bluuebunny/crossref_metadata_2025_split huggingface dataset:
Myosin Myopathies
Authors: Konhilas John P. , Leinwand Leslie A. 
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

Cardiac Myosin Heavy Chains

My
HC
Structure and Function

Cardiac Muscle Regulation and Disease

Cardiac
My
HC
Myopathy

Functional Characterization of
My
HC
Motor Domain Mutations

Transgenic Models of Myosin‐based
FHC

My
HC
Interacting Proteins and
FHC

The Essential and Regulatory Light chains

Myosin Light Chain‐based
FHC

Myosin Binding Protein
C
‐Based
FHC

Titin‐based Familial Hypertrophic Cardiomyopathy

Myosin‐based Myopathies in Skeletal Muscle

Conclusions
Protein Sequence Variants: Resources and Tools
Authors: Yip Yum Lina , Famiglietti Maria Livia , Gasteiger Elisabeth , Bairoch Amos 
Published: March 2008

AbstractOriginally published in: Biomedical Applications of Proteomics. Edited by Jean‐Charles Sanchez, Garry L. Corthals and Denis F. Hochstrasser. Copyright © 2004 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30807‐1The sections in this article areIntroductionMedical Protein AnnotationDatabasesCentral DatabasesOnline Mendelian Inheritance in Man (OMIM)The Human Gene Mutation Database (HGMD)The SNP DatabasesAdvantages and Drawbacks of Central DatabasesSpecialized DatabasesAn Example of a Locus‐specific Database: the IARC TP53 DatabaseAn Example of a Disease‐oriented Specialized Database: Retina International's Scientific Newsletter – Mutation DatabaseOther Locus‐specific DatabasesAdvantages and Drawbacks of Specialized DatabasesThe Swiss‐Prot Protein Knowledgebase and Information on Disease and Sequence VariationsGene NamesDescription of DiseasesProteins as Therapeutic DrugsData on VariantsCross‐referencesMedical‐oriented KeywordsTechniques of SearchChallenges for DatabasesAnalysis Tools in the Context of Protein VariantsProteomic Tools for Protein Identification and the Characterization of VariantsProtein Identification ToolsPeptide Characterization ToolsTools for Analyzing and/or Predicting the Effects of Protein VariantsSequence‐based Analysis or Prediction ToolsStructure‐based Analysis or Prediction ToolsThe Swiss‐Prot Variant Page and Comparative ModelingRemarksConclusions
PPARs and Cancer
Authors: Gill J. H. , Roberts Ruth A. 
Published: March 2008

AbstractOriginally published in: Cellular Proteins and Their Fatty Acids in Health and Disease. Edited by Asim K. Duttaroy and Friedrich Spener. Copyright © 2003 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30437‐0The sections in this article areIntroductionThe PPAR FamilyPPARαExpression and ActivationPPARα and CancerSpecies DifferencesPPARα as a Therapeutic Target?PPARγExpression and ActivationPPARγ and CancerPPARγ as a Therapeutic Target?PPARβExpression and ActivationPPARβ and CancerPPARβ as a Therapeutic Target?Conclusions
PPARs in Atherosclerosis
Authors: Plutzky Jorge 
Published: March 2008

AbstractOriginally published in: Cellular Proteins and Their Fatty Acids in Health and Disease. Edited by Asim K. Duttaroy and Friedrich Spener. Copyright © 2003 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30437‐0The sections in this article areAtherosclerosisIntroductionAtherosclerosis as a Clinical SyndromeCellular Constituents of AtherosclerosisAtherosclerosis as an Inflammatory DisorderAtherosclerosis as a Metabolic DisorderPPAR in the VasculaturePPARs in Vascular Biology and AtherosclerosisExamining Evidence for PPAR in Vascular ResponsesPPARγ in Vascular Biology and AtherosclerosisIn vitroEvidenceIn vivoEvidencePPARα in Vascular Biology and AtherosclerosisIn vitroEvidenceIn vivoEvidencePPARδ in Vascular Biology and AtherosclerosisConclusion
Biochemistry and Structural Biology of Mammalian Prion Disease
Authors: Glockshuber Rudi 
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 areIntroductionPrions and the “Protein‐Only” HypothesisModels ofPrPScPropagationProperties ofPrPCandPrPScThree‐dimensional Structure and Folding of RecombinantPrPExpression of the Recombinant Prion Protein for Structural and Biophysical StudiesThree‐dimensional Structures of Recombinant Prion Proteins from Different Species and Their Implications for the Species Barrier of Prion TransmissionSolution Structure of MurinePrPComparison of Mammalian Prion Protein Structures and the Species Barrier of Prion TransmissionBiophysical Characterization of the Recombinant Prion ProteinFolding and Stability of RecombinantPrPRole of the Disulfide Bond inPrPInfluence of Point Mutations Linked With InheritedTSEs on the Stability of RecombinantPrPGeneration of Infectious Prionsin vitro: Principal Difficulties in Proving the Protein‐Only HypothesisUnderstanding the Strain Phenomenon in the Context of the Protein‐Only Hypothesis: Are Prions Crystals?Conclusions
Prion Protein
Authors: Derreumaux Philippe 
Published: March 2008

AbstractOriginally published in: Amyloid Proteins. Edited by Jean D. Sipe. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31072‐XThe sections in this article areIntroductionConformations of PrPCand PrPScStability and Unfolding/Folding of PrPCIn VitroMechanisms of Prion ReplicationIn VivoConclusions
Protein Aggregates in Neurodegenerative Disorders
Authors: Giaccone Giorgio , Salmona Mario , Tagliavini Fabrizio , Forloni Gianluigi 
Published: March 2008

AbstractOriginally published in: Amyloid Proteins. Edited by Jean D. Sipe. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31072‐XThe sections in this article areIntroductionNeuropathologyAlzheimer's DiseaseTauopathiesPrion DiseasesSynucleinopathiesThe Neurotoxic ProteinsAlzheimer's DiseasePrion DiseasesSynucleinopathiesConclusionsAcknowledgments
Cellular Toxicity of Protein Aggregates
Authors: Kagan Bruce 
Published: March 2008

Abstract
Originally published in: Amyloid Proteins. Edited by Jean D. Sipe. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31072‐X
The sections in this article are

Introduction

Aggregation

Cellular Mechanisms of Oligomeric Toxicity

Loss of Function Hypothesis

Receptors for Advanced End‐products of Glycation (RAGE) Receptors

Oxidative Stress

The Channel Hypothesis

Aβ

PrP106‐126

IAPP

ANP

SAA

AS

β
2
M

AL Amyloidosis

PG

HypF

Calcitonin (CT)

Lysozyme
Protein Folding and Aggregation in the Expanded Polyglutamine Repeat Diseases
Authors: Wetzel Ronald 
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

Key Features of the Polyglutamine Diseases

The Variety of Expanded Poly
Gln
Diseases

Clinical Features

Repeat Expansions and Repeat Length

The Role of Poly
Gln
and Poly
Gln
Aggregates

PolyGln Peptides in Studies of the Molecular Basis of Expanded Polyglutamine Diseases

Conformational Studies

Preliminary
in vitro
Aggregation Studies

In Vivo Aggregation Studies

Analyzing Polyglutamine Behavior With Synthetic Peptides: Practical Aspects

Disaggregation of Synthetic Polyglutamine Peptides

Growing and Manipulating Aggregates

Polyglutamine Aggregation by Freeze Concentration

Preparing Small Aggregates

In vitro Studies of Poly
Gln
Aggregation

The Universe of Protein Aggregation Mechanisms

Basic Studies on Spontaneous Aggregation

Nucleation Kinetics of Poly
Gln

Elongation Kinetics

Microtiter Plate Assay for Elongation Kinetics

Repeat‐length and Aggregate‐size Dependence of Elongation Rates

The Structure of PolyGln Aggregates

Electron Microscopy Analysis

Analysis with Amyloid Dyes Thioflavin T and Congo Red

Circular Dichroism Analysis

Presence of a Generic Amyloid Epitope in Poly
Gln
Aggregates

Proline Mutagenesis to Dissect the Polyglutamine Fold Within the Aggregate

Polyglutamine Aggregates and Cytotoxicity

Direct Cytotoxicity of Poly
Gln
Aggregates

Delivery of Aggregates into Cells and Cellular Compartments

Cell Killing by Nuclear‐targeted Poly
Gln
Aggregates

Visualization of Functional, Recruitment‐positive Aggregation Foci

Inhibitors of Poly
Gln
Aggregation

Designed Peptide Inhibitors

Screening for Inhibitors of Poly
Gln
Elongation

Conclusions

Acknowledgements
Thermodynamics of Amyloid Formation
Authors: Baskakov Ilia V. 
Published: March 2008

AbstractOriginally published in: Amyloid Proteins. Edited by Jean D. Sipe. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31072‐XThe sections in this article areIntroductionThermodynamic versus Kinetic Control of Protein FoldingWhat Thermodynamic Forces are Responsible for the Exceptional Stability of Amyloid Aggregates?Single Polypeptide Chain‐Multiple β‐Sheet‐rich Abnormal IsoformsDoes the Process of Prion Propagation Differ from Formation of Ordered Amyloid Aggregates?Prion Propagation is an Autocatalytic ProcessConformational Diversity of Self‐propagating Prion AggregatesHigh Species Specificity of Prion PropagationConclusions
Post‐translational Chemical Modifications in Amyloid Fibril Formation
Authors: Nilsson Melanie R. 
Published: March 2008

Abstract
Originally published in: Amyloid Proteins. Edited by Jean D. Sipe. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31072‐X
The sections in this article are

Introduction

Common Modifications that May Play a Significant Role
In Vivo

Cleavage by Proteases or Non‐enzymatic Hydrolysis

Deamidation, Isomerization, Racemization and Protein
l
‐Isoaspartyl Methyltransferase (
PIMT
)

Oxidative Damage

AGE
s

Phosphorylation

Proposed Mechanisms by which Chemical Modifications may Affect Amyloid Deposition

Conclusions

Acknowledgments
Serum amyloid P Component
Authors: Wood Steve P. , Coker Alun R. 
Published: March 2008

AbstractOriginally published in: Amyloid Proteins. Edited by Jean D. Sipe. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31072‐XThe sections in this article areIntroductionAmyloid Fibrils and their FormationThe Structure of SAPThe Calcium‐binding SiteComparative studies ofCRPSAP Structure in the Absence of CalciumBinding of Small Molecule Ligands to SAPThe Role of Glycosaminoglycans (GAGs)SAP, Protein Folding and Amyloid Fibril FormationConclusion
Amyloid Fibril Formation of Natively Unfolded Proteins
Authors: Uversky Vladimir N. , Fink Anthony L. 
Published: March 2008

AbstractOriginally published in: Amyloid Proteins. Edited by Jean D. Sipe. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31072‐XThe sections in this article areIntroductionMolecular Mechanisms of Amyloid Fibril Formation by a Natively Unfolded Protein: α‐Synucleinα‐Synuclein in Parkinson's Disease and other Neurodegenerative DisordersKey Structural Properties of α‐Synuclein: A Natively Unfolded ProteinMajor Structural Characteristics of Partially Folded α‐SynucleinFibril Formation by α‐Synuclein and the Partially Folded Amyloidogenic ConformationFibrillogenesis of Natively Unfolded Proteins Requires Partial FoldingFibril Formation by Proteins Involved in Conformational DisordersAmyloid β protein (Aβ)Tau proteinIslet Amyloid Polypeptide (IAPP) or AmylinPrion ProteinPolyglutamine Repeat DiseasesFibrillation of Proteins Unrelated to Conformational DiseaseYeast PrionsProthymosin αApolipoprotein CII (ApoCII)HistonesConclusionsAcknowledgments
Kinesin Superfamily Proteins
Authors: Hirokawa Nobutaka , Takemura Reiko 
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

The Kinesin Superfamily Proteins

N‐Kinesins

N
‐1 Kinesins

N
‐2 Kinesins

N
‐3 Kinesins

The
Unc
104/
KIF
1 family

The
KIF
13 family

The
KIF
16 family

N‐4 Kinesins

The
KIF
3 family

The
Osm
3/
KIF
17 family

N‐5 Kinesins

N‐6 Kinesins

The
CHO
1/
KIF
23 family

The
KIF
20/
Rab
6 kinesin family

N‐7 Kinesins

N‐8 Kinesins

The
K
id/
KIF
22 family

The
KIF
18 family

N
‐9 Kinesins

N
‐10 Kinesins

N
‐11 Kinesins

M‐Kinesins

C
‐Kinesins

C
‐1 Kinesins

C
‐2 Kinesins

Orphans

Cargoes of KIFs; Specificity and Redundancy

Recognition and Binding to Cargoes

How to Determine the Direction of Transport
Myosin Superfamily Proteins
Authors: Kieke Michele C. , Titus Margaret A. 
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 areIntroductionFunctional Properties of MyosinsDirectionality and ProcessivityProtein Motifs Found in MyosinsMyosin RegulationDiverse Functions for MyosinsNon‐muscle Contractile StructuresCell Motility and AdhesionOrganelle/Cellular Component TransportMaintenance of Actin‐rich ExtensionsMembrane TraffickingSignal TransductionMyosins in DiseaseGriscelli SyndromeRoles for Myosins in HearingNew Myosins and Myosin Functions on the HorizonConclusionsAcknowledgements
Plasma‐MembraneH+‐ATPaseFrom Yeast
Authors: Lecchi Silvia , Slayman Carolyn W. 
Published: March 2008

AbstractOriginally published in: Handbook of ATPase. Edited by Masamitsu Futai, Yoh Wada and Jack H. Kaplan. Copyright © 2004 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30689‐3The sections in this article areIntroductionStructureCa2+‐ATPaseas a ModelApplicability of theCa2+‐ATPaseStructure to OtherP2‐ATPase, Including the Pma1H+‐ATPaseH+‐ATPaseOligomersAssociated ProteolipidsReaction MechanismOverview of the Reaction CycleATPBinding and PhosphorylationE1–E2 Conformational ChangeH+PumpingBiogenesisPma1 Mutants with Defects in Folding and BiogenesisUse of Pma1 Mutants to Screen for Other Genes that Play a Role in Biogenesis and Quality ControlRole of Lipid RaftsRegulationEmerging Knowledge of Other Yeast P‐typeATPaseAcknowledgments
GastricH+,K+‐ATPase
Authors: Shin Jaim Moo , Vagin Olga , Munson Keith , Sachs George 
Published: March 2008

AbstractOriginally published in: Handbook of ATPase. Edited by Masamitsu Futai, Yoh Wada and Jack H. Kaplan. Copyright © 2004 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30689‐3The sections in this article areGastricH+,K+‐ATPaseα Subunit of GastricH+,K+‐ATPaseβ Subunit of GastricH+,K+‐ATPaseRegions of Association Between the α and β SubunitsRegions of Association of the α SubunitsKinetics of theH+,K+‐ATPaseConformations of theH+,K+‐ATPaseFunctional Residues of theH+,K+‐ATPaseStructural Model of theH+,K+‐ATPaseCrystal Structure of theH+,K+‐ATPaseMolecular Modeling of the GastricH+,K+‐ATPaseAcid Secretion and theH+,K+‐ATPaseInhibitors of theH+,K+‐ATPaseSubstituted BenzimidazolesSubstituted Imidazo[1,2α]pyridines and other K+‐competitive AntagonistsTrafficking of theH+,K+‐ATPase
Proton TranslocatingATPases
Authors: Futai Masamitsu , Sun‐Wada Ge‐Hong , Wada Yoh 
Published: March 2008

AbstractOriginally published in: Handbook of ATPase. Edited by Masamitsu Futai, Yoh Wada and Jack H. Kaplan. Copyright © 2004 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30689‐3The sections in this article areIntroductionCatalytic Mechanism ofF‐ATPaseRoles of the γ subunit: energy coupling by mechanical rotationRoles of the γ Subunit in Energy Couplingγ Subunit RotationMutational Analysis of the γ Subunit RotationRotational Catalysis of theF‐ATPaseHoloenzymeStructure ofFoSector and Proton Transport PathwayRotational Catalysis of theF‐ATPaseHoloenzymeRotational Catalysis ofF‐ATPasein MembranesRotational catalysis ofV‐ATPaseCatalytic Site and Proton PathwaySubunit Rotation ofV‐ATPaseDuring CatalysisConclusionAcknowledgments
VacuolarH+‐ATPases: Structure, Mechanism and Regulation
Authors: Shao Elim , Forgac Michael 
Published: March 2008

AbstractOriginally published in: Handbook of ATPases. Edited by Masamitsu Futai, Yoh Wada and Jack H. Kaplan. Copyright © 2004 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30689‐3The sections in this article areIntroductionFunction ofV‐ATPasesOverall Structure ofV‐ATPases and Relationship toF‐ATPasesStructure and Function of the Nucleotide‐binding SubunitsStructure and Function of otherV1Subunits and Arrangement of Subunits in theV‐ATPase ComplexStructure and Function ofV0SubunitsMechanism ofATP‐dependent Proton TransportRegulation ofV‐ATPase ActivityIn VivoConclusionsAcknowledgments
Anchoring Proteins of the Erythrocyte Membrane
Authors: Yawata Yoshihito 
Published: March 2008

AbstractOriginally published in: Cell Membrane. Yoshihito Yawata. Copyright © 2003 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30463‐9The sections in this article areAnkyrinIntroductionStructure of Red Cell AnkyrinMembrane (Band 3)‐Binding Domain of AnkyrinSpectrin‐Binding Domain of AnkyrinRegulatory Domain of AnkyrinFunctions of AnkyrinErythroid and Nonerythroid AnkyrinsProtein 4.2Protein Chemistry of Protein 4.2Functions of Protein 4.2Binding Properties of Protein 4.2Transglutaminase Activity of Protein 4.2Phosphorylation of Protein 4.2Protein 4.2 in Red Cell Membrane UltrastructureProtein 4.2 GeneCharacteristics of GenomicDNAcDNAof the Protein 4.2 GeneProtein 4.2 Gene in Mouse Red CellsTissue‐Specific Expression of the Mouse Protein 4.2 Gene and the Pallid Mutation
Skeletal Proteins of the Erythrocyte Membrane
Authors: Yawata Yoshihito 
Published: March 2008

AbstractOriginally published in: Cell Membrane. Yoshihito Yawata. Copyright © 2003 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30463‐9The sections in this article areα‐ and β‐SpectrinsIntroductionStructure of Red Cell SpectrinsFunctions of Red Cell SpectrinsErythroid and Nonerythroid SpectrinsProtein 4.1Structure of Protein 4.1Binding to Other Membrane ProteinsExtensive Alternative SplicingsNonerythroid Protein 4.1 IsoformsActinOther Minor Skeletal ProteinsThep55 ProteinAdducinDematin (Protein 4.9)TropomyosinTropomodulinOther Membrane Proteins
Integral Proteins of the Erythrocyte Membrane
Authors: Yawata Yoshihito 
Published: March 2008

AbstractOriginally published in: Cell Membrane. Yoshihito Yawata. Copyright © 2003 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30463‐9The sections in this article areBand 3Structure of Band 3Functions of Band 3Membrane Protein Binding by the Cytoplasmic Domain of Band 3Binding to Glycolytic Enzymes by the Cytoplasmic Domain of Band 3Binding to Hemoglobin by the Cytoplasmic Domain of Band 3Anion Exchange Channel by the Transmembrane Domain of Band 3Lateral and Rotational Mobility of Band 3Blood Type Antigens and Band 3Band 3 in Nonerythyroid CellsGlycophorinsGlycophorinsA,B, andEGlycophorinA(GPA)GlycophorinB(GPB)GlycophorinE(GPE)GylcophorinsCandDGlycophorinC(GPC)GlycophorinD(GPD)Blood Group AntigensABOBlood GroupRh Blood GroupPBlood GroupLutheran Blood GroupKell Blood GroupLewis Blood GroupDuffy Blood GroupKidd Blood GroupLWBlood GroupIiBlood GroupTheDiego andWright Blood Group Antigens on Band 3Other Minor Blood Group AntigensGlycosyl Phoshatidylinositol (GPI) Anchor Proteins
Retinoid Receptors RAR and RXR: Structure and Function
Authors: Mata de Urquiza Alexander , Perlmann Thomas 
Published: March 2008

AbstractOriginally published in: Cellular Proteins and Their Fatty Acids in Health and Disease. Edited by Asim K. Duttaroy and Friedrich Spener. Copyright © 2003 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30437‐0The sections in this article areRetinoids in DevelopmentRetinoid Receptors Transduce Retinoic Acid SignalsRetinoid Receptors Belong to the Nuclear Hormone Receptor FamilyNuclear Receptors Share a Common StructureThe LBD and Ligand‐dependent TransactivationCross‐talkCo‐activatorsCo‐repressorsNuclear Receptors from an Evolutionary PerspectiveFatty acids as Endogenous Ligands for RXRConclusionsAcknowledgements
HumanABCTransporters: Function, Expression, and Regulation
Authors: Schmitz Gerd , Langmann Thomas 
Published: March 2008

AbstractOriginally published in: Cellular Proteins and Their Fatty Acids in Health and Disease. Edited by Asim K. Duttaroy and Friedrich Spener. Copyright © 2003 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30437‐0The sections in this article areIntroductionStructural Features ofATPBinding Cassette (ABC) TransportersOverview of HumanABCGene SubfamiliesThe ABCA (ABC1) SubfamilyThe ABCB (MDR/TAP) SubfamilyThe ABCC (CFTR/MRP) SubfamilyThe ABCD (ALD) SubfamilyThe ABCE (OABP) and ABCF (GCN20) SubfamiliesThe ABCG (White) SubfamilyDiseases and Phenotypes Caused byABCMTransportersFamilial HDL‐deficiency andABCA1Retinal Degeneration andABCA4 (ABCR)Cystic Fibrosis (ABCC7/CFTR)Multidrug Resistance (ABCB1/MDR1,ABCC1/MRP1,ABCG2)Adrenoleukodystrophy (ABCD1/ALD)Sulfonylurea Receptor (ABCC8/SUR)Function and Regulation ofABCTransporters in Lipid TransportABCA1 in Macrophage Lipid TransportABCG1 and OtherABCGMembers in Sterol HomeostasisABCTransporters involved in Hepatobiliary TransportConclusions
The Photoproteins
Authors: Shimomura Osamu 
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 areIntroductionVarious Types of Photoproteins Presently KnownRadiolarian (Protozoa) PhotoproteinsCoelenterate PhotoproteinsCtenophore PhotoproteinsPholasin (PholasLuciferin)ChaetopterusPhotoproteinPolynoidinSymplectinLuminodesmusPhotoproteinOphiopsilaPhotoproteinBasic Strategy of Extracting and Purifying PhotoproteinsThe Photoprotein AequorinExtraction and Purification of AequorinHydrophobic Interaction ChromatographyProperties of AequorinStabilityFreeze‐dryingSpecificity toCa2+Luminescence of Aequorin by Substances Other Than Divalent CationsMechanism of Aequorin Luminescence and Regeneration of AequorinStructure of AequorinLuminescence ReactionRegenerationInhibitors of Aequorin LuminescenceRecombinant AequorinSemi‐synthetic Aequorinse‐Aequorins
The Outer Mitochondrial Membrane Pore (Voltage‐Dependent Anion Channel)
Authors: Vyssokikh Mikhail , Brdiczka Dieter 
Published: March 2008

AbstractOriginally published in: Bacterial and Eukaryotic Porins. Edited by Roland Benz. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30775‐3The sections in this article areIntroductionStructure and Isotypes of VDACThe Influence of Phospholipids on VDAC StructureVDAC Conductance and Ion SelectivityPhysiological Significance of the Voltage DependencePorins as Specific Binding SitesVDAC senses Inner Membrane Functions in the Contact SiteCytochromecis a Component of the Contact SitesIsolation and Characterization of VDAC‐ANT ComplexesReconstitution of VDAC‐ANT ComplexesImportance of Metabolic Channeling in Regulation of Energy MetabolismThe VDAC‐ANT Complex as Permeability Transition PoreThe VDAC‐ANT Complex as a Target for Bax‐dependent CytochromecReleaseThe VDAC–ANT Complexes contain CytochromecThe Importance of the Kinases in Regulation of ApoptosisSuppression of Bax‐dependent CytochromecRelease and Permeability Transition by HexokinaseSuppression of Permeability Transition by Mitochondrial Creatine KinaseConclusion