Results 151 to 160 of about 554,293 (337)

[Cockayne syndrome: peculiarities of clinical manifestations and algorithm of observation in childhood]. [PDF]

open access: yesProbl Endokrinol (Mosk)
Kungurtseva AL   +6 more
europepmc   +1 more source

Selective targeting of cortactin tandem repeat acetylation by human lysine deacetylases

open access: yesThe FEBS Journal, EarlyView.
Cortactin function is regulated by acetylation at several lysine residues within its tandem repeat region. Using genetic code expansion to generate cortactin variants containing precisely defined acetylation marks, we show that HDAC6 is the primary enzyme removing these modifications, with SIRT1 and SIRT2 also acting at selected sites but with lower ...
Jan Komarek   +12 more
wiley   +1 more source

[Non-classic lipoid adrenal hyperplasia: clinical cases report]. [PDF]

open access: yesProbl Endokrinol (Mosk)
Sichinava IG   +5 more
europepmc   +1 more source

Polyesterase activity and thermostability of carboxylesterases from Thermoleophilum album YS‐3

open access: yesThe FEBS Journal, EarlyView.
Three novel α/β‐hydrolases from thermophilic bacterium Thermoleophilum album display carboxylesterase and polyesterase activity. These enzymes hydrolyse PET, PLA and PCL both at high and moderate temperatures. TA21 shows superior activity, efficiently converting MHET to terephthalic acid. Structural features underlying substrate binding highlight their
Tatyana N. Chernikova   +6 more
wiley   +1 more source

[Hypogonadotropic hypogonadism due to pathogenic variants in the POLR3B gene]. [PDF]

open access: yesProbl Endokrinol (Mosk)
Malievskiy OA   +2 more
europepmc   +1 more source

Investigating transthyretin variants H88R and I107V in amyloid priming: From destabilization to complete dissociation

open access: yesThe FEBS Journal, EarlyView.
Investigated mutations in transthyretin (TTR) disrupt the F87‐centered hydrophobic core that stabilizes its tetrameric structure. The mild I107V mutation weakens inter‐chain packing, while H88R fully abolishes tetramer formation, yielding a monomeric, aggregation‐prone form. Structural, biophysical, and computational analyses reveal that both mutations
István L. Bódy   +7 more
wiley   +1 more source

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