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Ulrich Brandt (1961-)

Biochemiker

Name	Ulrich Brandt
Zeit	1961- (Lebensdaten)
Ort	Deutschland
Beruf	Biochemiker (charakteristischer Beruf) Hochschullehrer
Beziehung	Goethe-Universität Frankfurt am Main
Quelle	Gesellschaft für Biochemie und Molekularbiologie (GBM): http://www.sterne-und-weltraum.de/blatt/d_bs_pdf&_id=993768 (Stand: 19.3.2018)
Datensatztyp	Person
GND-Nummer	115471392X
Datensatz-ID	115471392X
Beteiligt an alle anzeigen Regulation of mitochondrial proteostasis by the proton gradient AIFM1 is a component of the mitochondrial disulfide relay that drives complex I assembly through efficient import of NDUFS5 Ablation of mitochondrial DNA results in widespread remodeling of the mitochondrial complexome A central functional role for the 49-kDa subunit within the catalytic core of mitochondrial complex I Cardiolipin stabilizes respiratory chain supercomplexes CEDAR, an online resource for the reporting and exploration of complexome profiling data CEDAR, an online resource for the reporting and exploration of complexome profiling data CEDAR, an online resource for the reporting and exploration of complexome profiling data Functional implications from an unexpected position of the 49-kDa subunit of NADH:ubiquinone oxidoreductase HDQ (1-hydroxy-2-dodecyl-4(1H)quinolone), a high affinity inhibitor for mitochondrial alternative NADH dehydrogenase: evidence for a ping-pong mechanism Histidine 129 in the 75-kDa subunit of mitochondrial complex I from Yarrowia lipolytica is not a ligand for [Fe4S4] cluster N5 but is required for catalytic activity Identification and characterization of a novel 9.2-kDa membrane sector-associated protein of vacuolar proton-ATPase from chromaffin granules Identification of the mitochondrial ND3 subunit as a structural component involved in the active/deactive enzyme transition of respiratory complex I K+-independent actions of diazoxide question the role of inner membrane KATP channels in mitochondrial cytoprotective signaling Significance of respirasomes for the assembly/stability of human respiratory chain complex I The mechanism of mitochondrial superoxide production by the cytochrome bc1 complex The Redox-Bohr group associated with iron-sulfur cluster N2 of complex I Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:ubiquinone oxidoreductase) Three molecules of ubiquinone bind specifically to mitochondrial cytochrome bc1 complex CEDAR, an online resource for the reporting and exploration of complexome profiling data Locking loop movement in the ubiquinone pocket of complex I disengages the proton pumps Locking loop movement in the ubiquinone pocket of complex I disengages the proton pumps Locking loop movement in the ubiquinone pocket of complex I disengages the proton pumps The membrane scaffold SLP2 anchors a proteolytic hub in mitochondria containing PARL and the i ‐AAA protease YME1L Exploring the ubiquinone binding cavity of respiratory complex I Superoxide radical formation by pure complex I (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica Determination of the structure of complex I of Yarrowia lipolytica by single particle analysis Functional significance of conserved histidines and arginines in the 49-kDa subunit of mitochondrial complex I Two aspartic acid residues in the PSST-homologous NUKM subunit of complex I from Yarrowia lipolytica are essential for catalytic activity Function of conserved acidic residues in the PSST homologue of complex I (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica

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Ulrich Brandt (1961-)

Regulation of mitochondrial proteostasis by the proton gradient

AIFM1 is a component of the mitochondrial disulfide relay that drives complex I assembly through efficient import of NDUFS5

Ablation of mitochondrial DNA results in widespread remodeling of the mitochondrial complexome

A central functional role for the 49-kDa subunit within the catalytic core of mitochondrial complex I

Cardiolipin stabilizes respiratory chain supercomplexes

CEDAR, an online resource for the reporting and exploration of complexome profiling data

CEDAR, an online resource for the reporting and exploration of complexome profiling data

CEDAR, an online resource for the reporting and exploration of complexome profiling data

Functional implications from an unexpected position of the 49-kDa subunit of NADH:ubiquinone oxidoreductase

HDQ (1-hydroxy-2-dodecyl-4(1H)quinolone), a high affinity inhibitor for mitochondrial alternative NADH dehydrogenase: evidence for a ping-pong mechanism

Histidine 129 in the 75-kDa subunit of mitochondrial complex I from Yarrowia lipolytica is not a ligand for [Fe4S4] cluster N5 but is required for catalytic activity

Identification and characterization of a novel 9.2-kDa membrane sector-associated protein of vacuolar proton-ATPase from chromaffin granules

Identification of the mitochondrial ND3 subunit as a structural component involved in the active/deactive enzyme transition of respiratory complex I

K+-independent actions of diazoxide question the role of inner membrane KATP channels in mitochondrial cytoprotective signaling

Significance of respirasomes for the assembly/stability of human respiratory chain complex I

The mechanism of mitochondrial superoxide production by the cytochrome bc1 complex

The Redox-Bohr group associated with iron-sulfur cluster N2 of complex I

Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:ubiquinone oxidoreductase)

Three molecules of ubiquinone bind specifically to mitochondrial cytochrome bc1 complex

CEDAR, an online resource for the reporting and exploration of complexome profiling data

Locking loop movement in the ubiquinone pocket of complex I disengages the proton pumps

Locking loop movement in the ubiquinone pocket of complex I disengages the proton pumps

Locking loop movement in the ubiquinone pocket of complex I disengages the proton pumps

The membrane scaffold SLP2 anchors a proteolytic hub in mitochondria containing PARL and the i ‐AAA protease YME1L

Exploring the ubiquinone binding cavity of respiratory complex I

Superoxide radical formation by pure complex I (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica

Determination of the structure of complex I of Yarrowia lipolytica by single particle analysis

Functional significance of conserved histidines and arginines in the 49-kDa subunit of mitochondrial complex I

Two aspartic acid residues in the PSST-homologous NUKM subunit of complex I from Yarrowia lipolytica are essential for catalytic activity

Function of conserved acidic residues in the PSST homologue of complex I (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica