Hochschulschrift
Role of the AAA protease Yme1 in folding of proteins in the mitochondrial intermembrane space
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
München, Ludwig-Maximilians-Universität, Diss., 2013
- Schlagwort
-
Mitochondrium
Membrantransport
Biomembran
Proteine
Molekülstruktur
Strukturbiologie
- Ereignis
-
Veröffentlichung
- (wo)
-
München
- (wer)
-
Universitätsbibliothek der Ludwig-Maximilians-Universität
- (wann)
-
2013
- Urheber
-
Schreiner, Bernadette
- Beteiligte Personen und Organisationen
- URN
-
urn:nbn:de:bvb:19-152997
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
14.08.2025, 10:47 MESZ
Datenpartner
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Objekttyp
- Hochschulschrift
Beteiligte
- Schreiner, Bernadette
- Soll, Jürgen
- Universitätsbibliothek der Ludwig-Maximilians-Universität
Entstanden
- 2013
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Proteolytic regulation of mitochondrial phospholipid metabolism by the i-AAA protease Yme1
Role of the mitochondrial m-AAA protease in quality control and calcium homeostasis
A multiomic approach to identify new substrates of the mitochondrial m-AAA protease
A protective function against apoptosis revealed by the neuronal interactome of the mitochondrial m-AAA protease
Polymerase delta-interacting protein 38 (PDIP38) modulates the stability and activity of the mitochondrial AAA+ protease CLPXP
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Mouse brain expression patterns of Spg7, Afg3l1, and Afg3l2 transcripts, encoding for the mitochondrial m-AAA protease
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Functional characterization of the mammalian iAAA protease subunit, YME1L
Role of the AAA protease Yme1 in folding of proteins in the mitochondrial intermembrane space
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Proteolytic regulation of mitochondrial phospholipid metabolism by the i-AAA protease Yme1
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A multiomic approach to identify new substrates of the mitochondrial m-AAA protease
A protective function against apoptosis revealed by the neuronal interactome of the mitochondrial m-AAA protease
Polymerase delta-interacting protein 38 (PDIP38) modulates the stability and activity of the mitochondrial AAA+ protease CLPXP
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