Structural Plasticity and Noncovalent Substrate Binding in the GroEL Apical Domain. A study using electrospray ionization mass spectrometry and fluorescence binding studies [PDF]
, 2002 Advances in understanding how GroEL binds to non-native proteins are reported. Conformational flexibility in the GroEL apical domain, which could account for the variety of substrates that GroEL binds, is illustrated by comparison of several independent ...
Adams +62 more
core +1 more source
Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU [PDF]
, 2002 Hsc66 and Hsc20 comprise a specialized chaperone system important for the assembly of iron-sulfur clusters in Escherchia coli. Only a single substrate, the Fe/S template protein IscU, has been identified for the Hsc66/Hsc20 system, but the mechanism by ...
Hoff, Kevin G. +4 more
core +1 more source
Alterations of the mitochondrial proteome caused by the absence of mitochondrial DNA: A proteomic view [PDF]
, 2006 The proper functioning of mitochondria requires that both the mitochondrial and the nuclear genome are functional. To investigate the importance of the mitochondrial genome, which encodes only 13 subunits of the respiratory complexes, the mitochondrial ...
Abdul +39 more
core +4 more sources
Erythrocytes as Carriers of Therapeutic Enzymes. [PDF]
, 2020 Therapeutic enzymes are administered for the treatment of a wide variety of diseases. They exert their effects through binding with a high affinity and specificity to disease-causing substrates to catalyze their conversion to a non-noxious product, to ...
Bax, BE
core +1 more source
Antioxidants, 2019 The antioxidant enzyme, 3-mercaptopyruvate sulfurtransferase (MST, EC 2.8.1.2) is localized in the cytosol and mitochondria, while the evolutionarily-related enzyme, rhodanese (thiosulfate sulfurtransferase, TST, EC 2.8.1.1) is localized in the ...
Noriyuki Nagahara +3 more
doaj +1 more source
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL [PDF]
, 1996 The chaperonin GroEL is a large complex composed of 14 identical 57-kDa subunits that requires ATP and GroES for some of its activities. We find that a monomeric polypeptide corresponding to residues 191 to 345 has the activity of the tetradecamer both ...
Buckle, A.M. (Asley M.) +6 more
core +1 more source
Scientific opinion on the acute health risks related to the presence of cyanogenic glycosides in raw apricot kernels and products derived from raw apricot kernels [PDF]
, 2016 Peer reviewedPublisher ...
core +3 more sources
Molecules, 2023 Yohimbine is a small indole alkaloid derived from the bark of the yohimbe tree with documented biological activity, including anti-inflammatory, erectile dysfunction relieving, and fat-burning properties.
Małgorzata Iciek +5 more
doaj +1 more source
Enzymatic activity of the Arabidopsis sulfurtransferase resides in the C-terminal domain but is boosted by the N-terminal domain and the linker peptide in the full-length enzyme [PDF]
, 2005 Sulfurtransferases/rhodaneses are a group of enzymes widely distributed in plants, animals, and bacteria that catalyze the transfer of sulfur from a donor molecule to a thiophilic acceptor substrate.
Burow, M. +2 more
core +2 more sources
The rhodanese RhdA helps Azotobacter vinelandii in maintaining cellular redox balance [PDF]
, 2010 The tandem domain rhodanese-homology protein RhdA of Azotobacter vinelandii shows an active-site loop structure that confers structural peculiarity in the environment of its catalytic cysteine residue.
Anderson A.J. +5 more
core +2 more sources