Mechanisms of ubiquitin transfer by the anaphase-promoting complex

Abstract The anaphase-promoting complex (APC) is a ubiquitin-protein ligase required for the completion of mitosis in all eukaryotes. Recent mechanistic studies reveal how this remarkable enzyme combines specificity in substrate binding with flexibility in ubiquitin transfer, thereby allowing the mo...
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Gespeichert in:

Autor*in:	Matyskiela, Mary E [verfasserIn] Rodrigo-Brenni, Monica C Morgan, David O

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2009

Schlagwörter:	Substrate Binding Substrate Recognition Ring Domain Polyubiquitin Chain Ubiquitin Chain

Anmerkung:	© BioMed Central Ltd 2009

Übergeordnetes Werk:	Enthalten in: Journal of biology - London : BioMed Central, 2002, 8(2009), 10 vom: 26. Okt.
Übergeordnetes Werk:	volume:8 ; year:2009 ; number:10 ; day:26 ; month:10

Links:	Volltext

DOI / URN:	10.1186/jbiol184

Katalog-ID:	SPR030038928

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allfields	10.1186/jbiol184 doi (DE-627)SPR030038928 (SPR)jbiol184-e DE-627 ger DE-627 rakwb eng Matyskiela, Mary E verfasserin aut Mechanisms of ubiquitin transfer by the anaphase-promoting complex 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © BioMed Central Ltd 2009 Abstract The anaphase-promoting complex (APC) is a ubiquitin-protein ligase required for the completion of mitosis in all eukaryotes. Recent mechanistic studies reveal how this remarkable enzyme combines specificity in substrate binding with flexibility in ubiquitin transfer, thereby allowing the modification of multiple lysines on the substrate as well as specific lysines on ubiquitin itself. Substrate Binding (dpeaa)DE-He213 Substrate Recognition (dpeaa)DE-He213 Ring Domain (dpeaa)DE-He213 Polyubiquitin Chain (dpeaa)DE-He213 Ubiquitin Chain (dpeaa)DE-He213 Rodrigo-Brenni, Monica C aut Morgan, David O aut Enthalten in Journal of biology London : BioMed Central, 2002 8(2009), 10 vom: 26. Okt. (DE-627)350258880 (DE-600)2082214-5 1475-4924 nnns volume:8 year:2009 number:10 day:26 month:10 https://dx.doi.org/10.1186/jbiol184 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2153 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 8 2009 10 26 10
spelling	10.1186/jbiol184 doi (DE-627)SPR030038928 (SPR)jbiol184-e DE-627 ger DE-627 rakwb eng Matyskiela, Mary E verfasserin aut Mechanisms of ubiquitin transfer by the anaphase-promoting complex 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © BioMed Central Ltd 2009 Abstract The anaphase-promoting complex (APC) is a ubiquitin-protein ligase required for the completion of mitosis in all eukaryotes. Recent mechanistic studies reveal how this remarkable enzyme combines specificity in substrate binding with flexibility in ubiquitin transfer, thereby allowing the modification of multiple lysines on the substrate as well as specific lysines on ubiquitin itself. Substrate Binding (dpeaa)DE-He213 Substrate Recognition (dpeaa)DE-He213 Ring Domain (dpeaa)DE-He213 Polyubiquitin Chain (dpeaa)DE-He213 Ubiquitin Chain (dpeaa)DE-He213 Rodrigo-Brenni, Monica C aut Morgan, David O aut Enthalten in Journal of biology London : BioMed Central, 2002 8(2009), 10 vom: 26. Okt. (DE-627)350258880 (DE-600)2082214-5 1475-4924 nnns volume:8 year:2009 number:10 day:26 month:10 https://dx.doi.org/10.1186/jbiol184 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2153 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 8 2009 10 26 10
allfields_unstemmed	10.1186/jbiol184 doi (DE-627)SPR030038928 (SPR)jbiol184-e DE-627 ger DE-627 rakwb eng Matyskiela, Mary E verfasserin aut Mechanisms of ubiquitin transfer by the anaphase-promoting complex 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © BioMed Central Ltd 2009 Abstract The anaphase-promoting complex (APC) is a ubiquitin-protein ligase required for the completion of mitosis in all eukaryotes. Recent mechanistic studies reveal how this remarkable enzyme combines specificity in substrate binding with flexibility in ubiquitin transfer, thereby allowing the modification of multiple lysines on the substrate as well as specific lysines on ubiquitin itself. Substrate Binding (dpeaa)DE-He213 Substrate Recognition (dpeaa)DE-He213 Ring Domain (dpeaa)DE-He213 Polyubiquitin Chain (dpeaa)DE-He213 Ubiquitin Chain (dpeaa)DE-He213 Rodrigo-Brenni, Monica C aut Morgan, David O aut Enthalten in Journal of biology London : BioMed Central, 2002 8(2009), 10 vom: 26. Okt. (DE-627)350258880 (DE-600)2082214-5 1475-4924 nnns volume:8 year:2009 number:10 day:26 month:10 https://dx.doi.org/10.1186/jbiol184 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2153 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 8 2009 10 26 10
allfieldsGer	10.1186/jbiol184 doi (DE-627)SPR030038928 (SPR)jbiol184-e DE-627 ger DE-627 rakwb eng Matyskiela, Mary E verfasserin aut Mechanisms of ubiquitin transfer by the anaphase-promoting complex 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © BioMed Central Ltd 2009 Abstract The anaphase-promoting complex (APC) is a ubiquitin-protein ligase required for the completion of mitosis in all eukaryotes. Recent mechanistic studies reveal how this remarkable enzyme combines specificity in substrate binding with flexibility in ubiquitin transfer, thereby allowing the modification of multiple lysines on the substrate as well as specific lysines on ubiquitin itself. Substrate Binding (dpeaa)DE-He213 Substrate Recognition (dpeaa)DE-He213 Ring Domain (dpeaa)DE-He213 Polyubiquitin Chain (dpeaa)DE-He213 Ubiquitin Chain (dpeaa)DE-He213 Rodrigo-Brenni, Monica C aut Morgan, David O aut Enthalten in Journal of biology London : BioMed Central, 2002 8(2009), 10 vom: 26. Okt. (DE-627)350258880 (DE-600)2082214-5 1475-4924 nnns volume:8 year:2009 number:10 day:26 month:10 https://dx.doi.org/10.1186/jbiol184 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2153 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 8 2009 10 26 10
allfieldsSound	10.1186/jbiol184 doi (DE-627)SPR030038928 (SPR)jbiol184-e DE-627 ger DE-627 rakwb eng Matyskiela, Mary E verfasserin aut Mechanisms of ubiquitin transfer by the anaphase-promoting complex 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © BioMed Central Ltd 2009 Abstract The anaphase-promoting complex (APC) is a ubiquitin-protein ligase required for the completion of mitosis in all eukaryotes. Recent mechanistic studies reveal how this remarkable enzyme combines specificity in substrate binding with flexibility in ubiquitin transfer, thereby allowing the modification of multiple lysines on the substrate as well as specific lysines on ubiquitin itself. Substrate Binding (dpeaa)DE-He213 Substrate Recognition (dpeaa)DE-He213 Ring Domain (dpeaa)DE-He213 Polyubiquitin Chain (dpeaa)DE-He213 Ubiquitin Chain (dpeaa)DE-He213 Rodrigo-Brenni, Monica C aut Morgan, David O aut Enthalten in Journal of biology London : BioMed Central, 2002 8(2009), 10 vom: 26. Okt. (DE-627)350258880 (DE-600)2082214-5 1475-4924 nnns volume:8 year:2009 number:10 day:26 month:10 https://dx.doi.org/10.1186/jbiol184 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2153 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 8 2009 10 26 10
language	English
source	Enthalten in Journal of biology 8(2009), 10 vom: 26. Okt. volume:8 year:2009 number:10 day:26 month:10
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topic_facet	Substrate Binding Substrate Recognition Ring Domain Polyubiquitin Chain Ubiquitin Chain
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author	Matyskiela, Mary E
spellingShingle	Matyskiela, Mary E misc Substrate Binding misc Substrate Recognition misc Ring Domain misc Polyubiquitin Chain misc Ubiquitin Chain Mechanisms of ubiquitin transfer by the anaphase-promoting complex
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topic_title	Mechanisms of ubiquitin transfer by the anaphase-promoting complex Substrate Binding (dpeaa)DE-He213 Substrate Recognition (dpeaa)DE-He213 Ring Domain (dpeaa)DE-He213 Polyubiquitin Chain (dpeaa)DE-He213 Ubiquitin Chain (dpeaa)DE-He213
topic	misc Substrate Binding misc Substrate Recognition misc Ring Domain misc Polyubiquitin Chain misc Ubiquitin Chain
topic_unstemmed	misc Substrate Binding misc Substrate Recognition misc Ring Domain misc Polyubiquitin Chain misc Ubiquitin Chain
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title	Mechanisms of ubiquitin transfer by the anaphase-promoting complex
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title_full	Mechanisms of ubiquitin transfer by the anaphase-promoting complex
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author_browse	Matyskiela, Mary E Rodrigo-Brenni, Monica C Morgan, David O
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title_sort	mechanisms of ubiquitin transfer by the anaphase-promoting complex
title_auth	Mechanisms of ubiquitin transfer by the anaphase-promoting complex
abstract	Abstract The anaphase-promoting complex (APC) is a ubiquitin-protein ligase required for the completion of mitosis in all eukaryotes. Recent mechanistic studies reveal how this remarkable enzyme combines specificity in substrate binding with flexibility in ubiquitin transfer, thereby allowing the modification of multiple lysines on the substrate as well as specific lysines on ubiquitin itself. © BioMed Central Ltd 2009
abstractGer	Abstract The anaphase-promoting complex (APC) is a ubiquitin-protein ligase required for the completion of mitosis in all eukaryotes. Recent mechanistic studies reveal how this remarkable enzyme combines specificity in substrate binding with flexibility in ubiquitin transfer, thereby allowing the modification of multiple lysines on the substrate as well as specific lysines on ubiquitin itself. © BioMed Central Ltd 2009
abstract_unstemmed	Abstract The anaphase-promoting complex (APC) is a ubiquitin-protein ligase required for the completion of mitosis in all eukaryotes. Recent mechanistic studies reveal how this remarkable enzyme combines specificity in substrate binding with flexibility in ubiquitin transfer, thereby allowing the modification of multiple lysines on the substrate as well as specific lysines on ubiquitin itself. © BioMed Central Ltd 2009
collection_details	GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2153 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700
container_issue	10
title_short	Mechanisms of ubiquitin transfer by the anaphase-promoting complex
url	https://dx.doi.org/10.1186/jbiol184
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author2	Rodrigo-Brenni, Monica C Morgan, David O
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up_date	2024-07-03T13:30:09.271Z
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