Results 91 to 100 of about 26,854 (254)

In Vivo Biosynthesis and Direct Incorporation of Noncanonical Amino Acids into Proteins

open access: yesChemBioChem, Volume 26, Issue 22, November 17, 2025.
This review evaluates engineered (semi)autonomous cell systems for the biosynthesis and incorporation of noncanonical amino acids (ncAAs) into proteins. While semi‐autonomous cells convert supplied precursors into ncAAs autonomous cells integrate biosynthetic pathways that produce these building blocks intracellularly.
Jan Hendrik Illies   +2 more
wiley   +1 more source

Thermophilic phosphoribosyltransferases Thermus thermophilus HB27 in nucleotide synthesis

open access: yesBeilstein Journal of Organic Chemistry, 2018
Phosphoribosyltransferases are the tools that allow the synthesis of nucleotide analogues using multi-enzymatic cascades. The recombinant adenine phosphoribosyltransferase (TthAPRT) and hypoxanthine phosphoribosyltransferase (TthHPRT) from Thermus ...
Ilja V. Fateev   +9 more
doaj   +1 more source

Properties and crystal structure of methylenetetrahydrofolate reductase from Thermus thermophilus HB8. [PDF]

open access: yesPLoS ONE, 2011
Methylenetetrahydrofolate reductase (MTHFR) is one of the enzymes involved in homocysteine metabolism. Despite considerable genetic and clinical attention, the reaction mechanism and regulation of this enzyme are not fully understood because of difficult
Sayaka Igari   +7 more
doaj   +1 more source

Multiple prebiotic metals mediate translation. [PDF]

open access: yes, 2018
Today, Mg2+ is an essential cofactor with diverse structural and functional roles in life's oldest macromolecular machine, the translation system. We tested whether ancient Earth conditions (low O2, high Fe2+, and high Mn2+) can revert the ribosome to a ...
Bowman, Jessica C   +8 more
core   +1 more source

Improving the Fidelity of Thermus Thermophilus DNA Ligase [PDF]

open access: yesNucleic Acids Research, 1996
The DNA ligase from Thermus thermophilus (Tth DNA ligase) seals single-strand breaks (nicks) in DNA duplex substrates. The specificity and thermostability of this enzyme are exploited in the ligase chain reaction (LCR) and ligase detection reaction (LDR) to distinguish single base mutations associated with genetic diseases.
J, Luo, D E, Bergstrom, F, Barany
openaire   +3 more sources

Biological surveys reveal unexpectedly high faunal diversity at Nankai Trough methane seeps

open access: yesEcosphere, Volume 16, Issue 11, November 2025.
Abstract Cold seeps are chemosynthesis‐based ecosystems powered by microbial primary production that support diverse and specialized faunal assemblages in the deep sea. Despite Nankai Trough in Japan being a geologically active margin hosting numerous seeps, much of the faunal diversity remains undocumented.
Chong Chen   +6 more
wiley   +1 more source

Diversity and biosynthesis of compatible solutes in hyper/thermophiles [PDF]

open access: yes, 2010
The accumulation of compatible solutes, either by uptake from the medium or by de novo synthesis, is a general response of microorganisms to osmotic stress. The diversity of compatible solutes is large but falls into a few major chemical categories, such
Milton S. da Costa, Nuno Empadinhas
core   +2 more sources

Origin of a folded repeat protein from an intrinsically disordered ancestor. [PDF]

open access: yes, 2016
Repetitive proteins are thought to have arisen through the amplification of subdomain-sized peptides. Many of these originated in a non-repetitive context as cofactors of RNA-based replication and catalysis, and required the RNA to assume their active ...
Abe   +119 more
core   +3 more sources

Functional and structural characterization of F1‐ATPase with common ancestral core domains in stator ring

open access: yesProtein Science, Volume 34, Issue 11, November 2025.
Abstract Extant F1‐ATPases exhibit diverse rotational stepping behaviors—3‐, 6‐, or 9‐step cycles—yet the evolutionary origin of these patterns remains unclear. Here, we used ancestral sequence reconstruction to infer the catalytic β and non‐catalytic α subunits of a putative ancestral F1‐ATPase.
Aya K. Suzuki   +7 more
wiley   +1 more source

Expression and Purification of the Thermus thermophilus Argonaute Protein

open access: yesBio-Protocol, 2014
The Argonaute protein of Thermus thermophilus (TtAgo) has recently been studied in detail. For its in vitro characterization, TtAgo was purified after heterologous expression in Escherichia coli (E. coli).
Daan Swarts, Matthijs Jore, John Oost
doaj   +1 more source

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