bluuebunny/crossref_metadata_2025_split huggingface dataset:
Force Generation in Molecular Motors
Authors: Oster George , Wang Hongyun 
Published: March 2008

Abstract
Originally published in: Molecular Motors. Edited by Manfred Schliwa. Copyright © 2003 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30594‐0
The sections in this article are

Introduction

A Brief Description of ATP Synthase Structure

The F
1
Motor: A Power Stroke

The F
0
Motor: A Brownian Ratchet

A Pure Brownian Ratchet

A Pure Power Stroke

Coupling and Coordination of Motors

Measures of Efficiency

Discussion

Appendix: Example Models to Illustrate the Difference between Ratchets and Power Strokes

Example 1: A power stroke without Brownian fluctuations

Example 2: A power stroke with Brownian fluctuations

Example 3: A Brownian ratchet that biases fluctuations

Example 4: A Brownian ratchet that rectifies fluctuations

A Closer Look at Binding Free Energy
Catalytic Antibodies as Mechanistic and Structural Models of Hydrolytic Enzymes
Authors: Lindner Ariel B. , Eshhar Zelig , Tawfik Dan S. 
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 areAbbreviationsIntroductionChapter OverviewCatalysis by Oxyanion Stabilization (OAS)Fidelity of TSA designEsterolytic Antibodies Based Solely on Oxyanion StabilizationAntibody Oxyanion HolesOxyanion holes–Antibodies vs. EnzymesAntibody Affinity and Rate Acceleration LimitationNucleophilic CatalysisEndogenous Nucleophiles in Hydrolytic AntibodiesReactive immunization (RI)Serendipity and 43C9 AntibodyExogenous Nucleophiles and Chemical Rescue in Hydrolytic AntibodiesGeneral Acid/Base Mechanisms in Hydrolytic AntibodiesMetal‐Activated Catalytic AntibodiesSubstrate DestabilizationThe Role of Conformational Changes in Catalytic AntibodiesConformational changes in catalytic antibodiesThe contribution of structural isomerization to catalysisConclusions
Chemical Microarrays for Small Molecule Ligand Screening
Authors: Metz G. , Ottleben H. , Vetter D. 
Published: March 2008

Abstract
Originally published in: Protein‐Ligand Interactions. Edited by Hans‐Joachim Böhm, Gisbert Schneider. Copyright © 2003 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30521‐6
The sections in this article are

Introduction

Fragment Approaches

Conceptual Ideas

Choice of Screening Fragments

Experimental Approaches

Chemical Microarrays

Background

On‐array Synthesis

Off‐array Synthesis and Spotting

Screening on Microarrays

Detection Technology

Protein Affinity Fingerprints

Conclusion

Acknowledgement
Single Molecule Measurements of Molecular Motors
Authors: Ishii Yoshiharu , Yanagida Toshio 
Published: March 2008

Abstract
Single molecule detection was developed to measure the unique operation of molecular motors. The function of molecular motors has been ascribed to the movement of a single motor molecule along a partner protein track. Manipulating single protein tracks and single motors and imaging single molecules has allowed the behaviour of such unitary machines to be measured. The mechanical responses to the energy input from the hydrolysis of ATP molecules have been determined and the underlying mechanism explored. The results indicate that the movement of molecular motors is driven by thermal motion rather than structural changes occurring in the motor molecules. Thermal Brownian motion must be biased in one direction. In this article, we summarize the methods and results of single molecule measurements of molecular motors.
Originally published in: Molecular Motors. Edited by Manfred Schliwa. Copyright © 2003 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30594‐0
The sections in this article are

Introduction

Manipulation of Actin Filaments

Nanometry of Actin Filaments

Movement of Actin Filaments Caused by Single Myosin Molecules

Visualization of Single Molecules

Visualization of ATP Turnover and Mechano‐chemical Coupling

Visualization of the Movement of Single Kinesin Motors

Visualization of the Processive Movement of Single Myosin Motors

Manipulation of Single Myosin Molecules with a Scanning Probe and Nanometry

Biased Brownian Movement

Conclusions
Analysis of Receptor‐Ligand Interaction
Authors: Höfliger M. M. , Beck‐Sickinger A. G. 
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 areReceptorsThe G‐Protein‐Coupled ReceptorsLigand‐binding TheoryCharacterization of the Receptor‐Ligand InteractionReceptor MaterialBinding StudiesBinding KineticsBinding AssaysSeparation AssaysRadioligand‐binding AssayFluorometric AssaysFluorescence LabelsFluorescence Correlation Spectroscopy (FCS)Fluorescence MicroscopyFluorescence Resonance Energy Transfer (FRET)Surface Plasmon ResonanceMolecular Characterization of the Receptor‐Ligand InteractionAntibodiesApplications of AntibodiesReceptor and Ligand DetectionReceptor CharacterizationFunctional Characterization of the Receptor‐Ligand InteractionAptamersReceptor Mutation and Ligand ModificationReceptor MutagenesisLigand ModificationCombination of Receptor Mutation and Ligand ModificationCross‐linkingConclusion
Protein Microarrays: Surface Chemistry and Coupling Schemes
Authors: Schäferling Michael , Kambhampati Dev 
Published: March 2008

AbstractOriginally published in: Protein Microarray Technology. Edited by Dev Kambhampati. Copyright © 2004 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30597‐1Efficient immobilization of biomolecules is a key factor in determining the overall success of a microarray or, for that matter, any high‐throughput (HTP) screening tool. If the immobilized probes are not correctly oriented on the microarray surface or are denatured, it can dramatically affect the downstream biomolecular interaction events. Here, various schemes for immobilizing biomolecules on glass, gold, polymer and semiconductor surfaces are described. In addition to tailoring the surface chemistry on the above substrates, various schemes for manipulating the probes with tags will also be addressed to achieve efficient and biocompatible screening platforms.The sections in this article areIntroductionBackground and Current State of Biomolecule LibrariesMicroarrays Based on Glass SubstratesSurface ModificationCurrent State of Glass‐Based Protein MicroarraysMicroarrays based on Gold SubstratesSurface ModificationsCurrent State of Gold‐based Protein MicroarraysMicroarrays based on Polymer SubstratesSurface ModificationsCurrent State of Polymer‐based MicroarraysSpecial Formats: Microfluidic Devices and Integrated Semiconductor ChipsChemical Immobilization Techniques for ProteinsCovalent Chemical CouplingPhotochemical Cross‐CouplingTagged ProteinsSite‐Specific Immobilization of AntibodiesConclusions
Surface Plasmon Resonance Imaging Measurements of Biomolecular Arrays
Authors: Wegner Greta J. , Lee Hye Jin , Corn Robert M. 
Published: March 2008

Abstract
Originally published in: Protein Microarray Technology. Edited by Dev Kambhampati. Copyright © 2004 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30597‐1
The sections in this article are

Introduction

Surface Plasmon Resonance Imaging

Surface Attachment Chemistries

SSMCC
Attachment Chemistry

SATP
Attachment Chemistry

SPR
Imaging Experiments Using Photopatterned Arrays

DNA
–
DNA
Hybridization

Mismatch Binding Protein,
Mut
S

Bacterial Response Regulators,
Omp
R
and
Van
R

SPR
Imaging Experiments of Arrays Created by Microfluidic Stencils

1‐D Peptide Array for Antibody Binding Measurements

2‐D
DNA
Array for
RNA
Hybridization

2‐D Peptide Array for Antibody Binding Measurements

2‐D Protein Array

Conclusions

Acknowledgments
Real‐time Characterization of
B
iomolecular Interactions using Biacore's Optical Biosensors
Authors: Franklin Gary , McWhirter Alan 
Published: March 2008

Abstract
Originally published in: Protein Microarray Technology. Edited by Dev Kambhampati. Copyright © 2004 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30597‐1
The sections in this article are

Introduction

The Proteomics Revolution

Biacore Technology

Surface Plasmon Resonance

The Sensor Surface and Immobilization Chemistry

Sensor chips

Immobilization Chemistry

General Capture Methods

Specialized Capture Methods

Lipids and Membrane Proteins

The Microfluidics System

Biacore Assay Basics

Correlation of
SPR
Response with Surface Binding

Assay Design: Assay Formats

Assay Design: Surface Preparation

Regeneration

Theoretical and Practical Implications of Technology Design for Biacore Assays

Label‐free Detection

The Optical Detection System and Bulk Effects

Surface‐based Versus Solution‐based Analysis

The Microfluidic Design and Mass Transport Effects

Biacore Applications in Basic and Clinical Research

Introduction

Applications of
B
iacore in Cancer Research

Applications of
B
iacore in Clinical Research

Applications of
B
iacore in Neuroscience

Drug: Plasma Protein Interactions

Drug:
DNA
Interactions

Nucleic Acid Structure and Analysis

Protein:
RNA
Interactions

Current Developments and Future Perspectives

SPR
‐
MS

The Challenges of High‐throughput Protein Analysis and Array Technologies
Cellular Assays and Their Application in Drug Discovery
Authors: Albrecht Hugo , Brodbeck‐Hummel Daniela , Hoever Michael , Nickel Beatrice , Regenass Urs 
Published: March 2008

AbstractOriginally published in: Molecular Biology in Medicinal Chemistry. Edited by Theodor Dingermann, Dieter Steinhilber and Gerd Folkers. Copyright © 2004 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30431‐8The sections in this article areIntroductionPositioning Cellular AssaysImpact on Drug DiscoveryClassification of Cellular AssaysProgress in Tools and Technologies for Cellular Compound ProfilingMembrane Proteins and Fast Cellular ResponsesReceptorsFLIPR Technology for Detection of Intracellular Calcium ReleaseCompetitive Immunoassay for Detection of Intracellular cAMPEnzyme Fragment Complementation (EFC) TechnologyMembrane Transport ProteinsIon ChannelsMDR ProteinsGene and Protein Expression Profiling in High‐throughput FormatsReporter Gene Assays in Lead FindingReporter Gene Assays in Lead OptimizationSpatio‐temporal Assays and Subpopulation AnalysisPhosphorylation Stage‐specific AntibodiesTarget‐protein‐specific AntibodiesProtein–GFP FusionsFluorescence Resonance Energy Transfer (FRET)GPCR Activation using Bioluminescence Resonance Energy Transfer (BRET)Protein Fragment Complementation Assays (PCA)Phenotypic AssaysProliferation/Respiration/ToxicityApoptosisDifferentiationMonitoring Cell MetabolismOther Phenotypic AssaysAcknowledgments
Mass Spectrometry of Peptides and Proteins
Authors: Warscheid Bettina 
Published: March 2008

Abstract
Originally published in: Proteomics in Drug Research. Edited by Michael Hamacher, Katrin Marcus, Kai Stühler, André van Hall, Bettina Warscheid and Helmut E. Meyer. Copyright © 2006 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31226‐9
Rapid advances in biological mass spectrometry have promoted proteomics to being a key technology in molecular cell biology and biomedical research. Current mass spectrometry‐based proteomics provides the capability for the identification of cellular and subcellular proteomes, the study of changes in protein concentrations via stable isotope labeling methods and the mapping of functional protein modules isolated by means of affinity purification. The large potential of proteomics techniques to identify and accurately quantify proteins from complex biological samples has been well recognized in the larger scientific community and it will in all probability have a great impact on future drug research.
The sections in this article are

Introduction

Ionization Principles

Matrix‐Assisted Laser Desorption/Ionization (
MALDI
)

Electrospray Ionization

Mass Spectrometric Instrumentation

Protein Identification Strategies

Quantitative Mass Spectrometry for Comparative and Functional Proteomics

Metabolic Labeling Approaches

15
N
Labeling

Stable Isotope Labeling by Amino Acids in Cell Culture (
SILAC
)

Chemical Labeling Approaches

Chemical Isotope Labeling at the Protein Level

Stable Isotope Labeling at the Peptide Level

Quantitative
MS
for Deciphering Protein‐Protein Interactions

Conclusions

Acknowledgements
Electrophysiological Analysis of Ion Channels
Authors: Pusch Michael 
Published: March 2008

Abstract
Originally 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: 3‐527‐31209‐2
This article outlines electrophysiological methods for extracting biophysical parameters that describe two fundamental properties of ion channels: gating and permeation. The Introduction provides a broad overview of the general concepts of ion channel biophysics and the text a review of the kind of information that can be extracted from electrophysiological recordings. The later sections introduce several methods for the analysis of electrophysiological experiments on heterologously expressed ion channels. Many parts are explicit and can be directly applied “at the bench”. Other, more advanced topics (gating current measurements, single‐channel kinetic analysis) are touched upon only superficially since their application requires further background that can be found in the references.
The sections in this article are

Introduction

Expression Systems and Related Recording Techniques

Expression in

Xenopus

Oocytes

Expression in Mammalian Cells

Leak and Capacitance Subtraction

Macroscopic Recordings

Analysis of Pore Properties–Permeation

Analysis of Fast Voltage‐dependent Block – the Woodhull Model

Information on Gating Properties from Macroscopic Measurements

Equilibrium Properties–Voltage‐gated Channels

Equilibrium Properties–Ligand Gated Channels

Macroscopic Kinetics

Channel Block

Nonstationary Noise Analysis

Gating Current Measurements in Voltage Gated Channels

Single Channel Analysis

Amplitude Histogram Analysis

Kinetic Single Channel Analysis

Conclusion

Acknowledgements
Ion Channel Assays Using Fluorescent Probes
Authors: González Jesús E. , Worley Jennings , Van Goor Fredrick 
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 areIntroductionMembrane Potential ProbesRedistribution ProbesFRETProbesAdvantages and Limitations of Membrane Potential ProbesIon‐sensitive Fluorescent ProbesCalcium DyesIndicators of Other IonsFluorescence Assays for Ion ChannelsCalcium ChannelsNon‐voltage‐gated Cation Permeable ChannelsSodium ChannelsPotassium ChannelsChloride ChannelsAssays for Monitoring Channel TraffickingConclusion
Enzyme Activity Fingerprinting Methods for Hydrolases
Authors: Grognux Johann , Reymond Jean‐Louis 
Published: March 2008

AbstractOriginally published in: Enzyme Assays. Edited by Jean‐Louis Reymond. Copyright © 2006 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31095‐1The sections in this article areIntroductionOne Enzyme – One SubstrateEnzyme Activity ProfilesTheAPIZYMSystem for Microbial Strain IdentificationHydrolase FingerprintingFingerprinting with Fluorogenic and Chromogenic SubstratesProcedure 1 Esterase/lipase Fingerprinting on Impregnated Silicagel PlatesFingerprinting with Indirect Chromogenic AssaysProcedure 2: Lipase/esterase Fingerprinting Using the Adrenaline Test for EnzymesCocktail FingerprintingClassification from Fingerprinting DataFingerprint RepresentationProcedure 3: Data Treatment for Representation of Colored Selectivity ArraysData NormalizationHierarchical Clustering of Enzyme FingerprintsAnalysis of Substrate SimilaritiesConclusionsAcknowledgment
Chemical Complementation Assays
Authors: Lefurgy Scott , Cornish Virginia 
Published: March 2008

AbstractOriginally published in: Enzyme Assays. Edited by Jean‐Louis Reymond. Copyright © 2006 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31095‐1The sections in this article areIntroductionComplementation AssaysIntroductionEarly Complementation AssaysEnzymology by ComplementationDirected Evolution by ComplementationDevelopment of Chemical ComplementationIntroductionThree‐hybrid AssayOriginal Yeast Three‐hybrid SystemDexamethasone–Methotrexate Yeast Three‐hybrid SystemTechnical ConsiderationsOther Three‐hybrid SystemsChemical ComplementationSelection Scheme and Model ReactionResultsGeneral ConsiderationsRelated MethodsApplications of Chemical ComplementationIntroductionEnzyme‐Inhibitor InteractionsRationaleScreen StrategyEnzyme Library ScreenGeneral ConsiderationsGlycosynthase EvolutionRationaleSelection SchemeGlycosynthase AssayDirected EvolutionGeneral ConsiderationsConclusion
High‐throughput Screening Methods for Oxidoreductases
Authors: Johannes Tyler W. , Woodyer Ryan D. , Zhao Huimin 
Published: March 2008

Abstract
Originally published in: Enzyme Assays. Edited by Jean‐Louis Reymond. Copyright © 2006 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31095‐1
The sections in this article are

Introduction

High‐throughput Methods for Various Oxidoreductases

Dehydrogenases

Colorimetric Screen Based on
NAD
(
P
)
H
Generation

Screens Based on
NAD
(
P
)
H
Depletion

Oxidases

Galactose Oxidase

d
‐Amino Acid Oxidase

Peroxidases

Oxygenases

Assays Based on Optical Properties of Substrates and Products

Assays Based on
G
ibbs' Reagent and 4‐Aminoantipyrine

para
‐Nitrophenoxy Analog (
p
NA
) Assay

Horseradish Peroxidase‐coupled Assay

Indole Assay

Laccases

ABTS
Assay

Poly
R
‐478 Assay

Other Assays

Conclusions

Acknowledgements
Quantitative Assay of Hydrolases for Activity and Selectivity Using Color Changes
Authors: Kazlauskas Romas J. 
Published: March 2008

Abstract
Originally published in: Enzyme Assays. Edited by Jean‐Louis Reymond. Copyright © 2006 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31095‐1
The sections in this article are

Introduction

Direct Assays Using Chromogenic Substrates

Indirect Assays Using Coupled Reactions –
p
H
Indicators

Overview of Quantitative Use of pH Indicator Assay

Applications

Searching for an Active Hydrolase (Testing Many Hydrolases Toward One Substrate)

Substrate Mapping of New Hydrolases (Testing Many Substrates Toward Hydrolase)

Comparison with Other Methods

Estimating and Measuring Selectivity

Estimating Selectivity without a Reference Compound

Quantitative Measure of Selectivity Using a Reference Compound (Quick

E

and Related Methods)

Chromogenic Substrate

p
H
Indicators

Application

Substrate Mapping of Hydrolases

Screening of Mutants in Directed Evolution

Advantages and Disadvantages

Acknowledgments
Protease Substrate Profiling
Authors: Harris Jennifer L. 
Published: March 2008

AbstractOriginally published in: Enzyme Assays. Edited by Jean‐Louis Reymond. Copyright © 2006 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31095‐1The sections in this article areIntroductionFunctional Protease Profiling – Peptide Substrate LibrariesSolution‐based Peptide Substrate LibrariesSolid Support‐based Synthesis and Screening of Peptide LibrariesGenetic Approaches to Identifying Protease Substrate SpecificityIdentification of Macromolecular SubstratesGenetic Approach to the Identification of Macromolecular SubstratesProteomic Approaches to Identifying Protease SubstratesConclusions
Photochemical Enzyme Regulation
Authors: Peng Ling , Goeldner Maurice 
Published: March 2008

AbstractOriginally published in: Dynamic Studies in Biology. Edited by Maurice Goeldner and Richard S. Givens. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30783‐8The sections in this article areIntroductionPhotoregulation ofATPasesATPases using CagedATPMoleculesNa,K‐ATPaseTransportATPasesand CarriersMolecular MotorsCa2+‐ATPaseCa2+‐ATPaseusing CagedATPCa2+‐ATPaseusing Caged InhibitorCa2+‐ATPaseusing CagedCa2+Photoregulation ofGTPases: Ras ProteinTime‐resolved Crystallographic Studies with CagedGTPTime‐resolvedFTIRStudies with CagedGTPPhotoregulation of KinasescAMP‐dependent Protein KinasePKAusing CagedcAMPPKAusing Caged InhibitorPKCPKCusing Caged ActivatorsPKCusing Caged Fluorescent SubstratesCalmodulin‐dependent Protein KinasesMyosin Light Chain Kinase (MLCK) using Caged Peptide InhibitorsCalmodulin‐dependent Protein KinaseII(CaMKII) using Caged Peptide InhibitorsPhotoregulation of Alcohol DehydrogenasesIsocitrate Dehydrogenase (IDH): CagedNADandNADPGlucose‐6‐Phosphate Dehydrogenase (G6PDH): Caged Glucose 6‐Phosphate and CagedNADP7α‐Hydroxy Steroid Dehydrogenase (7α‐HSDH): Caged Cholic AcidCaged Benzyl AlcoholPhotoregulation of CholinesterasesCaged Choline DerivativesCaged Cholinesterase SubstrateMiscellaneous Examples of Caged Enzyme ModulatorsCaged Nitric Oxide Synthase (NOS) InhibitorCaged Substrate of Quinol‐oxidizing EnzymesCaged Urease SubstrateCaged Ribonuclease Reductase SubstrateConclusions
Kinetic Protein Crystallography using Caged Compounds
Authors: Bourgeois Dominique , Weik Martin 
Published: March 2008

Abstract
Originally published in: Dynamic Studies in Biology. Edited by Maurice Goeldner and Richard S. Givens. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30783‐8
The sections in this article are

Introduction

Protein Activity and Conformational Changes in Crystals

Timescales and Activation States

Accumulating Unstable Species in the Crystal

Real‐time Crystallography and the Laue Technique

A Favorable Case: Isocitrate Dehydrogenase

The Case of
Ha
‐
ras
p
21: From Laue to Monochromatic Diffraction and Further Difficulties with Caged Compounds in Kinetic Crystallography

Trapping of Intermediate States

Cryo‐photolysis of
NPE
‐caged Compounds

Temperature‐dependent Enzymatic Activity and Dynamical Transitions

Potential Applications of Cryo‐photolysis Combined with Temperature‐controlled Protein Crystallography

Cryo‐photolysis Wavelength and Cryo‐radiolysis of
NPE
‐caged Compounds

X
‐ray Data Collection Strategy

Conclusion

Acknowledgments
Luminescent Proteins in Binding Assays
Authors: Roda Aldo , Guardigli Massimo , Michelini Elisa , Mirasoli Mara , Pasini Patrizia 
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 areIntroductionProtein–Protein and Protein–Ligand Interaction AssaysFRETandBRETMTechniquesFRET and BRET ApplicationsOther Detection PrinciplesAntibody‐based Binding AssaysChemical ConjugationGene FusionDual‐analyte AssaysExpression ImmunoassaysBRET‐based ImmunoassaysBiotin–Avidin Binding AssaysNucleic Acid Hybridization AssaysOther Binding AssaysConclusions
Sensory Defects Caused by Mutant Motor Proteins
Authors: Avraham Karen B. 
Published: March 2008

AbstractOriginally published in: Molecular Motors. Edited by Manfred Schliwa. Copyright © 2003 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30594‐0The sections in this article areIntroductionDevelopment of the Visual and Auditory Sensory SystemsVisual ImpairmentHearing ImpairmentMyosins Involved In Sensory DefectsMyosinVIIAStructure, function, and expression of myosinVIIAShaker 1 Mice and Other ModelsUsher Syndrome Type 1BDFNB2 andDFNA11MyosinVIStructure, function, and expression of myosinVISnell's waltzer mice and other modelsDFNA22MyosinXVAStructure, function, and expression of myosinXVAShaker 2DFNB3MYH9Structure, function, and expression ofMYH9DFNA17MyosinIIIAStructure, function, and expression of myosinIIIAMyosinIIIAmutantsDFNB30ConclusionsAcknowledgements