000			04517nam a22004935i 4500
001			978-3-7091-0885-7
003			DE-He213
005			20160615110248.0
007			cr nn 008mamaa
008			140121s2013 au | s |||| 0|eng d
020			_a9783709108857 _9978-3-7091-0885-7
024	7		_a10.1007/978-3-7091-0885-7 _2doi
049			_aAlfaisal Main Library
050		4	_aQD431-431.7
072		7	_aPSBZ _2bicssc
072		7	_aSCI007000 _2bisacsh
082	0	4	_a572.6 _223
245	1	0	_aProteases: Structure and Function _h[electronic resource] / _cedited by Klaudia Brix, Walter Stöcker.
264		1	_aVienna : _bSpringer Vienna : _bImprint: Springer, _c2013.
300			_aXII, 564 p. 98 illus., 65 illus. in color. _bonline resource.
336			_atext _btxt _2rdacontent
337			_acomputer _bc _2rdamedia
338			_aonline resource _bcr _2rdacarrier
347			_atext file _bPDF _2rda
505	0		_a1 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			_aProteolysis 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	_aLife sciences.
650		0	_aProteins.
650		0	_aEnzymology.
650	1	4	_aLife Sciences.
650	2	4	_aEnzymology.
650	2	4	_aProtein Structure.
650	2	4	_aProtein Science.
655		7	_aElectronic books. _2local
700	1		_aBrix, Klaudia. _eeditor.
700	1		_aStöcker, Walter. _eeditor.
710	2		_aSpringerLink (Online service)
773	0		_tSpringer eBooks
776	0	8	_iPrinted edition: _z9783709108840
856	4	0	_uhttp://ezproxy.alfaisal.edu/login?url=http://dx.doi.org/10.1007/978-3-7091-0885-7
912			_aZDB-2-SBL
942			_2lcc _cEBOOKS
999			_c280001 _d280001