Results 81 to 90 of about 1,607,008 (329)

The cytochrome oxidase defect in ISC‐depleted yeast is caused by impaired iron–sulfur cluster maturation of the mitoribosome assembly factor Rsm22

open access: yesFEBS Letters, EarlyView.
The yeast mitoribosome assembly factor Rsm22 contains a [4Fe‐4S] cluster that is matured by the mitochondrial iron–sulfur cluster assembly (ISC) machinery. Defects in ISC components result in impaired mitochondrial protein synthesis due to a mitoribosome assembly defect.
Ulrich Mühlenhoff   +4 more
wiley   +1 more source

Value of eight-amino-acid matches in predicting the allergenicity status of proteins: an empirical bioinformatic investigation

open access: yesClinical and Molecular Allergy, 2009
The use of biotechnological techniques to introduce novel proteins into food crops (transgenic or GM crops) has motivated investigation into the properties of proteins that favor their potential to elicit allergic reactions.
ThirumalaiswamySekhar Arvind   +2 more
doaj   +1 more source

Purification and Characterization of a 44-kDa Recombinant Collagen I α 1 Fragment from Corn Grain [PDF]

open access: yes, 2009
This paper demonstrates that a fibrous, repetitive amino acid sequence collagen-related protein, a 44-kDa fragment of human collagen I α 1 (CIα1), was expressed in corn grain molecularly equivalent to that produced in recombinant yeast.
Baez, Julio   +3 more
core   +3 more sources

Development of visible light‐sensitive human neuropsin (OPN5) via single amino acid substitution

open access: yesFEBS Letters, EarlyView.
The present study determines a key amino acid residue, Lys91, for defining UV sensitivity of human OPN5. Heterologous action spectroscopy of the wild type and K91 mutants of OPN5 in HEK293T cells reveals that substitution of Lys91 with neutral (alanine) or acidic amino acids (glutamic or aspartic acids) causes substantial shifts in spectral sensitivity
Yusuke Sakai   +2 more
wiley   +1 more source

Exploring hydrophilic sequence space to search for uncharted foldable proteins by AlphaFold2

open access: yesBiophysics and Physicobiology
Proteins typically fold into unique three-dimensional structures largely driven by interactions between hydrophobic amino acids. This understanding has helped improve our knowledge of protein folding.
Naoki Tomita   +3 more
doaj   +1 more source

The Jena Library of Biological Macromolecules - JenaLib [PDF]

open access: yes, 2009
The JenaLib database ("www.fli-leibniz.de/IMAGE.html":http://www.fli-leibniz.de/IMAGE.html) offers value-added information for all Protein Data Bank (PDB) and Nucleic Acid Database (NDB) entries.
Juergen Suehnel, Rolf Huehne
core   +2 more sources

Exploring lipid diversity and minimalism to define membrane requirements for synthetic cells

open access: yesFEBS Letters, EarlyView.
Designing the lipid membrane of synthetic cells is a complex task, in which its various roles (among them solute transport, membrane protein support, and self‐replication) should all be integrated. In this review, we report the latest top‐down and bottom‐up advances and discuss compatibility and complexity issues of current engineering approaches ...
Sergiy Gan   +2 more
wiley   +1 more source

ANCAC: amino acid, nucleotide, and codon analysis of COGs – a tool for sequence bias analysis in microbial orthologs

open access: yesBMC Bioinformatics, 2012
Background The COG database is the most popular collection of orthologous proteins from many different completely sequenced microbial genomes. Per definition, a cluster of orthologous groups (COG) within this database exclusively contains proteins that ...
Meiler Arno   +2 more
doaj   +1 more source

C‐mannosylation promotes ADAMTS1 activation and secretion in human testicular germ cell tumor NEC8 cells

open access: yesFEBS Letters, EarlyView.
C‐mannosylation is a unique form of protein glycosylation. In this study, we demonstrated that ADAMTS1 is C‐mannosylated at Trp562 and Trp565 in human testicular germ cell tumor NEC8 cells. We found that C‐mannosylation of ADAMTS1 is essential for its secretion, processing, enzymatic activity, and ability to promote vasculogenic mimicry. These findings
Takato Kobayashi   +5 more
wiley   +1 more source

The Amino Acid Sequence of Chromatium Ferredoxin

open access: yesJournal of Biological Chemistry, 1970
The amino acid sequence of Chromatium ferredoxin was determined by studies of thermolysin peptides of S-carboxymethylcysteinylferredoxin and chymotryptic peptides of oxidized ferredoxin. The 81 amino acid residues in the molecule have the following sequence: Ala-Leu-Met-Ile-Thr-Asp-Gln-Cys-Ile-Asn-Cys-Asn-Val-Cys-Gln-Pro-Glu-Cys-Pro-Asn-Gly-Ala-Ile-Ser-
Hiroshi Matsubara   +3 more
openaire   +3 more sources

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