Intrinsic Disorder in Ubiquitination Substrates (Q53087322)

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scientific article published on July 23, 2011

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Language	Label	Description	Also known as
English	Intrinsic Disorder in Ubiquitination Substrates	scientific article published on July 23, 2011

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scholarly article

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Europe PubMed Central

PubMed publication ID

21802429

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11 May 2018

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http://europepmc.org/abstract/MED/21802429

title

Intrinsic Disorder in Ubiquitination Substrates (English)

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Crossref

DOI

10.1016/J.JMB.2011.07.024

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https://api.crossref.org/works/10.1016/J.JMB.2011.07.024

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8 December 2024

main subject

protein ubiquitination

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based on heuristic

inferred from title

protein folding

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Europe PubMed Central

PubMed publication ID

21802429

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21802429

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8 December 2024

author name string

Tzachi Hagai

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1

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Europe PubMed Central

PubMed publication ID

21802429

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11 May 2018

reference URL

http://europepmc.org/abstract/MED/21802429

Ariel Azia

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2

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Europe PubMed Central

PubMed publication ID

21802429

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11 May 2018

reference URL

http://europepmc.org/abstract/MED/21802429

Ágnes Tóth-Petróczy

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3

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Europe PubMed Central

PubMed publication ID

21802429

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11 May 2018

reference URL

http://europepmc.org/abstract/MED/21802429

Yaakov Levy

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4

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Europe PubMed Central

PubMed publication ID

21802429

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11 May 2018

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http://europepmc.org/abstract/MED/21802429

language of work or name

English

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publication date

23 July 2011

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Europe PubMed Central

PubMed publication ID

21802429

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11 May 2018

reference URL

http://europepmc.org/abstract/MED/21802429

full work available at URL

https://api.elsevier.com/content/article/PII:S0022283611007789?httpAccept=text/xml

1 reference

stated in

Crossref

DOI

10.1016/J.JMB.2011.07.024

reference URL

https://api.crossref.org/works/10.1016/J.JMB.2011.07.024

retrieved

8 December 2024

https://api.elsevier.com/content/article/PII:S0022283611007789?httpAccept=text/plain

1 reference

stated in

Crossref

DOI

10.1016/J.JMB.2011.07.024

reference URL

https://api.crossref.org/works/10.1016/J.JMB.2011.07.024

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8 December 2024

published in

Journal of Molecular Biology

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Europe PubMed Central

PubMed publication ID

21802429

retrieved

11 May 2018

reference URL

http://europepmc.org/abstract/MED/21802429

volume

412

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Europe PubMed Central

PubMed publication ID

21802429

retrieved

11 May 2018

reference URL

http://europepmc.org/abstract/MED/21802429

issue

3

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Europe PubMed Central

PubMed publication ID

21802429

retrieved

11 May 2018

reference URL

http://europepmc.org/abstract/MED/21802429

page(s)

319-324

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Europe PubMed Central

PubMed publication ID

21802429

retrieved

11 May 2018

reference URL

http://europepmc.org/abstract/MED/21802429

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Lysine acetylation targets protein complexes and co-regulates major cellular functions

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Targeting proteins for degradation

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ATP-dependent steps in the binding of ubiquitin conjugates to the 26S proteasome that commit to degradation

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Degradation of some polyubiquitinated proteins requires an intrinsic proteasomal binding element in the substrates

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Defining the geometry of the two-component proteasome degron

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Endoproteolytic activity of the proteasome

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Proteasome-mediated protein processing by bidirectional degradation initiated from an internal site

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Rad23 escapes degradation because it lacks a proteasome initiation region

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The spatial and temporal organization of ubiquitin networks

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IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content

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PONDR-FIT: a meta-predictor of intrinsically disordered amino acids

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The importance of intrinsic disorder for protein phosphorylation

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Intrinsically unstructured proteins and their functions

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Intrinsically unstructured proteins

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Intrinsic disorder and functional proteomics

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Intrinsically disordered proteins: regulation and disease

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Identification, analysis, and prediction of protein ubiquitination sites

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Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life

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Flavors of protein disorder

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Tight regulation of unstructured proteins: from transcript synthesis to protein degradation

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Dependence of Proteasome Processing Rate on Substrate Unfolding

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A conserved unfoldase activity for the p97 AAA-ATPase in proteasomal degradation

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Structural basis for control by phosphorylation

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The age of crosstalk: phosphorylation, ubiquitination, and beyond

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Biological regulation via ankyrin repeat folding

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The folding and evolution of multidomain proteins

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Effects of excluded volume upon protein stability in covalently cross-linked proteins with variable linker lengths

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The N-end rule

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8 December 2024

Ubiquitin not only serves as a tag but also assists degradation by inducing protein unfolding

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8 December 2024

Autoregulation of an E2 enzyme by ubiquitin-chain assembly on its catalytic residue

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8 December 2024

Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination

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The nanny model for IDPs.

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8 December 2024

Identifiers

DOI

10.1016/J.JMB.2011.07.024

1 reference

stated in

Europe PubMed Central

PubMed publication ID

21802429

retrieved

11 May 2018

reference URL

http://europepmc.org/abstract/MED/21802429

PubMed publication ID

21802429

1 reference

stated in

Europe PubMed Central

PubMed publication ID

21802429

retrieved

11 May 2018

reference URL

http://europepmc.org/abstract/MED/21802429

ResearchGate publication ID

51533723

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