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Browsing by Subject "complex formation"

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Dominance analysis of competing protein assembly pathways

Lankeit, Johannes; Förste, Stefanie; Rudorf, Sophia (San Francisco, California, US : PLOS, 2023)

Most proteins form complexes consisting of two or more subunits, where complex assembly can proceed via two competing pathways: co-translational assembly of a mature and a nascent subunit, and post-translational assembly ...
High yield synthesis and structures of some achiral and chiral (diphosphine)tetracarbonylchromium(0) chelate complexes with tetracarbonyl(norbornadiene)chromium(0) as complexation reagent

Strotmann, Markus; Wartchow, Rudolf; Butenschön, Holger (Gainesville : Arkat USA, 2004)

Tetracarbonyl(norbornadiene)chromium(0) was used as complexation reagent in the synthesis of tetracarbonylchromium chelate complexes of dppe, dppb, dppf, DIOP, BINAP, and Tol-BINAP. In all cases the reactions took place ...
The higher level of organization of the oxidative phosphorylation system: Mitochondrial supercomplexes

Dudkina, Natalya V.; Sunderhaus, Stephanie; Boekema, Egbert J.; Braun, Hans-Peter (Dordrecht [u.a.] : Springer Science + Business Media B.V, 2008)

The organization of the oxidative phosphorylation (OXPHOS) system within the inner mitochondrial membrane appears to be far more complicated than previously thought. In particular, the individual protein complexes of the ...
Inositol pyrophosphates promote the interaction of SPX domains with the coiled-coil motif of PHR transcription factors to regulate plant phosphate homeostasis

Ried, Martina K.; Wild, Rebekka; Zhu, Jinsheng; Pipercevic, Joka; Sturm, Kristina; Broger, Larissa; Harmel, Robert K.; Abriata, Luciano A.; Hothorn, Ludwig A.; Fiedler, Dorothea; Hiller, Sebastian; Hothorn, Michael (London : Nature Publishing Group, 2021)

Phosphorus is an essential nutrient taken up by organisms in the form of inorganic phosphate (Pi). Eukaryotes have evolved sophisticated Pi sensing and signaling cascades, enabling them to stably maintain cellular Pi ...
L-galactono-1,4-lactone dehydrogenase (GLDH) forms part of three subcomplexes of mitochondrial complex I in Arabidopsis thaliana

Schertl, Peter; Sunderhaus, Stephanie; Klodmann, Jennifer; Gergoff Grozeff, Gustavo E.; Bartoli, Carlos G.; Braun, Hans-Peter (Bethesda, Md. : ASBMB Publications, 2012)

L-Galactono-1,4-lactone dehydrogenase (GLDH) catalyzes the terminal step of the Smirnoff-Wheeler pathway for vitamin C (L-ascorbate) biosynthesis in plants. A GLDH in gel activity assay was developed to biochemically ...
The native structure and composition of the cruciferin complex in brassica napus

Nietzel, Thomas; Dudkina, Natalya V.; Haase, Christin; Denolf, Peter; Semchonok, Dmitry A.; Boekema, Egbert J.; Braun, Hans-Peter; Sunderhaus, Stephanie (Bethesda, Md. : ASBMB Publications, 2013)

Globulins are an important group of seed storage proteins in dicotyledonous plants. They are synthesized during seed development, assembled into very compact protein complexes, and finally stored in protein storage vacuoles ...
New insights into the co-evolution of cytochrome c reductase and the mitochondrial processing peptidase

Brumme, Stefanie; Kruft, Volker; Schmitz, Udo K.; Braun, Hans-Peter (Bethesda, Md. : ASBMB Publications, 1998)

The mitochondrial processing peptidase (MPP) is a heterodimeric enzyme that forms part of the cytochrome c reductase complex from higher plants. Mitochondria from mammals and yeast contain two homologous enzymes: (i) an ...
Specificity and regulation of phosphotyrosine signaling through SH2 domains

Marasco, Michelangelo; Carlomagno, Teresa (Amsterdam : Elsevier, 2020)

Phosphotyrosine (pY) signaling is instrumental to numerous cellular processes. pY recognition occurs through specialized protein modules, among which the Src-homology 2 (SH2) domain is the most common. SH2 domains are small ...
Structural Basis for Regulation of the Opposing (p)ppGpp Synthetase and Hydrolase within the Stringent Response Orchestrator Rel

Pausch, Patrick; Abdelshahid, Maha; Steinchen, Wieland; Schäfer, Heinrich; Gratani, Fabio Lino; Freibert, Sven-Andreas.; Wolz, Christiane; Turgay, Kürşad; Wilson, Daniel N.; Bange, Gert (New York, NY : Elsevier, 2020)

The stringent response enables metabolic adaptation of bacteria under stress conditions and is governed by RelA/SpoT Homolog (RSH)-type enzymes. Long RSH-type enzymes encompass an N-terminal domain (NTD) harboring the ...
A structural model of the cytochrome c reductase/oxidase supercomplex from yeast mitochondria

Heinemeyer, Jesco; Braun, Hans-Peter; Boekema, Egbert J.; Kouřil, Roman (Bethesda, Md. : ASBMB Publications, 2007)

Mitochondrial respiratory chain complexes are arranged in supercomplexes within the inner membrane. Interaction of cytochrome c reductase (complex III) and cytochrome c oxidase (complex IV) was investigated in Saccharomyces ...
Supramolecular structure of the mitochondrial oxidative phosphorylation system

Boekema, Egbert J.; Braun, Hans-Peter (Bethesda, Md. : ASBMB Publications, 2007)

The protein complexes of the mitochondrial oxidative phosphorylation system were recently reported to form supramolecular assemblies termed respiratory supercomplexes or respirasomes. These supercomplexes are considered ...

Now showing items 1-11 of 11

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