The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation

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Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 2041-1723

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation ; volume:9 ; number:1 ; day:20 ; month:8 ; year:2018 ; pages:1-14 ; date:12.2018
Nature Communications ; 9, Heft 1 (20.8.2018), 1-14, 12.2018

Classification: Biowissenschaften, Biologie

Creator: Aichem, Annette

Contributor: Anders, Samira
Catone, Nicola
Rößler, Philip
Stotz, Sophie
Berg, Andrej
Schwab, Ricarda
Scheuermann, Sophia
Bialas, Johanna
Schütz-Stoffregen, Mira C.
Schmidtke, Gunter
Peter, Christine
Groettrup, Marcus
Wiesner, Silke
SpringerLink (Online service)

DOI: 10.1038/s41467-018-05776-3

URN: urn:nbn:de:101:1-2018102520312994570954

Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 15.08.2025, 7:25 AM CEST

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Associated

Aichem, Annette
Anders, Samira
Catone, Nicola
Rößler, Philip
Stotz, Sophie
Berg, Andrej
Schwab, Ricarda
Scheuermann, Sophia
Bialas, Johanna
Schütz-Stoffregen, Mira C.
Schmidtke, Gunter
Peter, Christine
Groettrup, Marcus
Wiesner, Silke
SpringerLink (Online service)

Other Objects (12)

The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation

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The ubiquitin-like modifier FAT10 : much more than a proteasome-targeting signal

Regulation of Interferon Induction by the Ubiquitin-Like Modifier FAT10

The ubiquitin-like modifier FAT10 in antigen processing and antimicrobial defense

The ubiquitin-like modifier FAT10 inhibits retinal PDE6 activity and mediates its proteasomal degradation

FAT10, a ubiquitin-independent signal for proteasomal degradation

The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition

FAT10ylation as a signal for proteasomal degradation

Evidence for an involvement of the ubiquitin-like modifier ISG15 in MHC class I antigen presentation

Evidence for an involvement of the ubiquitin‐like modifier ISG15 in MHC class I antigen presentation

The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation

Conjugation of the Ubiquitin Activating Enzyme UBE1 with the Ubiquitin-Like Modifier FAT10 Targets It for Proteasomal Degradation

The ubiquitin-like modifier FAT10 in cancer development

The ubiquitin-like modifier FAT10 : much more than a proteasome-targeting signal

Regulation of Interferon Induction by the Ubiquitin-Like Modifier FAT10

The ubiquitin-like modifier FAT10 in antigen processing and antimicrobial defense

The ubiquitin-like modifier FAT10 inhibits retinal PDE6 activity and mediates its proteasomal degradation

FAT10, a ubiquitin-independent signal for proteasomal degradation

The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition

FAT10ylation as a signal for proteasomal degradation

Evidence for an involvement of the ubiquitin-like modifier ISG15 in MHC class I antigen presentation

Evidence for an involvement of the ubiquitin‐like modifier ISG15 in MHC class I antigen presentation

The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation

Conjugation of the Ubiquitin Activating Enzyme UBE1 with the Ubiquitin-Like Modifier FAT10 Targets It for Proteasomal Degradation

The ubiquitin-like modifier FAT10 in cancer development

The ubiquitin-like modifier FAT10 : much more than a proteasome-targeting signal

Regulation of Interferon Induction by the Ubiquitin-Like Modifier FAT10

The ubiquitin-like modifier FAT10 in antigen processing and antimicrobial defense

The ubiquitin-like modifier FAT10 inhibits retinal PDE6 activity and mediates its proteasomal degradation

FAT10, a ubiquitin-independent signal for proteasomal degradation

The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition

FAT10ylation as a signal for proteasomal degradation

Evidence for an involvement of the ubiquitin-like modifier ISG15 in MHC class I antigen presentation

Evidence for an involvement of the ubiquitin‐like modifier ISG15 in MHC class I antigen presentation

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The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation

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Other Objects (12)

The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation

Conjugation of the Ubiquitin Activating Enzyme UBE1 with the Ubiquitin-Like Modifier FAT10 Targets It for Proteasomal Degradation

The ubiquitin-like modifier FAT10 in cancer development

The ubiquitin-like modifier FAT10 : much more than a proteasome-targeting signal

Regulation of Interferon Induction by the Ubiquitin-Like Modifier FAT10

The ubiquitin-like modifier FAT10 in antigen processing and antimicrobial defense

The ubiquitin-like modifier FAT10 inhibits retinal PDE6 activity and mediates its proteasomal degradation

FAT10, a ubiquitin-independent signal for proteasomal degradation

The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition

FAT10ylation as a signal for proteasomal degradation

Evidence for an involvement of the ubiquitin-like modifier ISG15 in MHC class I antigen presentation

Evidence for an involvement of the ubiquitin‐like modifier ISG15 in MHC class I antigen presentation

The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation

Conjugation of the Ubiquitin Activating Enzyme UBE1 with the Ubiquitin-Like Modifier FAT10 Targets It for Proteasomal Degradation

The ubiquitin-like modifier FAT10 in cancer development

The ubiquitin-like modifier FAT10 : much more than a proteasome-targeting signal

Regulation of Interferon Induction by the Ubiquitin-Like Modifier FAT10

The ubiquitin-like modifier FAT10 in antigen processing and antimicrobial defense

The ubiquitin-like modifier FAT10 inhibits retinal PDE6 activity and mediates its proteasomal degradation

FAT10, a ubiquitin-independent signal for proteasomal degradation

The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition

FAT10ylation as a signal for proteasomal degradation

Evidence for an involvement of the ubiquitin-like modifier ISG15 in MHC class I antigen presentation

Evidence for an involvement of the ubiquitin‐like modifier ISG15 in MHC class I antigen presentation

The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation

Conjugation of the Ubiquitin Activating Enzyme UBE1 with the Ubiquitin-Like Modifier FAT10 Targets It for Proteasomal Degradation

The ubiquitin-like modifier FAT10 in cancer development

The ubiquitin-like modifier FAT10 : much more than a proteasome-targeting signal

Regulation of Interferon Induction by the Ubiquitin-Like Modifier FAT10

The ubiquitin-like modifier FAT10 in antigen processing and antimicrobial defense

The ubiquitin-like modifier FAT10 inhibits retinal PDE6 activity and mediates its proteasomal degradation

FAT10, a ubiquitin-independent signal for proteasomal degradation

The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition

FAT10ylation as a signal for proteasomal degradation

Evidence for an involvement of the ubiquitin-like modifier ISG15 in MHC class I antigen presentation

Evidence for an involvement of the ubiquitin‐like modifier ISG15 in MHC class I antigen presentation

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