The stability and formation of native proteins from unfolded monomers is increased through interactions with unrelated proteins - Wikidata - wikimedia - TriplyDB

The stability and formation of native proteins from unfolded monomers is increased through interactions with unrelated proteins

The stability and formation of native proteins from unfolded monomers is increased through interactions with unrelated proteins

http://www.wikidata.org/entity/Q28469215

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Hsp70- and Hsp90-mediated proteasomal degradation underlies TPI sugarkill pathogenesis in Drosophila.Macromolecular crowding directs extracellular matrix organization and mesenchymal stem cell behavior A novel hyaluronidase from brown spider (Loxosceles intermedia) venom (Dietrich's Hyaluronidase): from cloning to functional characterization.Substrate-Induced Dimerization of Engineered Monomeric Variants of Triosephosphate Isomerase from Trichomonas vaginalis.Protein-stabilizing and cell-penetrating properties of α-helix domain of 30Kc19 protein In vitro refolding of triosephosphate isomerase from L. donovani.

P2860

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P2860

The stability and formation of native proteins from unfolded monomers is increased through interactions with unrelated proteins

http://www.wikidata.org/entity/Q28469215

description

2007 nî lūn-bûn

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2007 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2007 թվականի հունիսին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

The stability and formation of ...... ctions with unrelated proteins

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The stability and formation of ...... ctions with unrelated proteins

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The stability and formation of ...... ctions with unrelated proteins

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The stability and formation of ...... ctions with unrelated proteins

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The stability and formation of ...... ctions with unrelated proteins

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The stability and formation of ...... ctions with unrelated proteins

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The stability and formation of ...... ctions with unrelated proteins

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Armando Gómez Puyou

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Claudia Rodríguez-Almazán

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Francisco J Torner

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Marieta Tuena de Gómez-Puyou

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P2860

Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell

How to measure and predict the molar absorption coefficient of a protein

The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media

Enzyme catalysis: not different, just better

Entropy effects on protein hinges: the reaction catalyzed by triosephosphate isomerase

The glycolytic enzymes, glyceraldehyde-3-phosphate dehydrogenase, triose-phosphate isomerase, and pyruvate kinase are components of the K(ATP) channel macromolecular complex and regulate its function

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

Folding and association of oligomeric and multimeric proteins.

Macromolecular crowding: obvious but underappreciated.

Enhanced association of mutant triosephosphate isomerase to red cell membranes and to brain microtubules

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e497

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scholarly article

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6

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2

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Ruy Pérez-Montfort

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2007-06-06T00:00:00Z

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6284297

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