Proteases: Structure and Function (Record no. 98954)

000 -LEADER
fixed length control field 04371nam a22004575i 4500
001 - CONTROL NUMBER
control field 978-3-7091-0885-7
003 - CONTROL NUMBER IDENTIFIER
control field DE-He213
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20140220082925.0
007 - PHYSICAL DESCRIPTION FIXED FIELD--GENERAL INFORMATION
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008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 140121s2013 au | s |||| 0|eng d
020 ## - INTERNATIONAL STANDARD BOOK NUMBER
International Standard Book Number 9783709108857
-- 978-3-7091-0885-7
024 7# - OTHER STANDARD IDENTIFIER
Standard number or code 10.1007/978-3-7091-0885-7
Source of number or code doi
050 #4 - LIBRARY OF CONGRESS CALL NUMBER
Classification number QD431-431.7
072 #7 - SUBJECT CATEGORY CODE
Subject category code PSBZ
Source bicssc
072 #7 - SUBJECT CATEGORY CODE
Subject category code SCI007000
Source bisacsh
082 04 - DEWEY DECIMAL CLASSIFICATION NUMBER
Classification number 572.6
Edition number 23
100 1# - MAIN ENTRY--PERSONAL NAME
Personal name Brix, Klaudia.
Relator term editor.
245 10 - TITLE STATEMENT
Title Proteases: Structure and Function
Medium [electronic resource] /
Statement of responsibility, etc edited by Klaudia Brix, Walter Stöcker.
264 #1 -
-- Vienna :
-- Springer Vienna :
-- Imprint: Springer,
-- 2013.
300 ## - PHYSICAL DESCRIPTION
Extent XII, 564 p. 98 illus., 65 illus. in color.
Other physical details online resource.
336 ## -
-- text
-- txt
-- rdacontent
337 ## -
-- computer
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-- rdamedia
338 ## -
-- online resource
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-- rdacarrier
347 ## -
-- text file
-- PDF
-- rda
505 0# - FORMATTED CONTENTS NOTE
Formatted contents note 1 Protease families, evolution and mechanisms of action "Set the stage" -- 1.1 Enzyme families, prototypes and catalytic mechanisms --  1.2 Enzyme kinetics, mathematical modelling and perspectives --  1.3 Structure determination and search for inhibitors -- 2 Regulation of proteolysis "Positioning and teaming-up to control activity" -- 2.1 Compartmentalization of proteolysis -- 2.2 Biosynthesis of lysosomal proteases -- 2.3 Interactions of proteases and inhibitors / networking in the degradome -- 2.4 In vivo analysis of the protease and inhibitors concert -- 3 Proteases in development "Born to be right" -- 3.1 Proteases for pattern formation during morphogenesis -- 3.2 Proteases in death pathways (apoptosis, necrosis) -- 4 Proteases in physiology and pathophysiology „Cleave to function in health or to cause disease" -- 4.1 Protein turnover and signaling functions (degrade to rebuild, remodel, process and mature for signalling) -- 4.2 Proteases in control of physiology -- 4.3 Cancer: invasion and metastasis -- 4.4 Bacterial proteases -- 4.5 Viral proteases.
520 ## - SUMMARY, ETC.
Summary, etc Proteolysis is an irreversible posttranslational modification affecting each and every protein from its biosynthesis to its degradation. Limited proteolysis regulates targeting and activity throughout the lifetime of proteins. Balancing proteolysis is therefore crucial for physiological homeostasis. Control mechanisms include proteolytic maturation of zymogens resulting in active proteases and the shut down of proteolysis by counteracting endogenous protease inhibitors. Beyond the protein level, proteolytic enzymes are involved in key decisions during development that determine life and death – from single cells to adult individuals. In particular, we are becoming aware of the subtle role that proteases play in signaling events within proteolysis networks, in which the enzymes act synergistically and form alliances in a web-like fashion. Proteases come in different flavors. At least five families of mechanistically distinct enzymes and even more inhibitor families are known to date, many family members are still to be studied in detail. We have learned a lot about the diversity of the about 600 proteases in the human genome and begin to understand their physiological roles in the degradome. However, there are still many open questions regarding their actions in pathophysiology. It is in this area where the development of small molecule inhibitors as therapeutic agents is extremely promising. Approaching proteolysis as the most important, irreversible post-translational protein modification essentially requires an integrated effort of complementary research disciplines. In fact, proteolytic enzymes seem as diverse as the scientists working with these intriguing proteins. This book reflects the efforts of many in this exciting field of research where team and network formations are essential to move ahead.
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Life sciences.
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Biochemistry.
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Enzymes.
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Life Sciences.
650 24 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Enzymology.
650 24 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Protein Structure.
650 24 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Protein Science.
700 1# - ADDED ENTRY--PERSONAL NAME
Personal name Stöcker, Walter.
Relator term editor.
710 2# - ADDED ENTRY--CORPORATE NAME
Corporate name or jurisdiction name as entry element SpringerLink (Online service)
773 0# - HOST ITEM ENTRY
Title Springer eBooks
776 08 - ADDITIONAL PHYSICAL FORM ENTRY
Display text Printed edition:
International Standard Book Number 9783709108840
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier http://dx.doi.org/10.1007/978-3-7091-0885-7
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