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

Extent: Online-Ressource

Language: Englisch

Bibliographic citation: In: Nature Communications ; 9 (2018). - 3321. - eISSN 2041-1723

Classification: Biowissenschaften, Biologie

Event: Veröffentlichung

(where): Konstanz

(who): Bibliothek der Universität Konstanz

(when): 2018

Creator: Aichem, Annette
Catone, Nicola
Berg, Andrej
Schwab, Ricarda
Scheuermann, Sophia
Bialas, Johanna
Schmidtke, Gunter
Peter, Christine
Groettrup, Marcus
Wiesner, Silke

URN: urn:nbn:de:bsz:352-2-1osbbqsz3ua1

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 15.08.2025, 7:22 AM CEST

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Associated

Aichem, Annette
Catone, Nicola
Berg, Andrej
Schwab, Ricarda
Scheuermann, Sophia
Bialas, Johanna
Schmidtke, Gunter
Peter, Christine
Groettrup, Marcus
Wiesner, Silke
Bibliothek der Universität Konstanz

Time of origin

2018

Other Objects (12)

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

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

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

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

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

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

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

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

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)

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

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

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

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

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

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

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

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

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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