquitin. The 26S proteasome is located in the nucleus and cytosol of eukaryotic cells, where the enzyme is responsible for the selective degradation of a vast number of important cellular proteins. Because rapid proteolysis is a pervasive regulatory mechanism, the 26S proteasome is essential for the proper functioning of many physiological processes.
Originally published in: Protein Degradation, Volume 1. Edited by R. John Mayer, Aaron Ciechanover and Martin Rechsteiner. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30837‐8
The sections in this article are

Introduction

The 20S Proteasome

Structure

Enzyme Mechanism and Proteasome Inhibitors

Immunoproteasomes

The 26S Proteasome

The Ubiquitin–Proteasome System

Ultrastructure of the 26S Proteasome and Regulatory Complex

The 19S Regulatory Complex

ATPases of the RC

The non‐ATPase Subunits

Biochemical Properties of the Regulatory Complex

Nucleotide Hydrolysis

Chaperone‐like Activity

Proteasome Activation

Ubiquitin Isopeptide Hydrolysis

Substrate Recognition

Substrate Recognition by Proteasomes

Degradation Signals (Degrons)

Ubiquitin‐dependent Recognition of Substrates

Substrate Selection Independent of Ubiquitin

Proteolysis by the 26S Proteasome

Presumed Mechanism

Contribution of Chaperones to Proteasome‐mediated Degradation

Substrate Binding to the 26S Proteasome

Translocation of the Polypeptide Substrate to the Central Proteolytic Chamber

Processing by the 26S Proteasome

Proteasome Biogenesis

Subunit Synthesis

Biogenesis of the 20S Proteasome

Biogenesis of the RC

Post‐translational Modification of Proteasome Subunits

Assembly of the 26S Proteasome

Proteasome Activators

REGs or PA28s

REGs

PA200

Hybrid Proteasomes

ECM29

Protein Inhibitors of the Proteasome

Physiological Aspects

Tissue and Subcellular Distribution of Proteasomes

Physiological Importance

Conclusions
Molecular Machines for Protein Degradation
Authors: Bochtler Matthias , Groll Michael , Brandstetter Hans , Clausen Tim , Huber Robert 
Published: March 2008

AbstractOriginally published in: Protein Degradation, Volume 1. Edited by R. John Mayer, Aaron Ciechanover and Martin Rechsteiner. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30837‐8The sections in this article areIntroductionThe ATP‐dependent Protease HslVUHslVU Physiology and BiochemistryHslV PeptidaseHslU ATPaseThe HslVU–Protease ComplexAllosteric ActivationA Comparison of HslVU with ClpXP and ClpAPHslVU Peptidase as a Model for the Eukaryotic 26S Proteasome?The Yeast 20S ProteasomeThe Proteasome, a Threonine ProteaseInhibiting the ProteasomeAccess to the Proteolytic ChamberThe Tricorn Protease and its Structural and Functional Relationship with Dipeptidyl Peptidase IVArchitecture of the Tricorn ProteaseCatalytic Residues and MechanismSubstrate Access and Product Egress Through β‐propellersStructural and Functional Relationship of Tricorn and DPIVThe DegP Protease Chaperone: A Molecular Cage with BouncersThe DegP Protomer, a PDZ ProteaseThe Two Forms of the DegP HexamerDegP, a ChaperoneThe Protease FormWorking Model for an ATP‐independent Heat‐shock ProteinAcknowledgment
Protein Sorting to the Lysosome
Authors: McCullough John , Clague Michale J. , Urbé Sylvie 
Published: March 2008

AbstractOriginally published in: Protein Degradation, Volume 3. Edited by R. John Mayer, Aaron Ciechanover and Martin Rechsteiner. Copyright © 2006 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31435‐0The sections in this article areIntroductionIdentification of Ubiquitin as an Endosomal Sorting SignalUbiquitin‐mediated Sorting at the Endosome: The MVB Sorting MachineryEndosome‐associated Ubiquitin Interacting Domains: Structure and FunctionThe Hrs‐STAM Complex and the Endosomal Clathrin CoatGGA and Tom1: Alternative Sorting Adapters?The ESCRT MachineryVps4‐SKD1Ubiquitin Ligases and Endosomal SortingNedd4 Familyc‐CblEndosomal DUBsUbp1 and Ubp2Doa4UBPYAMSHPolyubiquitin Linkages and EndocytosisProteasome Involvement in Endocytic SortingK63‐linked UbiquitinConclusionsAcknowledgements
Regulation of Proteolysis at the Proteasome Portal
Authors: Bajorek Monika , Glickman Michael H. 
Published: March 2008

AbstractThe proteolytic active sites of the 26S proteasome are sequestered within the central chamber of its 20S catalytic core particle. Access to this chamber is through a narrow channel defined by the outer alpha subunits. An intricate lattice of interactions anchors the N‐termini of these alpha subunits, blocking access to the channel in free 20S core particles of eukaryotes. Entry of substrates can be enhanced by attachment of activators or regulatory particles to the proteolytic 20S core. Regulatory particles rearrange the blocking residues to form an open pore and promote substrate entry into the proteolytic chamber. Channel gating is apparently partially rate limiting for proteasome activity, as facilitating substrate entry in the open channel state leads to enhanced overall proteolysis rates. Interestingly, some substrates, particularly hydrophobic ones, can activate gate opening themselves, thus facilitating their own destruction. Properties of channel gating and the interactions required to maintain stable closed and open conformations and their consequences for proteasome function are discussed.Originally published in: Protein Degradation, Volume 2. Edited by R. John Mayer, Aaron Ciechanover and Martin Rechsteiner. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31130‐0The sections in this article areBackgroundThe Importance of Channel GatingA Porthole into the ProteasomeThe Closed StateThe Open StateFacilitating Traffic Through the Gated ChannelRegulatory ComplexesSubstrate‐facilitated TrafficConclusions
Tailoring Protein Scaffolds for Ligand Recognition
Authors: Skerra A. 
Published: March 2008

AbstractOriginally published in: Protein‐Ligand Interactions.Edited by Hans‐Joachim Böhm, Gisbert Schneider. Copyright © 2003 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30521‐6The sections in this article areIntroductionLipocalins: A Class of Natural Compound CarriersAnticalins: Lipocalins Reshaped via Combinatorial BiotechnologyStructural Aspects of Ligand Recognition by Engineered LipocalinsProspects and Future Applications of Anticalins
Evolutionary Generation of Enzymes with Novel Substrate Specificities
Authors: Bornscheuer Uwe T. 
Published: March 2008

Abstract
Originally published in: Directed Molecular Evolution of Proteins. Edited by Susanne Brakmann, Kai Johnsson. Copyright © 2002 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30423‐1
The sections in this article are

Introduction

General Considerations

Examples

Group 1

Group 2

Group 3

Conclusions

Acknowledgements
Design of Restriction Endonucleases with Novel Specificity
Authors: Lanio Thomas , Jeltsch Albert , Pingoud Alfred 
Published: March 2008

AbstractOriginally published in: Directed Molecular Evolution of Proteins. Edited by Susanne Brakmann, Kai Johnsson. Copyright © 2002 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30423‐1The sections in this article areIntroductionBiology of restriction/modification systemsBiochemical properties of type II restriction endonucleasesApplications for type II restriction endonucleasesSetting the stage for protein engineering of type II restriction endonucleasesDesign of Restriction Endonucleases with New SpecificitiesRational designAttempts to employ rational design to change the specificity of restriction enzymesChanging the substrate specificity of type IIs restriction enzymes by domain fusionRational design to extend specificities of type II restriction enzymesEvolutionary design of extended specificitiesConclusionsAcknowledgements
Protein Engineering by Evolutionary Methods
Authors: Lutz Stefan , Benkovk* Stephen J. 
Published: March 2008

Abstract
Originally published in: Directed Molecular Evolution of Proteins. Edited by Susanne Brakmann, Kai Johnsson. Copyright © 2002 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30423‐1
The sections in this article are

Introduction

Mechanisms of Protein Evolution in Nature

Gene duplication

Tandem duplication

Proteases

βα‐barrels

Circular permutation

Oligomerization

Gene fusion

Domain recruitment

Substrate specificity

Regulation

Chemistry

Exon shuffling

Engineering Genes and Gene Fragments

Protein fragmentation

Rational swapping of secondary structure elements and domains

Combinatorial gene fragment shuffling

DNA shuffling

Homology‐independent fragment swapping

Homology‐independent fragment shuffling

Modular recombination and protein folding

Rational domain assembly – engineering zinc fingers

Combinatorial domain recombination – exon shuffling

Gene Fusion – From Bi‐ to Multifunctional Enzymes

End‐to‐end gene fusions

Gene insertions

Modular design in multifunctional enzymes

Conclusions

Acknowledgements
Engineered Nanopores
Authors: Bayley Hagan , Braha Orit , Cheley Stephen , Gu Li‐Qun 
Published: March 2008

AbstractOriginally published in: Nanobiotechnology. Edited by Christof M. Niemeyer and Chad A. Mirkin. Copyright © 2004 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30658‐9The sections in this article areOverviewWhat is a Nanopore?Engineering NanoporesWhat Can a Nanopore Do?What are the Potential Applications of Nanopores?Keeping Nanopores HappyMethodsProtein ProductionProtein EngineeringElectrical RecordingOther SystemsOutlookRugged PoresSupported BilayersMembrane ArraysAlternative Protein PoresPores with New Attributes and ApplicationsTheoryAcknowledgments
Design and Stability of α‐Helices
Authors: Doig Andrew J. , Errington Neil , Iqbalsyah Teuku M. 
Published: March 2008

Abstract
Originally published in: Protein Folding Handbook. Part I. 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

Structure of the α‐Helix

Capping Motifs

Metal Binding

The 3
10
‐Helix

The π‐Helix

Design of Peptide Helices

Host–Guest Studies

Helix Lengths

The Helix Dipole

Acetylation and Amidation

Side Chain Spacings

Solubility

Concentration Determination

Design of Peptides to Measure Helix Parameters

Helix Templates

Design of 3
10
‐Helices

Design of π‐helices

Helix Coil Theory

Zimm‐Bragg Model

Lifson‐Roig Model

The Unfolded State and Polyproline II Helix

Single Sequence Approximation

N‐ and C‐Caps

Capping Boxes

Side‐chain Interactions

N1, N2, and N3 Preferences

Helix Dipole

3
10
‐ and π‐Helices

AGADIR

Lomize‐Mosberg Model

Extension of the Zimm‐Bragg Model

Availability of Helix/Coil Programs

Forces Affecting α‐helix Stability

Helix Interior

Caps

Phosphorylation

Noncovalent Side‐chain Interactions

Covalent Side‐chain interactions

Capping Motifs

Ionic Strength

Temperature

Trifluoroethanol

p
K
a
Values

Relevance to Proteins

Acknowledgments
Design and Stability of Peptide β‐sheets
Authors: Searle Mark S. 
Published: March 2008

AbstractOriginally published in: Protein Folding Handbook. Part I. 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 areIntroductionβ‐Hairpins Derived from Native Protein SequencesRole of β‐turns in Nucleating β‐hairpin FoldingIntrinsic ϕ, Ψ Propensities of Amino AcidsSide‐chain Interactions and β‐hairpin StabilityAromatic Clusters Stabilize β‐hairpinsSalt Bridges Enhance Hairpin StabilityCooperative Interactions in β‐sheet Peptides: Kinetic Barriers to FoldingQuantitative Analysis of Peptide FoldingThermodynamics of β‐hairpin FoldingMultistranded Antiparallel β‐sheet PeptidesConclusions
Engineering Proteins for Stability and Efficient Folding
Authors: Schimmele Bernhard , Plückthun Andreas 
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

Kinetic and Thermodynamic Aspects of Natural Proteins

The Stability of Natural Proteins

Different Kinds of “Stability”

Thermodynamic Stability

Kinetic Stability

Folding Efficiency

The Engineering Approach

Consensus Strategies

Principles

Examples

Structure‐based Engineering

Entropic Stabilization

Hydrophobic Core Packing

Charge Interactions

Hydrogen Bonding

Disallowed Phi‐Psi Angles

Local Secondary Structure Propensities

Exposed Hydrophobic Side Chains

Inter‐domain Interactions

Case Study: Combining Consensus Design and Rational Engineering to Yield Antibodies with Favorable Biophysical Properties

The Selection and Evolution Approach

Principles

Screening and Selection Technologies Available for Improving Biophysical Properties

In Vitro Display Technologies

Partial in Vitro Display Technologies

In Vivo Selection Technologies

Selection for Enhanced Biophysical Properties

Selection for Solubility

Selection for Protein Display Rates

Selection on the Basis of Cellular Quality Control

Selection for Increased Stability

General Strategies

Protein Destabilization

Selections Based on Elevated Temperature

Selections Based on Destabilizing Agents

Selection for Proteolytic Stability

Conclusions

Acknowledgements
Protein‐based Artificial Enzymes
Authors: Duckworth Ben , Distefano Mark D. 
Published: March 2008

Abstract
Originally published in: Artificial Enzymes. Edited by Ronald Breslow. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31165‐1
The sections in this article are

Introduction

Artificial Nucleases Based on DNA and RNA Binding Proteins

Introduction

Artificial Nucleases from Native Protein Scaffolds

OP Nuclease Design by Mutagenesis and Chemical Modification

Additional Applications for OP Conjugates

A Fe‐EDTA Artificial Nuclease

Concluding Remarks

Catalysts Based on Hollow Lipid‐binding Proteins

Lipid‐binding Proteins

Initial Work

Exploiting the Advantage of a Protein‐based Scaffold

Catalytic Turnover with Rate Acceleration

Modulation of Cofactor Reactivity with Metal Ions

Chemogenetic Approach

Adding Functional Groups within the Cavity

Scaffold Redesign

Hydrolytic Reactions

A Flavin‐containing Conjugate

Some Limitations

Myoglobin as a Starting Point for Oxidase Design

Artificial Metalloproteins and Myoglobin

Non‐covalent Attachment of a Redox Center

Dual Anchoring Strategy

Antibodies as Scaffolds for Catalyst Design

Antibodies as Specificity Elements

Incorporation of an Imidazole Functional Group into an Antibody for Catalysis

Comparison of Imidazole‐containing Antibodies Produced by Chemical Modification and Site‐directed Mutagenesis

Conclusions