UQCRFS1N assembles mitochondrial respiratory complex-III into an asymmetric 21-subunit dimer

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Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 1674-8018

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: UQCRFS1N assembles mitochondrial respiratory complex-III into an asymmetric 21-subunit dimer ; day:6 ; month:3 ; year:2018 ; pages:1-6
Protein & cell ; (6.3.2018), 1-6

Classification: Biowissenschaften, Biologie

Creator: Zong, Shuai

Contributor: Gu, Jinke
Liu, Tianya
Guo, Runyu
Wu, Meng
Yang, Maojun
SpringerLink (Online service)

DOI: 10.1007/s13238-018-0515-x

URN: urn:nbn:de:1111-201805122000

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 14.08.2025, 10:59 AM CEST

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Zong, Shuai
Gu, Jinke
Liu, Tianya
Guo, Runyu
Wu, Meng
Yang, Maojun
SpringerLink (Online service)

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

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The key residue for substrate transport (Glu14) in the EmrE dimer is asymmetric

Most mitochondrial dGTP is tightly bound to respiratory complex I through the NDUFA10 subunit

Asymmetric dynamic coupling promotes alternative evolutionary pathways in an enzyme dimer

Graffiti | Streetart

Dimer

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

Personenakten

Dimer, Philipp

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Dimer, Wilhelm

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Dimer, Philipp

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Dimer, Willy

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Dimer, Josef

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Dimer, Willi

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The key residue for substrate transport (Glu14) in the EmrE dimer is asymmetric

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UQCRFS1N assembles mitochondrial respiratory complex-III into an asymmetric 21-subunit dimer

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Other Objects (12)

Most mitochondrial dGTP is tightly bound to respiratory complex I through the NDUFA10 subunit

Asymmetric dynamic coupling promotes alternative evolutionary pathways in an enzyme dimer

Dimer

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

Dimer, Philipp

Dimer, Wilhelm

Dimer, Philipp

Dimer, Willy

Dimer, Josef

Dimer, Willi

Dimer, Josef

The key residue for substrate transport (Glu14) in the EmrE dimer is asymmetric

Most mitochondrial dGTP is tightly bound to respiratory complex I through the NDUFA10 subunit

Asymmetric dynamic coupling promotes alternative evolutionary pathways in an enzyme dimer

Dimer

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

Dimer, Philipp

Dimer, Wilhelm

Dimer, Philipp

Dimer, Willy

Dimer, Josef

Dimer, Willi

Dimer, Josef

The key residue for substrate transport (Glu14) in the EmrE dimer is asymmetric

Most mitochondrial dGTP is tightly bound to respiratory complex I through the NDUFA10 subunit

Asymmetric dynamic coupling promotes alternative evolutionary pathways in an enzyme dimer

Dimer

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

Dimer, Philipp

Dimer, Wilhelm

Dimer, Philipp

Dimer, Willy

Dimer, Josef

Dimer, Willi

Dimer, Josef

The key residue for substrate transport (Glu14) in the EmrE dimer is asymmetric

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