Structure, function and inhibition of ClpP proteases:
Gespeichert in:
| 1. Verfasser: | |
|---|---|
| Format: | Abschlussarbeit Buch |
| Sprache: | English |
| Veröffentlicht: |
München
Verlag Dr. Hut
2014
|
| Ausgabe: | 1. Auflage |
| Schriftenreihe: | Biochemie
|
| Schlagworte: | |
| Online-Zugang: | Inhaltstext Inhaltsverzeichnis |
| Beschreibung: | XIII, 202 Seiten Illustrationen, Diagramme 240 mm x 170 mm, 416 g |
| ISBN: | 9783843913942 3843913943 |
Internformat
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Datensatz im Suchindex
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| adam_text |
XII
TABLE OF CONTENTS
SUMMARY V
ZUSAMMENFASSUNG VII
PARTS OF THIS DISSERTATION HAVE BEEN PUBLISHED AS LISTED BELOW: IX
TABLE OF CONTENTS XII
PART I - SCIENTIFIC BACKGROUND AND SUMMARY
1 SCIENTIFIC BACKGROUND AND SUMMARY OF RESULTS 3
1.1 A SHORT INTRODUCTION INTO
PROTEOSTASIS AND PROTEOLYSIS 3
1.2 CASEINOLYTIC PROTEASES 4
1.2.1 STRUCTURE 4
1.2.2 FUNCTION 6
1.2.3 INHIBITION 7
1.3 CONTENTS OF THIS THESIS
8
1.4 REFERENCES 12
PART II - RESEARCH
2 INSIGHTS INTO THE STRUCTURAL NETWORK RESPONSIBLE FOR OLIGOMERIZATION
AND ACTIVITY
OF THE BACTERIAL VIRULENCE REGULATOR CASEINOLYIC PROTEASE P (CIPP) 19
3 THE MECHANISM OF CIPP INHIBITION 39
4 DISRUPTION OF OLIGOMERIZATION AND DEHYDROALANINE FORMATION AS
MECHANISMS FOR
CIPP PROTEASE INHIBITION 71
5 STRUCTURAL AND FUNCTIONAL INSIGHTS INTO CASEINOLYTIC PROTEASES REVEAL
AN
UNPRECEDENTED REGULATION PRINCIPLE OF THEIR CATALYTIC TRIAD 105
5.1 INTRODUCTION 105
5.2 RESULTS & DISCUSSION 106
5.2.1 PEPTIDASE ACTIVITIES OF LMCIPP PROTEINS 106
5.2.2 QUANTIFICATION OF INHIBITOR BINDING TO LMCIPP PROTEINS 107
5.3 METHODS 108
5.4 REFERENCES 110
HTTP://D-NB.INFO/1046741454
6 THE CLEAVAGE SITE SPECIFICITIES OF CIPP PROTEASES 113
6.
1 INTRODUCTION 113
6.2 RESULTS AND DISCUSSION 115
6.2.1 SCREENING FLUOROGENIC SUBSTRATE LIBRARIES 115
6.2.2 ANALYSIS OF CLPP-DERIVED PEPTIDES 119
6.2.3 TOWARD A CHARACTERIZATION OF DISEASE-ASSOCIATED HCIPP PROTEINS 122
6.3 METHODS 125
6.4 REFERENCES 127
7 INTACT-PROTEIN MASS SPECTROMETRY OF PROTEASOME CORE PARTICLES UNRAVELS
INHIBITION
MECHANISMS AND SUBUNIT SPECIFICITY 129
7.1 INTRODUCTION 129
7.1.1 STRUCTURE AND FUNCTION OF THE EUKARYOTIC PROTEASOME 129
7.1.2 THE PROTEASOME AS AN ANTICANCER TARGET 130
7.1.3 SULFONYL FLUORIDES AS NOVEL PROTEASOME INHIBITORS 131
7.2 RESULTS AND DISCUSSION 132
7.2.1 COMPLETE MASS SPECTROMETRY ASSIGNMENT OF 20S CORE PARTICLES 132
7.2.2 SULFONYL FLUORIDES CAUSE FORMATION OF AZIRIDINE IN THE $5 SUBUNIT
136
7.3 METHODS 141
7.4 REFERENCES 141
8 SYNTHESIS OF METHIONINE
ISOTOPOLOGUES FOR USE IN PROTEIN NMR SPECTROSCOPY. 145
8.1 INTRODUCTION 145
8.1.1 PROTEIN NMR SPECTROSCOPY OF LARGE COMPLEXES 145
8.1.2 METHIONINE AS PROBE IN PROTEIN NMR SPECTROSCOPY 146
8.1.3 RECENT EXAMPLES OF THE USE OF METHIONINE IN PROTEIN NMR STUDIES
146
8.2 RESULTS 148
8.3 METHODS 149
8.4 REFERENCES 158
PART III - REVIEWS AND BOOK-CHAPTERS
9 ELECTROPHILIC NATURAL PRODUCTS AND THEIR BIOLOGICAL TARGETS 161
10 MODULATION OF CIPP PROTEASE ACTIVITY: FROM ANTIBIOTICS TO
ANTI-VIRULENCE 187
10.1 INTRODUCTION 187
10.2 THE BIOLOGICAL PROBLEM 187
10.3 THE CHEMICAL CHALLENGE 189
10.4 THE DISCOVERY OF A NOVEL ANTIBIOTIC MECHANISM 190
10.4.1 TARGET IDENTIFICATION 190
10.4.2 TARGET VALIDATION 191
10.4.3 MECHANISM OF ACTION 191
10.5 THE ANTI-
VIRULENCE APPROACH 192
10.6 CONCLUSIONS 194
10.7 REFERENCES 194
10.8 BOXES 195
DANKSAGUNG 201 |
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| dewey-ones | 572 - Biochemistry |
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| dewey-search | 572.763329353 |
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| dewey-tens | 570 - Biology |
| discipline | Biologie Chemie |
| edition | 1. Auflage |
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| spelling | Gersch, Malte Verfasser (DE-588)106659998X aut Structure, function and inhibition of ClpP proteases Malte Matthias Gersch 1. Auflage München Verlag Dr. Hut 2014 XIII, 202 Seiten Illustrationen, Diagramme 240 mm x 170 mm, 416 g txt rdacontent n rdamedia nc rdacarrier Biochemie Dissertation Technische Universität München 2013 Clp Protease (DE-588)4821476-0 gnd rswk-swf Struktur-Aktivitäts-Beziehung (DE-588)4183784-8 gnd rswk-swf Staphylococcus aureus (DE-588)4182912-8 gnd rswk-swf (DE-588)4113937-9 Hochschulschrift gnd-content Staphylococcus aureus (DE-588)4182912-8 s Clp Protease (DE-588)4821476-0 s Struktur-Aktivitäts-Beziehung (DE-588)4183784-8 s DE-604 X:MVB text/html http://deposit.dnb.de/cgi-bin/dokserv?id=4575348&prov=M&dok_var=1&dok_ext=htm Inhaltstext DNB Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=027678119&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Gersch, Malte Structure, function and inhibition of ClpP proteases Clp Protease (DE-588)4821476-0 gnd Struktur-Aktivitäts-Beziehung (DE-588)4183784-8 gnd Staphylococcus aureus (DE-588)4182912-8 gnd |
| subject_GND | (DE-588)4821476-0 (DE-588)4183784-8 (DE-588)4182912-8 (DE-588)4113937-9 |
| title | Structure, function and inhibition of ClpP proteases |
| title_auth | Structure, function and inhibition of ClpP proteases |
| title_exact_search | Structure, function and inhibition of ClpP proteases |
| title_full | Structure, function and inhibition of ClpP proteases Malte Matthias Gersch |
| title_fullStr | Structure, function and inhibition of ClpP proteases Malte Matthias Gersch |
| title_full_unstemmed | Structure, function and inhibition of ClpP proteases Malte Matthias Gersch |
| title_short | Structure, function and inhibition of ClpP proteases |
| title_sort | structure function and inhibition of clpp proteases |
| topic | Clp Protease (DE-588)4821476-0 gnd Struktur-Aktivitäts-Beziehung (DE-588)4183784-8 gnd Staphylococcus aureus (DE-588)4182912-8 gnd |
| topic_facet | Clp Protease Struktur-Aktivitäts-Beziehung Staphylococcus aureus Hochschulschrift |
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