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Protein phosphorylation / / edited by F. Marks
| Protein phosphorylation / / edited by F. Marks |
| Pubbl/distr/stampa | Weinheim, [Germany] : , : VCH, , 1996 |
| Descrizione fisica | 1 online resource (409 p.) |
| Disciplina |
572.65
574.19245 |
| Soggetto topico |
Phosphoproteins - Synthesis
Phosphoproteins - Metabolism Protein kinases |
| Soggetto genere / forma | Electronic books. |
| ISBN |
1-281-84268-0
9786611842680 3-527-61503-2 3-527-61502-4 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | ger |
| Nota di contenuto |
Protein Phosphorylation; Preface; Contents; List of contributors; List of Abbreviations; 1 The brain of the cell; 1.1 Signals and symbols; 1.2 Proteins as communicative molecules; 1.3 The discovery of protein phosphorylation; 1.4 Protein phosphorylation in prokaryotes; 1.5 Protein phosphorylation in eukaryotes; 1.5.1 Eukaryotic protein kinases: common features and diversities; 1.5.2 Control of protein kinase activity; 1.5.3 The problem of substrate specificity; 1.5.4 Regulatory signals for protein kinases and examples of signaling cross-talk
1.5.5 Protein tyrosine phosphorylation and the integrity of multicellular organisms1.6 Signal extinction by protein dephosphorylation; 1.7 Cancer: a cellular 'psychosis'; 1.8 Advancing beyond the metaphor: proteins as non-trivial machines; References; 2 cAMP-dependent protein kinase: structure, function and control; 2.1 Introduction; 2.2 Biochemistry of cAPK; 2.2.1 Principles of purification of cAPK; 2.2.2 The catalytic subunit (C-subunit); 2.2.3 Control of cAPK; 2.3 Cellular aspects of cAPK function and control; 2.3.1 In vivo control of cAPK; 2.3.2 Cellular location of cAPK subunits 2.4 Structural aspects of cAPK function2.4.1 Dynamics of substrate-induced fit in solution; 2.4.2 Crystal structure of cAPK C-subunit; 2.4.3 Aspects of future research on cAPK; 2.5 A quick look at the cGMP-dependent protein kinase: a close relative of cAPK; 2.6 Structural consequences of protein phosphorylation in general; 2.6.1 Immediate physical consequences; 2.6.2 Conformational change - indirect evidence; 2.6.3 Conformational change - direct evidence; 2.6.4 Structural effects in peptides; References; 3 Protein kinase C; 3.1 Introduction; 3.2 The protein kinase C isoenzyme family 3.2.1 The PKC subfamilies3.2.2 PKC isoenzyme structures: common features and differences3; 3.2.3 Regulation of PKC activity4; 3.3 Cellular functions of protein kinase C; 3.3.1 Activators and inhibitors as tools in PKC research; 3.3.2 Phorbol ester effects; 3.3.3 Are effects of phorbol esters and DAG reliable indicators of PKC action?; 3.3.4 Effects of altered PKC expression on cellular functions; 3.3.5 PKC substrates11; 3.3.6 How PKC may acquire substrate specificity; 3.4 Protein kinase C in disease; 3.4.1 Involvement of PKC expression in benign and malignant hyperproliferative diseases 3.4.2 Oncogenic and anti-oncogenic effects of protein kinase C expression3.4.3 Protein kinase C and skin tumor promotion; References; 4 Casein kinases; 4.1 The different classes of casein kinases; 4.2 Protein kinase CK2; 4.2.1 History; 4.2.2 Biochemical features; 4.2.3 Molecular structures. interaction of subunits and regulation mechanisms; 4.2.4 CK2 genes and their chromosomal locations; 4.2.5 Transcribed CK2 messages and transcription control; 4.2.6 Cell physiological roles of CK2; 4.2.7 CK2 in mitogenic signal transmission; 4.2.8 CK2 and the cell cycle; 4.3 Protein kinase CK1 4.3.1 Biochemical features and molecular structures of CK1 |
| Record Nr. | UNINA-9910144009603321 |
| Weinheim, [Germany] : , : VCH, , 1996 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein phosphorylation / / edited by F. Marks
| Protein phosphorylation / / edited by F. Marks |
| Pubbl/distr/stampa | Weinheim, [Germany] : , : VCH, , 1996 |
| Descrizione fisica | 1 online resource (409 p.) |
| Disciplina |
572.65
574.19245 |
| Soggetto topico |
Phosphoproteins - Synthesis
Phosphoproteins - Metabolism Protein kinases |
| ISBN |
1-281-84268-0
9786611842680 3-527-61503-2 3-527-61502-4 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | ger |
| Nota di contenuto |
Protein Phosphorylation; Preface; Contents; List of contributors; List of Abbreviations; 1 The brain of the cell; 1.1 Signals and symbols; 1.2 Proteins as communicative molecules; 1.3 The discovery of protein phosphorylation; 1.4 Protein phosphorylation in prokaryotes; 1.5 Protein phosphorylation in eukaryotes; 1.5.1 Eukaryotic protein kinases: common features and diversities; 1.5.2 Control of protein kinase activity; 1.5.3 The problem of substrate specificity; 1.5.4 Regulatory signals for protein kinases and examples of signaling cross-talk
1.5.5 Protein tyrosine phosphorylation and the integrity of multicellular organisms1.6 Signal extinction by protein dephosphorylation; 1.7 Cancer: a cellular 'psychosis'; 1.8 Advancing beyond the metaphor: proteins as non-trivial machines; References; 2 cAMP-dependent protein kinase: structure, function and control; 2.1 Introduction; 2.2 Biochemistry of cAPK; 2.2.1 Principles of purification of cAPK; 2.2.2 The catalytic subunit (C-subunit); 2.2.3 Control of cAPK; 2.3 Cellular aspects of cAPK function and control; 2.3.1 In vivo control of cAPK; 2.3.2 Cellular location of cAPK subunits 2.4 Structural aspects of cAPK function2.4.1 Dynamics of substrate-induced fit in solution; 2.4.2 Crystal structure of cAPK C-subunit; 2.4.3 Aspects of future research on cAPK; 2.5 A quick look at the cGMP-dependent protein kinase: a close relative of cAPK; 2.6 Structural consequences of protein phosphorylation in general; 2.6.1 Immediate physical consequences; 2.6.2 Conformational change - indirect evidence; 2.6.3 Conformational change - direct evidence; 2.6.4 Structural effects in peptides; References; 3 Protein kinase C; 3.1 Introduction; 3.2 The protein kinase C isoenzyme family 3.2.1 The PKC subfamilies3.2.2 PKC isoenzyme structures: common features and differences3; 3.2.3 Regulation of PKC activity4; 3.3 Cellular functions of protein kinase C; 3.3.1 Activators and inhibitors as tools in PKC research; 3.3.2 Phorbol ester effects; 3.3.3 Are effects of phorbol esters and DAG reliable indicators of PKC action?; 3.3.4 Effects of altered PKC expression on cellular functions; 3.3.5 PKC substrates11; 3.3.6 How PKC may acquire substrate specificity; 3.4 Protein kinase C in disease; 3.4.1 Involvement of PKC expression in benign and malignant hyperproliferative diseases 3.4.2 Oncogenic and anti-oncogenic effects of protein kinase C expression3.4.3 Protein kinase C and skin tumor promotion; References; 4 Casein kinases; 4.1 The different classes of casein kinases; 4.2 Protein kinase CK2; 4.2.1 History; 4.2.2 Biochemical features; 4.2.3 Molecular structures. interaction of subunits and regulation mechanisms; 4.2.4 CK2 genes and their chromosomal locations; 4.2.5 Transcribed CK2 messages and transcription control; 4.2.6 Cell physiological roles of CK2; 4.2.7 CK2 in mitogenic signal transmission; 4.2.8 CK2 and the cell cycle; 4.3 Protein kinase CK1 4.3.1 Biochemical features and molecular structures of CK1 |
| Record Nr. | UNISA-996197616603316 |
| Weinheim, [Germany] : , : VCH, , 1996 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. di Salerno | ||
| ||
Protein phosphorylation / / edited by F. Marks
| Protein phosphorylation / / edited by F. Marks |
| Pubbl/distr/stampa | Weinheim, [Germany] : , : VCH, , 1996 |
| Descrizione fisica | 1 online resource (409 p.) |
| Disciplina |
572.65
574.19245 |
| Soggetto topico |
Phosphoproteins - Synthesis
Phosphoproteins - Metabolism Protein kinases |
| ISBN |
1-281-84268-0
9786611842680 3-527-61503-2 3-527-61502-4 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | ger |
| Nota di contenuto |
Protein Phosphorylation; Preface; Contents; List of contributors; List of Abbreviations; 1 The brain of the cell; 1.1 Signals and symbols; 1.2 Proteins as communicative molecules; 1.3 The discovery of protein phosphorylation; 1.4 Protein phosphorylation in prokaryotes; 1.5 Protein phosphorylation in eukaryotes; 1.5.1 Eukaryotic protein kinases: common features and diversities; 1.5.2 Control of protein kinase activity; 1.5.3 The problem of substrate specificity; 1.5.4 Regulatory signals for protein kinases and examples of signaling cross-talk
1.5.5 Protein tyrosine phosphorylation and the integrity of multicellular organisms1.6 Signal extinction by protein dephosphorylation; 1.7 Cancer: a cellular 'psychosis'; 1.8 Advancing beyond the metaphor: proteins as non-trivial machines; References; 2 cAMP-dependent protein kinase: structure, function and control; 2.1 Introduction; 2.2 Biochemistry of cAPK; 2.2.1 Principles of purification of cAPK; 2.2.2 The catalytic subunit (C-subunit); 2.2.3 Control of cAPK; 2.3 Cellular aspects of cAPK function and control; 2.3.1 In vivo control of cAPK; 2.3.2 Cellular location of cAPK subunits 2.4 Structural aspects of cAPK function2.4.1 Dynamics of substrate-induced fit in solution; 2.4.2 Crystal structure of cAPK C-subunit; 2.4.3 Aspects of future research on cAPK; 2.5 A quick look at the cGMP-dependent protein kinase: a close relative of cAPK; 2.6 Structural consequences of protein phosphorylation in general; 2.6.1 Immediate physical consequences; 2.6.2 Conformational change - indirect evidence; 2.6.3 Conformational change - direct evidence; 2.6.4 Structural effects in peptides; References; 3 Protein kinase C; 3.1 Introduction; 3.2 The protein kinase C isoenzyme family 3.2.1 The PKC subfamilies3.2.2 PKC isoenzyme structures: common features and differences3; 3.2.3 Regulation of PKC activity4; 3.3 Cellular functions of protein kinase C; 3.3.1 Activators and inhibitors as tools in PKC research; 3.3.2 Phorbol ester effects; 3.3.3 Are effects of phorbol esters and DAG reliable indicators of PKC action?; 3.3.4 Effects of altered PKC expression on cellular functions; 3.3.5 PKC substrates11; 3.3.6 How PKC may acquire substrate specificity; 3.4 Protein kinase C in disease; 3.4.1 Involvement of PKC expression in benign and malignant hyperproliferative diseases 3.4.2 Oncogenic and anti-oncogenic effects of protein kinase C expression3.4.3 Protein kinase C and skin tumor promotion; References; 4 Casein kinases; 4.1 The different classes of casein kinases; 4.2 Protein kinase CK2; 4.2.1 History; 4.2.2 Biochemical features; 4.2.3 Molecular structures. interaction of subunits and regulation mechanisms; 4.2.4 CK2 genes and their chromosomal locations; 4.2.5 Transcribed CK2 messages and transcription control; 4.2.6 Cell physiological roles of CK2; 4.2.7 CK2 in mitogenic signal transmission; 4.2.8 CK2 and the cell cycle; 4.3 Protein kinase CK1 4.3.1 Biochemical features and molecular structures of CK1 |
| Record Nr. | UNINA-9910830864603321 |
| Weinheim, [Germany] : , : VCH, , 1996 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein phosphorylation in parasites : novel targets for antiparasitic intervention / / edited by Christian Doerig, Gerald Späth, and Martin Wiese
| Protein phosphorylation in parasites : novel targets for antiparasitic intervention / / edited by Christian Doerig, Gerald Späth, and Martin Wiese |
| Pubbl/distr/stampa | Weinheim : , : Wiley Blackwell, , [2014] |
| Descrizione fisica | 1 online resource (452 p.) |
| Disciplina | 452 |
| Altri autori (Persone) |
DoerigChristian
SpäthGerald WieseMartin |
| Collana | Drug discovery in infectious diseases |
| Soggetto topico |
Phosphoproteins - Synthesis
Parasitology Parasites Antiparasitic agents |
| ISBN |
3-527-67537-X
3-527-67540-X 3-527-67539-6 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | part one. Bioinformatics -- part two. Functional analysis of parasite kinomes and phosphatomes -- part three. Role of host cell kinomes and phosphatomes in parasitic infections -- part four. Drug discovery. |
| Record Nr. | UNINA-9910142023903321 |
| Weinheim : , : Wiley Blackwell, , [2014] | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein phosphorylation in parasites : novel targets for antiparasitic intervention / / edited by Christian Doerig, Gerald Späth, and Martin Wiese
| Protein phosphorylation in parasites : novel targets for antiparasitic intervention / / edited by Christian Doerig, Gerald Späth, and Martin Wiese |
| Pubbl/distr/stampa | Weinheim : , : Wiley Blackwell, , [2014] |
| Descrizione fisica | 1 online resource (452 p.) |
| Disciplina | 452 |
| Altri autori (Persone) |
DoerigChristian
SpäthGerald WieseMartin |
| Collana | Drug discovery in infectious diseases |
| Soggetto topico |
Phosphoproteins - Synthesis
Parasitology Parasites Antiparasitic agents |
| ISBN |
3-527-67537-X
3-527-67540-X 3-527-67539-6 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | part one. Bioinformatics -- part two. Functional analysis of parasite kinomes and phosphatomes -- part three. Role of host cell kinomes and phosphatomes in parasitic infections -- part four. Drug discovery. |
| Record Nr. | UNINA-9910816781103321 |
| Weinheim : , : Wiley Blackwell, , [2014] | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Proteomics of biological systems [[electronic resource] ] : protein phosphorylation using mass spectrometry techniques / / Bryan M Ham
| Proteomics of biological systems [[electronic resource] ] : protein phosphorylation using mass spectrometry techniques / / Bryan M Ham |
| Autore | Ham Bryan M |
| Pubbl/distr/stampa | Hoboken, N.J., : John Wiley & Sons, 2012 |
| Descrizione fisica | 1 online resource (376 p.) |
| Disciplina | 572/.62 |
| Soggetto topico |
Proteomics - Methodology
Phosphorylation - Research - Methodology Phosphoproteins - Synthesis Mass spectrometry Biological systems - Research - Methodology |
| ISBN |
1-283-28285-2
9786613282859 1-118-13703-5 1-118-13704-3 1-118-13701-9 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
PROTEOMICS OF BIOLOGICAL SYSTEMS: Protein Phosphorylation Using Mass Spectrometry Techniques; CONTENTS; PREFACE; ACKNOWLEDGMENTS; ABOUT THE AUTHOR; 1: Posttranslational Modification (PTM) of Proteins; 1.1 OVER 200 FORMS OF PTM OF PROTEINS; 1.2 THREE MAIN TYPES OF PTM STUDIED BY MS; 1.3 OVERVIEW OF NANO-ELECTROSPRAY/NANOFLOW LC-MS; 1.3.1 Definition and Description of MS; 1.3.2 Basic Design of Mass Analyzer Instrumentation; 1.3.3 ESI; 1.3.4 Nano-ESI; 1.4 OVERVIEW OF NUCLEIC ACIDS; 1.5 PROTEINS AND PROTEOMICS; 1.5.1 Introduction to Proteomics; 1.5.2 Protein Structure and Chemistry
1.5.3 Bottom-Up Proteomics: MS of Peptides1.5.3.1 History and Strategy; 1.5.3.2 Protein Identification through Product Ion Spectra; 1.5.3.3 High-Energy Product Ions; 1.5.3.4 De Novo Sequencing; 1.5.3.5 Electron Capture Dissociation (ECD); 1.5.4 Top-Down Proteomics: MS of Intact Proteins; 1.5.4.1 Background; 1.5.4.2 GP Basicity and Protein Charging; 1.5.4.3 Calculation of Charge State and Molecular Weight; 1.5.4.4 Top-Down Protein Sequencing; 1.5.5 Systems Biology and Bioinformatics; 1.5.6 Biomarkers in Cancer; REFERENCES; 2: Glycosylation of Proteins; 2.1 PRODUCTION OF A GLYCOPROTEIN 2.2 BIOLOGICAL PROCESSES OF PROTEIN GLYCOSYLATION2.3 N-LINKED AND O-LINKED GLYCOSYLATION; 2.4 CARBOHYDRATES; 2.4.1 Ionization of Oligosaccharides; 2.4.2 Carbohydrate Fragmentation; 2.4.3 Complex Oligosaccharide Structural Elucidation; 2.5 THREE OBJECTIVES IN STUDYING GLYCOPROTEINS; 2.6 GLYCOSYLATION STUDY APPROACHES; 2.6.1 MS of Glycopeptides; 2.6.2 Mass Pattern Recognition; 2.6.2.1 High Galactose Glycosylation Pattern; 2.6.3 Charge State Determination; 2.6.4 Diagnostic Fragment Ions; 2.6.5 High-Resolution/High-Mass Accuracy Measurement and Identification; 2.6.6 Digested Bovine Fetuin REFERENCES3: Sulfation of Proteins as Posttranslational Modification; 3.1 GLYCOSAMINOGLYCAN SULFATION; 3.2 CELLULAR PROCESSES INVOLVED IN SULFATION; 3.3 BRIEF EXAMPLE OF PHOSPHORYLATION; 3.4 SULFOTRANSFERASE CLASS OF ENZYMES; 3.5 FRAGMENTATION NOMENCLATURE FOR CARBOHYDRATES; 3.6 SULFATED MUCIN OLIGOSACCHARIDES; 3.7 TYROSINE SULFATION; 3.8 TYROSYLPROTEIN SULFOTRANSFERASES TPST1 AND TPST2; 3.9 O-SULFATED HUMAN PROTEINS; 3.10 SULFATED PEPTIDE PRODUCT ION SPECTRA; 3.11 USE OF HIGHER ENERGY COLLISIONS; 3.12 ELECTRON CAPTURE DISSOCIATION (ECD); 3.13 SULFATION VERSUS PHOSPHORYLATION; REFERENCES 4: Eukaryote PTM as Phosphorylation: Normal State Studies4.1 MASS SPECTRAL MEASUREMENT WITH EXAMPLES OF HELA CELL PHOSPHOPROTEOME; 4.1.1 Introduction; 4.1.2 Protein Phosphatase and Kinase; 4.1.3 Hydroxy-Amino Acid Phosphorylation; 4.1.4 Traditional Phosphoproteomic Approaches; 4.1.5 Current Approaches; 4.1.5.1 Phosphoproteomic Enrichment Techniques; 4.1.5.2 IMAC; 4.1.5.3 MOAC; 4.1.5.4 Methylation of Peptides prior to IMAC or MOAC Enrichment; 4.1.6 The Ideal Approach; 4.1.7 One-Dimensional (1-D) Sodium Dodecyl Sulfate (SDS) PAGE; 4.1.8 Tandem MS Approach; 4.1.8.1 pS Loss of Phosphate Group 4.1.8.2 pT Loss of Phosphate Group |
| Record Nr. | UNINA-9910139593603321 |
Ham Bryan M
|
||
| Hoboken, N.J., : John Wiley & Sons, 2012 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Proteomics of biological systems : protein phosphorylation using mass spectrometry techniques / / Bryan M Ham
| Proteomics of biological systems : protein phosphorylation using mass spectrometry techniques / / Bryan M Ham |
| Autore | Ham Bryan M |
| Edizione | [1st ed.] |
| Pubbl/distr/stampa | Hoboken, N.J., : John Wiley & Sons, 2012 |
| Descrizione fisica | 1 online resource (376 p.) |
| Disciplina | 572/.62 |
| Soggetto topico |
Proteomics - Methodology
Phosphorylation - Research - Methodology Phosphoproteins - Synthesis Mass spectrometry Biological systems - Research - Methodology |
| ISBN |
1-283-28285-2
9786613282859 1-118-13703-5 1-118-13704-3 1-118-13701-9 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
PROTEOMICS OF BIOLOGICAL SYSTEMS: Protein Phosphorylation Using Mass Spectrometry Techniques; CONTENTS; PREFACE; ACKNOWLEDGMENTS; ABOUT THE AUTHOR; 1: Posttranslational Modification (PTM) of Proteins; 1.1 OVER 200 FORMS OF PTM OF PROTEINS; 1.2 THREE MAIN TYPES OF PTM STUDIED BY MS; 1.3 OVERVIEW OF NANO-ELECTROSPRAY/NANOFLOW LC-MS; 1.3.1 Definition and Description of MS; 1.3.2 Basic Design of Mass Analyzer Instrumentation; 1.3.3 ESI; 1.3.4 Nano-ESI; 1.4 OVERVIEW OF NUCLEIC ACIDS; 1.5 PROTEINS AND PROTEOMICS; 1.5.1 Introduction to Proteomics; 1.5.2 Protein Structure and Chemistry
1.5.3 Bottom-Up Proteomics: MS of Peptides1.5.3.1 History and Strategy; 1.5.3.2 Protein Identification through Product Ion Spectra; 1.5.3.3 High-Energy Product Ions; 1.5.3.4 De Novo Sequencing; 1.5.3.5 Electron Capture Dissociation (ECD); 1.5.4 Top-Down Proteomics: MS of Intact Proteins; 1.5.4.1 Background; 1.5.4.2 GP Basicity and Protein Charging; 1.5.4.3 Calculation of Charge State and Molecular Weight; 1.5.4.4 Top-Down Protein Sequencing; 1.5.5 Systems Biology and Bioinformatics; 1.5.6 Biomarkers in Cancer; REFERENCES; 2: Glycosylation of Proteins; 2.1 PRODUCTION OF A GLYCOPROTEIN 2.2 BIOLOGICAL PROCESSES OF PROTEIN GLYCOSYLATION2.3 N-LINKED AND O-LINKED GLYCOSYLATION; 2.4 CARBOHYDRATES; 2.4.1 Ionization of Oligosaccharides; 2.4.2 Carbohydrate Fragmentation; 2.4.3 Complex Oligosaccharide Structural Elucidation; 2.5 THREE OBJECTIVES IN STUDYING GLYCOPROTEINS; 2.6 GLYCOSYLATION STUDY APPROACHES; 2.6.1 MS of Glycopeptides; 2.6.2 Mass Pattern Recognition; 2.6.2.1 High Galactose Glycosylation Pattern; 2.6.3 Charge State Determination; 2.6.4 Diagnostic Fragment Ions; 2.6.5 High-Resolution/High-Mass Accuracy Measurement and Identification; 2.6.6 Digested Bovine Fetuin REFERENCES3: Sulfation of Proteins as Posttranslational Modification; 3.1 GLYCOSAMINOGLYCAN SULFATION; 3.2 CELLULAR PROCESSES INVOLVED IN SULFATION; 3.3 BRIEF EXAMPLE OF PHOSPHORYLATION; 3.4 SULFOTRANSFERASE CLASS OF ENZYMES; 3.5 FRAGMENTATION NOMENCLATURE FOR CARBOHYDRATES; 3.6 SULFATED MUCIN OLIGOSACCHARIDES; 3.7 TYROSINE SULFATION; 3.8 TYROSYLPROTEIN SULFOTRANSFERASES TPST1 AND TPST2; 3.9 O-SULFATED HUMAN PROTEINS; 3.10 SULFATED PEPTIDE PRODUCT ION SPECTRA; 3.11 USE OF HIGHER ENERGY COLLISIONS; 3.12 ELECTRON CAPTURE DISSOCIATION (ECD); 3.13 SULFATION VERSUS PHOSPHORYLATION; REFERENCES 4: Eukaryote PTM as Phosphorylation: Normal State Studies4.1 MASS SPECTRAL MEASUREMENT WITH EXAMPLES OF HELA CELL PHOSPHOPROTEOME; 4.1.1 Introduction; 4.1.2 Protein Phosphatase and Kinase; 4.1.3 Hydroxy-Amino Acid Phosphorylation; 4.1.4 Traditional Phosphoproteomic Approaches; 4.1.5 Current Approaches; 4.1.5.1 Phosphoproteomic Enrichment Techniques; 4.1.5.2 IMAC; 4.1.5.3 MOAC; 4.1.5.4 Methylation of Peptides prior to IMAC or MOAC Enrichment; 4.1.6 The Ideal Approach; 4.1.7 One-Dimensional (1-D) Sodium Dodecyl Sulfate (SDS) PAGE; 4.1.8 Tandem MS Approach; 4.1.8.1 pS Loss of Phosphate Group 4.1.8.2 pT Loss of Phosphate Group |
| Record Nr. | UNINA-9910821480603321 |
|
Ham Bryan M
|
||
| Hoboken, N.J., : John Wiley & Sons, 2012 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
