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04462nam a22005055i 4500 |
| 001 - CONTROL NUMBER |
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978-1-4939-1010-6 |
| 003 - CONTROL NUMBER IDENTIFIER |
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DE-He213 |
| 005 - DATE AND TIME OF LATEST TRANSACTION |
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20160405112809.0 |
| 007 - PHYSICAL DESCRIPTION FIXED FIELD--GENERAL INFORMATION |
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cr nn 008mamaa |
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141021s2015 xxu| s |||| 0|eng d |
| 020 ## - INTERNATIONAL STANDARD BOOK NUMBER |
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| International Standard Book Number |
9781493910106 |
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978-1-4939-1010-6 |
| 024 7# - OTHER STANDARD IDENTIFIER |
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| Standard number or code |
10.1007/978-1-4939-1010-6 |
| Source of number or code |
doi |
| 050 #4 - LIBRARY OF CONGRESS CALL NUMBER |
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| Classification number |
QR46 |
| 072 #7 - SUBJECT CATEGORY CODE |
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| Subject category code |
MMFM |
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bicssc |
| 072 #7 - SUBJECT CATEGORY CODE |
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| Subject category code |
MED052000 |
| Source |
bisacsh |
| 082 04 - DEWEY DECIMAL CLASSIFICATION NUMBER |
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| Classification number |
616.9041 |
| Edition number |
23 |
| 100 1# - MAIN ENTRY--PERSONAL NAME |
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| Personal name |
Li, Yanyan. |
| Relator term |
author. |
| 245 10 - TITLE STATEMENT |
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| Title |
Lasso Peptides |
| Medium |
[electronic resource] : |
| Remainder of title |
Bacterial Strategies to Make and Maintain Bioactive Entangled Scaffolds / |
| Statement of responsibility, etc |
by Yanyan Li, Séverine Zirah, Sylvie Rebuffat. |
| 264 #1 - |
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New York, NY : |
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Springer New York : |
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Imprint: Springer, |
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2015. |
| 300 ## - PHYSICAL DESCRIPTION |
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| Extent |
XIII, 103 p. 22 illus., 9 illus. in color. |
| Other physical details |
online resource. |
| 336 ## - |
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text |
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txt |
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rdacontent |
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computer |
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c |
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rdamedia |
| 338 ## - |
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online resource |
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cr |
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rdacarrier |
| 347 ## - |
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text file |
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PDF |
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rda |
| 490 1# - SERIES STATEMENT |
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| Series statement |
SpringerBriefs in Microbiology, |
| International Standard Serial Number |
2191-5385 |
| 505 0# - FORMATTED CONTENTS NOTE |
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| Formatted contents note |
Overview on Lasso Peptide Research -- From the Producer Microorganisms to the Lasso Scaffold -- Biological Activities of Lasso Peptides and Structure-Activity Relationships -- Biosynthesis, Regulation and Export of Lasso Peptides -- Lasso Peptide Bioengineering and Bioprospecting. |
| 520 ## - SUMMARY, ETC. |
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| Summary, etc |
Lasso peptides form a growing family of fascinating ribosomally-synthesized and post-translationally modified peptides produced by bacteria. They contain 15 to 24 residues and share a unique interlocked topology that involves an N-terminal 7 to 9-residue macrolactam ring where the C-terminal tail is threaded and irreversibly trapped. The ring results from the condensation of the N-terminal amino group with a side-chain carboxylate of a glutamate at position 8 or 9, or an aspartate at position 7, 8 or 9. The trapping of the tail involves bulky amino acids located in the tail below and above the ring and/or disulfide bridges connecting the ring and the tail. Lasso peptides are subdivided into three subtypes depending on the absence (class II) or presence of one (class III) or two (class I) disulfide bridges. The lasso topology results in highly compact structures that give to lasso peptides an extraordinary stability towards both protease degradation and denaturing conditions. Lasso peptides are generally receptor antagonists, enzyme inhibitors and/or antibacterial or antiviral (anti-HIV) agents. The lasso scaffold and the associated biological activities shown by lasso peptides on different key targets make them promising molecules with high therapeutic potential. Their application in drug design has been exemplified by the development of an integrin antagonist based on a lasso peptide scaffold. The biosynthesis machinery of lasso peptides is therefore of high biotechnological interest, especially since such highly compact and stable structures have to date revealed inaccessible by peptide synthesis. Lasso peptides are produced from a linear precursor LasA, which undergoes a maturation process involving several steps, in particular cleavage of the leader peptide and cyclization. The post-translational modifications are ensured by a dedicated enzymatic machinery, which is composed of an ATP-dependent cysteine protease (LasB) and a lactam synthetase (LasC) that form an enzymatic complex called lasso synthetase. Microcin J25, produced by Escherichia coli AY25, is the archetype of lasso peptides and the most extensively studied. To date only around forty lasso peptides have been isolated, but genome mining approaches have revealed that they are widely distributed among Proteobacteria and Actinobacteria, particularly in Streptomyces, making available a rich resource of novel lasso peptides and enzyme machineries towards lasso topologies. |
| 650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM |
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| Topical term or geographic name as entry element |
Medicine. |
| 650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM |
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| Topical term or geographic name as entry element |
Immunology. |
| 650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM |
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| Topical term or geographic name as entry element |
Medical microbiology. |
| 650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM |
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| Topical term or geographic name as entry element |
Vaccines. |
| 650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM |
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| Topical term or geographic name as entry element |
Biomedicine. |
| 650 24 - SUBJECT ADDED ENTRY--TOPICAL TERM |
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| Topical term or geographic name as entry element |
Medical Microbiology. |
| 650 24 - SUBJECT ADDED ENTRY--TOPICAL TERM |
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| Topical term or geographic name as entry element |
Immunology. |
| 650 24 - SUBJECT ADDED ENTRY--TOPICAL TERM |
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| Topical term or geographic name as entry element |
Vaccine. |
| 700 1# - ADDED ENTRY--PERSONAL NAME |
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| Personal name |
Zirah, Séverine. |
| Relator term |
author. |
| 700 1# - ADDED ENTRY--PERSONAL NAME |
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| Personal name |
Rebuffat, Sylvie. |
| Relator term |
author. |
| 710 2# - ADDED ENTRY--CORPORATE NAME |
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| Corporate name or jurisdiction name as entry element |
SpringerLink (Online service) |
| 773 0# - HOST ITEM ENTRY |
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| Title |
Springer eBooks |
| 776 08 - ADDITIONAL PHYSICAL FORM ENTRY |
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| Display text |
Printed edition: |
| International Standard Book Number |
9781493910090 |
| 830 #0 - SERIES ADDED ENTRY--UNIFORM TITLE |
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| Uniform title |
SpringerBriefs in Microbiology, |
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2191-5385 |
| 856 40 - ELECTRONIC LOCATION AND ACCESS |
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| Uniform Resource Identifier |
<a href="http://dx.doi.org/10.1007/978-1-4939-1010-6">http://dx.doi.org/10.1007/978-1-4939-1010-6</a> |
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ZDB-2-SBL |
