Emerging technologies for protease engineering: New tools to clear out disease

Proteases regulate many biological processes through their ability to activate or inactive their target substrates. Because proteases catalytically turnover proteins and peptides, they present unique opportunities for use in biotechnological and therapeutic applications. However, many proteases are...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Jennifer L Guerrero [verfasserIn] Patrick S Daugherty Michelle A O'Malley

Format:	Artikel
Sprache:	Englisch

Erschienen:	2017

Schlagwörter:	Toxicity Proteases Catalysis Biomedical engineering

Übergeordnetes Werk:	Enthalten in: Biotechnology and bioengineering - New York, NY [u.a.] : Wiley, 1962, 114(2017), 1, Seite 33
Übergeordnetes Werk:	volume:114 ; year:2017 ; number:1 ; pages:33

Links:	Volltext Link aufrufen

DOI / URN:	10.1002/bit.26066

Katalog-ID:	OLC1988598397

Internformat


LEADER	01000caa a2200265 4500
001	OLC1988598397
003	DE-627
005	20230511164307.0
007	tu
008	170207s2017 xx \|\|\|\|\| 00\| \|\|eng c
024	7		\|a 10.1002/bit.26066 \|2 doi
028	5	2	\|a PQ20170206
035			\|a (DE-627)OLC1988598397
035			\|a (DE-599)GBVOLC1988598397
035			\|a (PRQ)p1171-1d8e1d31b09636aac2cc772222bd19450fbc5a622ffde43cdbff7bff18b496763
035			\|a (KEY)0118076220170000114000100033emergingtechnologiesforproteaseengineeringnewtools
040			\|a DE-627 \|b ger \|c DE-627 \|e rakwb
041			\|a eng
082	0	4	\|a 570 \|q DNB
084			\|a BIODIV \|2 fid
084			\|a 58.30 \|2 bkl
100	0		\|a Jennifer L Guerrero \|e verfasserin \|4 aut
245	1	0	\|a Emerging technologies for protease engineering: New tools to clear out disease
264		1	\|c 2017
336			\|a Text \|b txt \|2 rdacontent
337			\|a ohne Hilfsmittel zu benutzen \|b n \|2 rdamedia
338			\|a Band \|b nc \|2 rdacarrier
520			\|a Proteases regulate many biological processes through their ability to activate or inactive their target substrates. Because proteases catalytically turnover proteins and peptides, they present unique opportunities for use in biotechnological and therapeutic applications. However, many proteases are capable of cleaving multiple physiological substrates. Therefore their activity, expression, and localization are tightly controlled to prevent unwanted proteolysis. Currently, the use of protease therapeutics has been limited to a handful of proteases with narrow substrate specificities, which naturally limits their toxicity. Wider application of proteases is contingent upon the development of methods for engineering protease selectivity, activity, and stability. Recent advances in the development of high-throughput, bacterial and yeast-based methods for protease redesign have yielded protease variants with novel specificities, reduced toxicity, and increased resistance to inhibitors. Here, we highlight new tools for protease engineering, including methods suitable for the redesign of human secreted proteases, and future opportunities to exploit the catalytic activity of proteases for therapeutic benefit. Biotechnol. Bioeng. 2017;114: 33-38. © 2016 Wiley Periodicals, Inc.
650		4	\|a Toxicity
650		4	\|a Proteases
650		4	\|a Catalysis
650		4	\|a Biomedical engineering
700	0		\|a Patrick S Daugherty \|4 oth
700	0		\|a Michelle A O'Malley \|4 oth
773	0	8	\|i Enthalten in \|t Biotechnology and bioengineering \|d New York, NY [u.a.] : Wiley, 1962 \|g 114(2017), 1, Seite 33 \|w (DE-627)129851000 \|w (DE-600)280318-5 \|w (DE-576)015150194 \|x 0006-3592 \|7 nnns
773	1	8	\|g volume:114 \|g year:2017 \|g number:1 \|g pages:33
856	4	1	\|u http://dx.doi.org/10.1002/bit.26066 \|3 Volltext
856	4	2	\|u http://search.proquest.com/docview/1844749274
912			\|a GBV_USEFLAG_A
912			\|a SYSFLAG_A
912			\|a GBV_OLC
912			\|a FID-BIODIV
912			\|a SSG-OLC-TEC
912			\|a SSG-OLC-CHE
912			\|a SSG-OLC-PHA
912			\|a SSG-OLC-DE-84
912			\|a SSG-OPC-FOR
912			\|a GBV_ILN_70
912			\|a GBV_ILN_215
912			\|a GBV_ILN_4012
936	b	k	\|a 58.30 \|q AVZ
951			\|a AR
952			\|d 114 \|j 2017 \|e 1 \|h 33

Indexfelder

author_variant	j l g jlg
matchkey_str	article:00063592:2017----::mrigehooisopoesegneigeto
hierarchy_sort_str	2017
bklnumber	58.30
publishDate	2017
allfields	10.1002/bit.26066 doi PQ20170206 (DE-627)OLC1988598397 (DE-599)GBVOLC1988598397 (PRQ)p1171-1d8e1d31b09636aac2cc772222bd19450fbc5a622ffde43cdbff7bff18b496763 (KEY)0118076220170000114000100033emergingtechnologiesforproteaseengineeringnewtools DE-627 ger DE-627 rakwb eng 570 DNB BIODIV fid 58.30 bkl Jennifer L Guerrero verfasserin aut Emerging technologies for protease engineering: New tools to clear out disease 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Proteases regulate many biological processes through their ability to activate or inactive their target substrates. Because proteases catalytically turnover proteins and peptides, they present unique opportunities for use in biotechnological and therapeutic applications. However, many proteases are capable of cleaving multiple physiological substrates. Therefore their activity, expression, and localization are tightly controlled to prevent unwanted proteolysis. Currently, the use of protease therapeutics has been limited to a handful of proteases with narrow substrate specificities, which naturally limits their toxicity. Wider application of proteases is contingent upon the development of methods for engineering protease selectivity, activity, and stability. Recent advances in the development of high-throughput, bacterial and yeast-based methods for protease redesign have yielded protease variants with novel specificities, reduced toxicity, and increased resistance to inhibitors. Here, we highlight new tools for protease engineering, including methods suitable for the redesign of human secreted proteases, and future opportunities to exploit the catalytic activity of proteases for therapeutic benefit. Biotechnol. Bioeng. 2017;114: 33-38. © 2016 Wiley Periodicals, Inc. Toxicity Proteases Catalysis Biomedical engineering Patrick S Daugherty oth Michelle A O'Malley oth Enthalten in Biotechnology and bioengineering New York, NY [u.a.] : Wiley, 1962 114(2017), 1, Seite 33 (DE-627)129851000 (DE-600)280318-5 (DE-576)015150194 0006-3592 nnns volume:114 year:2017 number:1 pages:33 http://dx.doi.org/10.1002/bit.26066 Volltext http://search.proquest.com/docview/1844749274 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_70 GBV_ILN_215 GBV_ILN_4012 58.30 AVZ AR 114 2017 1 33
spelling	10.1002/bit.26066 doi PQ20170206 (DE-627)OLC1988598397 (DE-599)GBVOLC1988598397 (PRQ)p1171-1d8e1d31b09636aac2cc772222bd19450fbc5a622ffde43cdbff7bff18b496763 (KEY)0118076220170000114000100033emergingtechnologiesforproteaseengineeringnewtools DE-627 ger DE-627 rakwb eng 570 DNB BIODIV fid 58.30 bkl Jennifer L Guerrero verfasserin aut Emerging technologies for protease engineering: New tools to clear out disease 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Proteases regulate many biological processes through their ability to activate or inactive their target substrates. Because proteases catalytically turnover proteins and peptides, they present unique opportunities for use in biotechnological and therapeutic applications. However, many proteases are capable of cleaving multiple physiological substrates. Therefore their activity, expression, and localization are tightly controlled to prevent unwanted proteolysis. Currently, the use of protease therapeutics has been limited to a handful of proteases with narrow substrate specificities, which naturally limits their toxicity. Wider application of proteases is contingent upon the development of methods for engineering protease selectivity, activity, and stability. Recent advances in the development of high-throughput, bacterial and yeast-based methods for protease redesign have yielded protease variants with novel specificities, reduced toxicity, and increased resistance to inhibitors. Here, we highlight new tools for protease engineering, including methods suitable for the redesign of human secreted proteases, and future opportunities to exploit the catalytic activity of proteases for therapeutic benefit. Biotechnol. Bioeng. 2017;114: 33-38. © 2016 Wiley Periodicals, Inc. Toxicity Proteases Catalysis Biomedical engineering Patrick S Daugherty oth Michelle A O'Malley oth Enthalten in Biotechnology and bioengineering New York, NY [u.a.] : Wiley, 1962 114(2017), 1, Seite 33 (DE-627)129851000 (DE-600)280318-5 (DE-576)015150194 0006-3592 nnns volume:114 year:2017 number:1 pages:33 http://dx.doi.org/10.1002/bit.26066 Volltext http://search.proquest.com/docview/1844749274 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_70 GBV_ILN_215 GBV_ILN_4012 58.30 AVZ AR 114 2017 1 33
allfields_unstemmed	10.1002/bit.26066 doi PQ20170206 (DE-627)OLC1988598397 (DE-599)GBVOLC1988598397 (PRQ)p1171-1d8e1d31b09636aac2cc772222bd19450fbc5a622ffde43cdbff7bff18b496763 (KEY)0118076220170000114000100033emergingtechnologiesforproteaseengineeringnewtools DE-627 ger DE-627 rakwb eng 570 DNB BIODIV fid 58.30 bkl Jennifer L Guerrero verfasserin aut Emerging technologies for protease engineering: New tools to clear out disease 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Proteases regulate many biological processes through their ability to activate or inactive their target substrates. Because proteases catalytically turnover proteins and peptides, they present unique opportunities for use in biotechnological and therapeutic applications. However, many proteases are capable of cleaving multiple physiological substrates. Therefore their activity, expression, and localization are tightly controlled to prevent unwanted proteolysis. Currently, the use of protease therapeutics has been limited to a handful of proteases with narrow substrate specificities, which naturally limits their toxicity. Wider application of proteases is contingent upon the development of methods for engineering protease selectivity, activity, and stability. Recent advances in the development of high-throughput, bacterial and yeast-based methods for protease redesign have yielded protease variants with novel specificities, reduced toxicity, and increased resistance to inhibitors. Here, we highlight new tools for protease engineering, including methods suitable for the redesign of human secreted proteases, and future opportunities to exploit the catalytic activity of proteases for therapeutic benefit. Biotechnol. Bioeng. 2017;114: 33-38. © 2016 Wiley Periodicals, Inc. Toxicity Proteases Catalysis Biomedical engineering Patrick S Daugherty oth Michelle A O'Malley oth Enthalten in Biotechnology and bioengineering New York, NY [u.a.] : Wiley, 1962 114(2017), 1, Seite 33 (DE-627)129851000 (DE-600)280318-5 (DE-576)015150194 0006-3592 nnns volume:114 year:2017 number:1 pages:33 http://dx.doi.org/10.1002/bit.26066 Volltext http://search.proquest.com/docview/1844749274 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_70 GBV_ILN_215 GBV_ILN_4012 58.30 AVZ AR 114 2017 1 33
allfieldsGer	10.1002/bit.26066 doi PQ20170206 (DE-627)OLC1988598397 (DE-599)GBVOLC1988598397 (PRQ)p1171-1d8e1d31b09636aac2cc772222bd19450fbc5a622ffde43cdbff7bff18b496763 (KEY)0118076220170000114000100033emergingtechnologiesforproteaseengineeringnewtools DE-627 ger DE-627 rakwb eng 570 DNB BIODIV fid 58.30 bkl Jennifer L Guerrero verfasserin aut Emerging technologies for protease engineering: New tools to clear out disease 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Proteases regulate many biological processes through their ability to activate or inactive their target substrates. Because proteases catalytically turnover proteins and peptides, they present unique opportunities for use in biotechnological and therapeutic applications. However, many proteases are capable of cleaving multiple physiological substrates. Therefore their activity, expression, and localization are tightly controlled to prevent unwanted proteolysis. Currently, the use of protease therapeutics has been limited to a handful of proteases with narrow substrate specificities, which naturally limits their toxicity. Wider application of proteases is contingent upon the development of methods for engineering protease selectivity, activity, and stability. Recent advances in the development of high-throughput, bacterial and yeast-based methods for protease redesign have yielded protease variants with novel specificities, reduced toxicity, and increased resistance to inhibitors. Here, we highlight new tools for protease engineering, including methods suitable for the redesign of human secreted proteases, and future opportunities to exploit the catalytic activity of proteases for therapeutic benefit. Biotechnol. Bioeng. 2017;114: 33-38. © 2016 Wiley Periodicals, Inc. Toxicity Proteases Catalysis Biomedical engineering Patrick S Daugherty oth Michelle A O'Malley oth Enthalten in Biotechnology and bioengineering New York, NY [u.a.] : Wiley, 1962 114(2017), 1, Seite 33 (DE-627)129851000 (DE-600)280318-5 (DE-576)015150194 0006-3592 nnns volume:114 year:2017 number:1 pages:33 http://dx.doi.org/10.1002/bit.26066 Volltext http://search.proquest.com/docview/1844749274 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_70 GBV_ILN_215 GBV_ILN_4012 58.30 AVZ AR 114 2017 1 33
allfieldsSound	10.1002/bit.26066 doi PQ20170206 (DE-627)OLC1988598397 (DE-599)GBVOLC1988598397 (PRQ)p1171-1d8e1d31b09636aac2cc772222bd19450fbc5a622ffde43cdbff7bff18b496763 (KEY)0118076220170000114000100033emergingtechnologiesforproteaseengineeringnewtools DE-627 ger DE-627 rakwb eng 570 DNB BIODIV fid 58.30 bkl Jennifer L Guerrero verfasserin aut Emerging technologies for protease engineering: New tools to clear out disease 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Proteases regulate many biological processes through their ability to activate or inactive their target substrates. Because proteases catalytically turnover proteins and peptides, they present unique opportunities for use in biotechnological and therapeutic applications. However, many proteases are capable of cleaving multiple physiological substrates. Therefore their activity, expression, and localization are tightly controlled to prevent unwanted proteolysis. Currently, the use of protease therapeutics has been limited to a handful of proteases with narrow substrate specificities, which naturally limits their toxicity. Wider application of proteases is contingent upon the development of methods for engineering protease selectivity, activity, and stability. Recent advances in the development of high-throughput, bacterial and yeast-based methods for protease redesign have yielded protease variants with novel specificities, reduced toxicity, and increased resistance to inhibitors. Here, we highlight new tools for protease engineering, including methods suitable for the redesign of human secreted proteases, and future opportunities to exploit the catalytic activity of proteases for therapeutic benefit. Biotechnol. Bioeng. 2017;114: 33-38. © 2016 Wiley Periodicals, Inc. Toxicity Proteases Catalysis Biomedical engineering Patrick S Daugherty oth Michelle A O'Malley oth Enthalten in Biotechnology and bioengineering New York, NY [u.a.] : Wiley, 1962 114(2017), 1, Seite 33 (DE-627)129851000 (DE-600)280318-5 (DE-576)015150194 0006-3592 nnns volume:114 year:2017 number:1 pages:33 http://dx.doi.org/10.1002/bit.26066 Volltext http://search.proquest.com/docview/1844749274 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_70 GBV_ILN_215 GBV_ILN_4012 58.30 AVZ AR 114 2017 1 33
language	English
source	Enthalten in Biotechnology and bioengineering 114(2017), 1, Seite 33 volume:114 year:2017 number:1 pages:33
sourceStr	Enthalten in Biotechnology and bioengineering 114(2017), 1, Seite 33 volume:114 year:2017 number:1 pages:33
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Toxicity Proteases Catalysis Biomedical engineering
dewey-raw	570
isfreeaccess_bool	false
container_title	Biotechnology and bioengineering
authorswithroles_txt_mv	Jennifer L Guerrero @@aut@@ Patrick S Daugherty @@oth@@ Michelle A O'Malley @@oth@@
publishDateDaySort_date	2017-01-01T00:00:00Z
hierarchy_top_id	129851000
dewey-sort	3570
id	OLC1988598397
language_de	englisch
fullrecord	<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a2200265 4500</leader><controlfield tag="001">OLC1988598397</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230511164307.0</controlfield><controlfield tag="007">tu</controlfield><controlfield tag="008">170207s2017 xx \|\|\|\|\| 00\| \|\|eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1002/bit.26066</subfield><subfield code="2">doi</subfield></datafield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">PQ20170206</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)OLC1988598397</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVOLC1988598397</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(PRQ)p1171-1d8e1d31b09636aac2cc772222bd19450fbc5a622ffde43cdbff7bff18b496763</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(KEY)0118076220170000114000100033emergingtechnologiesforproteaseengineeringnewtools</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">570</subfield><subfield code="q">DNB</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">BIODIV</subfield><subfield code="2">fid</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">58.30</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="0" ind2=" "><subfield code="a">Jennifer L Guerrero</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Emerging technologies for protease engineering: New tools to clear out disease</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2017</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Proteases regulate many biological processes through their ability to activate or inactive their target substrates. Because proteases catalytically turnover proteins and peptides, they present unique opportunities for use in biotechnological and therapeutic applications. However, many proteases are capable of cleaving multiple physiological substrates. Therefore their activity, expression, and localization are tightly controlled to prevent unwanted proteolysis. Currently, the use of protease therapeutics has been limited to a handful of proteases with narrow substrate specificities, which naturally limits their toxicity. Wider application of proteases is contingent upon the development of methods for engineering protease selectivity, activity, and stability. Recent advances in the development of high-throughput, bacterial and yeast-based methods for protease redesign have yielded protease variants with novel specificities, reduced toxicity, and increased resistance to inhibitors. Here, we highlight new tools for protease engineering, including methods suitable for the redesign of human secreted proteases, and future opportunities to exploit the catalytic activity of proteases for therapeutic benefit. Biotechnol. Bioeng. 2017;114: 33-38. © 2016 Wiley Periodicals, Inc.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Toxicity</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Proteases</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Catalysis</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Biomedical engineering</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Patrick S Daugherty</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Michelle A O'Malley</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Biotechnology and bioengineering</subfield><subfield code="d">New York, NY [u.a.] : Wiley, 1962</subfield><subfield code="g">114(2017), 1, Seite 33</subfield><subfield code="w">(DE-627)129851000</subfield><subfield code="w">(DE-600)280318-5</subfield><subfield code="w">(DE-576)015150194</subfield><subfield code="x">0006-3592</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:114</subfield><subfield code="g">year:2017</subfield><subfield code="g">number:1</subfield><subfield code="g">pages:33</subfield></datafield><datafield tag="856" ind1="4" ind2="1"><subfield code="u">http://dx.doi.org/10.1002/bit.26066</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://search.proquest.com/docview/1844749274</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_OLC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">FID-BIODIV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-TEC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-CHE</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-DE-84</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OPC-FOR</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_70</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_215</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4012</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">58.30</subfield><subfield code="q">AVZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">114</subfield><subfield code="j">2017</subfield><subfield code="e">1</subfield><subfield code="h">33</subfield></datafield></record></collection>
author	Jennifer L Guerrero
spellingShingle	Jennifer L Guerrero ddc 570 fid BIODIV bkl 58.30 misc Toxicity misc Proteases misc Catalysis misc Biomedical engineering Emerging technologies for protease engineering: New tools to clear out disease
authorStr	Jennifer L Guerrero
ppnlink_with_tag_str_mv	@@773@@(DE-627)129851000
format	Article
dewey-ones	570 - Life sciences; biology
delete_txt_mv	keep
author_role	aut
collection	OLC
remote_str	false
illustrated	Not Illustrated
issn	0006-3592
topic_title	570 DNB BIODIV fid 58.30 bkl Emerging technologies for protease engineering: New tools to clear out disease Toxicity Proteases Catalysis Biomedical engineering
topic	ddc 570 fid BIODIV bkl 58.30 misc Toxicity misc Proteases misc Catalysis misc Biomedical engineering
topic_unstemmed	ddc 570 fid BIODIV bkl 58.30 misc Toxicity misc Proteases misc Catalysis misc Biomedical engineering
topic_browse	ddc 570 fid BIODIV bkl 58.30 misc Toxicity misc Proteases misc Catalysis misc Biomedical engineering
format_facet	Aufsätze Gedruckte Aufsätze
format_main_str_mv	Text Zeitschrift/Artikel
carriertype_str_mv	nc
author2_variant	p s d psd m a o mao
hierarchy_parent_title	Biotechnology and bioengineering
hierarchy_parent_id	129851000
dewey-tens	570 - Life sciences; biology
hierarchy_top_title	Biotechnology and bioengineering
isfreeaccess_txt	false
familylinks_str_mv	(DE-627)129851000 (DE-600)280318-5 (DE-576)015150194
title	Emerging technologies for protease engineering: New tools to clear out disease
ctrlnum	(DE-627)OLC1988598397 (DE-599)GBVOLC1988598397 (PRQ)p1171-1d8e1d31b09636aac2cc772222bd19450fbc5a622ffde43cdbff7bff18b496763 (KEY)0118076220170000114000100033emergingtechnologiesforproteaseengineeringnewtools
title_full	Emerging technologies for protease engineering: New tools to clear out disease
author_sort	Jennifer L Guerrero
journal	Biotechnology and bioengineering
journalStr	Biotechnology and bioengineering
lang_code	eng
isOA_bool	false
dewey-hundreds	500 - Science
recordtype	marc
publishDateSort	2017
contenttype_str_mv	txt
container_start_page	33
author_browse	Jennifer L Guerrero
container_volume	114
class	570 DNB BIODIV fid 58.30 bkl
format_se	Aufsätze
author-letter	Jennifer L Guerrero
doi_str_mv	10.1002/bit.26066
dewey-full	570
title_sort	emerging technologies for protease engineering: new tools to clear out disease
title_auth	Emerging technologies for protease engineering: New tools to clear out disease
abstract	Proteases regulate many biological processes through their ability to activate or inactive their target substrates. Because proteases catalytically turnover proteins and peptides, they present unique opportunities for use in biotechnological and therapeutic applications. However, many proteases are capable of cleaving multiple physiological substrates. Therefore their activity, expression, and localization are tightly controlled to prevent unwanted proteolysis. Currently, the use of protease therapeutics has been limited to a handful of proteases with narrow substrate specificities, which naturally limits their toxicity. Wider application of proteases is contingent upon the development of methods for engineering protease selectivity, activity, and stability. Recent advances in the development of high-throughput, bacterial and yeast-based methods for protease redesign have yielded protease variants with novel specificities, reduced toxicity, and increased resistance to inhibitors. Here, we highlight new tools for protease engineering, including methods suitable for the redesign of human secreted proteases, and future opportunities to exploit the catalytic activity of proteases for therapeutic benefit. Biotechnol. Bioeng. 2017;114: 33-38. © 2016 Wiley Periodicals, Inc.
abstractGer	Proteases regulate many biological processes through their ability to activate or inactive their target substrates. Because proteases catalytically turnover proteins and peptides, they present unique opportunities for use in biotechnological and therapeutic applications. However, many proteases are capable of cleaving multiple physiological substrates. Therefore their activity, expression, and localization are tightly controlled to prevent unwanted proteolysis. Currently, the use of protease therapeutics has been limited to a handful of proteases with narrow substrate specificities, which naturally limits their toxicity. Wider application of proteases is contingent upon the development of methods for engineering protease selectivity, activity, and stability. Recent advances in the development of high-throughput, bacterial and yeast-based methods for protease redesign have yielded protease variants with novel specificities, reduced toxicity, and increased resistance to inhibitors. Here, we highlight new tools for protease engineering, including methods suitable for the redesign of human secreted proteases, and future opportunities to exploit the catalytic activity of proteases for therapeutic benefit. Biotechnol. Bioeng. 2017;114: 33-38. © 2016 Wiley Periodicals, Inc.
abstract_unstemmed	Proteases regulate many biological processes through their ability to activate or inactive their target substrates. Because proteases catalytically turnover proteins and peptides, they present unique opportunities for use in biotechnological and therapeutic applications. However, many proteases are capable of cleaving multiple physiological substrates. Therefore their activity, expression, and localization are tightly controlled to prevent unwanted proteolysis. Currently, the use of protease therapeutics has been limited to a handful of proteases with narrow substrate specificities, which naturally limits their toxicity. Wider application of proteases is contingent upon the development of methods for engineering protease selectivity, activity, and stability. Recent advances in the development of high-throughput, bacterial and yeast-based methods for protease redesign have yielded protease variants with novel specificities, reduced toxicity, and increased resistance to inhibitors. Here, we highlight new tools for protease engineering, including methods suitable for the redesign of human secreted proteases, and future opportunities to exploit the catalytic activity of proteases for therapeutic benefit. Biotechnol. Bioeng. 2017;114: 33-38. © 2016 Wiley Periodicals, Inc.
collection_details	GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_70 GBV_ILN_215 GBV_ILN_4012
container_issue	1
title_short	Emerging technologies for protease engineering: New tools to clear out disease
url	http://dx.doi.org/10.1002/bit.26066 http://search.proquest.com/docview/1844749274
remote_bool	false
author2	Patrick S Daugherty Michelle A O'Malley
author2Str	Patrick S Daugherty Michelle A O'Malley
ppnlink	129851000
mediatype_str_mv	n
isOA_txt	false
hochschulschrift_bool	false
author2_role	oth oth
doi_str	10.1002/bit.26066
up_date	2024-07-03T18:28:50.914Z
_version_	1803583572849721344
fullrecord_marcxml	<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a2200265 4500</leader><controlfield tag="001">OLC1988598397</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230511164307.0</controlfield><controlfield tag="007">tu</controlfield><controlfield tag="008">170207s2017 xx \|\|\|\|\| 00\| \|\|eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1002/bit.26066</subfield><subfield code="2">doi</subfield></datafield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">PQ20170206</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)OLC1988598397</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVOLC1988598397</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(PRQ)p1171-1d8e1d31b09636aac2cc772222bd19450fbc5a622ffde43cdbff7bff18b496763</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(KEY)0118076220170000114000100033emergingtechnologiesforproteaseengineeringnewtools</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">570</subfield><subfield code="q">DNB</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">BIODIV</subfield><subfield code="2">fid</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">58.30</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="0" ind2=" "><subfield code="a">Jennifer L Guerrero</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Emerging technologies for protease engineering: New tools to clear out disease</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2017</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Proteases regulate many biological processes through their ability to activate or inactive their target substrates. Because proteases catalytically turnover proteins and peptides, they present unique opportunities for use in biotechnological and therapeutic applications. However, many proteases are capable of cleaving multiple physiological substrates. Therefore their activity, expression, and localization are tightly controlled to prevent unwanted proteolysis. Currently, the use of protease therapeutics has been limited to a handful of proteases with narrow substrate specificities, which naturally limits their toxicity. Wider application of proteases is contingent upon the development of methods for engineering protease selectivity, activity, and stability. Recent advances in the development of high-throughput, bacterial and yeast-based methods for protease redesign have yielded protease variants with novel specificities, reduced toxicity, and increased resistance to inhibitors. Here, we highlight new tools for protease engineering, including methods suitable for the redesign of human secreted proteases, and future opportunities to exploit the catalytic activity of proteases for therapeutic benefit. Biotechnol. Bioeng. 2017;114: 33-38. © 2016 Wiley Periodicals, Inc.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Toxicity</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Proteases</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Catalysis</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Biomedical engineering</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Patrick S Daugherty</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Michelle A O'Malley</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Biotechnology and bioengineering</subfield><subfield code="d">New York, NY [u.a.] : Wiley, 1962</subfield><subfield code="g">114(2017), 1, Seite 33</subfield><subfield code="w">(DE-627)129851000</subfield><subfield code="w">(DE-600)280318-5</subfield><subfield code="w">(DE-576)015150194</subfield><subfield code="x">0006-3592</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:114</subfield><subfield code="g">year:2017</subfield><subfield code="g">number:1</subfield><subfield code="g">pages:33</subfield></datafield><datafield tag="856" ind1="4" ind2="1"><subfield code="u">http://dx.doi.org/10.1002/bit.26066</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://search.proquest.com/docview/1844749274</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_OLC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">FID-BIODIV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-TEC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-CHE</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-DE-84</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OPC-FOR</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_70</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_215</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4012</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">58.30</subfield><subfield code="q">AVZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">114</subfield><subfield code="j">2017</subfield><subfield code="e">1</subfield><subfield code="h">33</subfield></datafield></record></collection>
score	7.4002085

Nicht das Richtige dabei?

Schreiben Sie uns!

Emerging technologies for protease engineering: New tools to clear out disease

Nicht das Richtige dabei?

Zugang & Verfügbarkeit

Vorhandene Bände

Nicht das Richtige dabei?