Results 111 to 120 of about 365,538 (313)

The structure of a resuscitation-promoting factor domain from Mycobacterium tuberculosis shows homology to lysozymes

open access: yes, 2005
Resuscitation-promoting factor (RPF) proteins reactivate stationary-phase cultures of (G+C)-rich Gram-positive bacteria including the causative agent of tuberculosis, Mycobacterium tuberculosis.
Nicholas H Keep   +19 more
core   +1 more source

Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates

open access: yesFEBS Letters, EarlyView.
Inositol pyrophosphates are energy‐rich signaling molecules that perform critical functions in cells. Three different families of phosphatases hydrolyze the β phosphate of the inositol pyrophosphate molecules: two have narrow specificities and one is promiscuous.
Ronda J. Rolfes
wiley   +1 more source

Activities and properties of calcineurin catalytic domain

open access: yesChinese Science Bulletin, 2000
Calcineurin (CN) is the only protein phosphatase known to be under the control of calcium (Ca2+) and calmodulin (CaM). The enzyme consists of two subunits, the catalytic A subunit of 61 ku (CNA) and a regulatory B subunit of 19 ku (CNB). In this study, we used PCR amplication to construct a truncation consisting of only the CNA catalytic domain.
Shujie Yang, Li Zhang, Qun Wei
openaire   +1 more source

Reconstructing enzyme evolution by protein engineering

open access: yesFEBS Letters, EarlyView.
Natural enzyme evolution can be retraced by protein engineering methods such as directed evolution, rational design, and ancestral sequence reconstruction. These approaches reveal how enzymes emerged from ligand‐binding scaffolds, developed varying substrate preferences, formed oligomeric complexes, adapted to environmental changes, and evolved novel ...
Lukas Drexler   +2 more
wiley   +1 more source

Elucidating the functional significance of catalytic and chitin-binding domains for the anti-cancer property of a bacterial endochitinase

open access: yesJournal of Genetic Engineering and Biotechnology
Chitinases are enzymes that facilitate the breakdown of chitin and also interact with carbohydrate moieties such as heparin sulphate due to structural similarity with chitin, thereby influencing cell adherence and migration.
Ankita Shrivastava   +5 more
doaj   +1 more source

IMPDH inhibition enhances cytarabine efficacy in SAMHD1‐expressing leukaemia cells via guanine nucleotide depletion

open access: yesMolecular Oncology, EarlyView.
Cytarabine is a key therapy for acute myeloid leukaemia (AML), but its efficacy is limited by the dNTPase SAMHD1, which hydrolyses its active metabolite. Screening nucleotide biosynthesis inhibitors revealed that IMPDH inhibitors selectively sensitise SAMHD1‐proficient AML cells to cytarabine.
Miriam Yagüe‐Capilla   +9 more
wiley   +1 more source

Rational Design of an Orthogonal Pair of Bimolecular RNase P Ribozymes through Heterologous Assembly of Their Modular Domains

open access: yesBiology, 2019
The modular structural domains of multidomain RNA enzymes can often be dissected into separate domain RNAs and their noncovalent assembly can often reconstitute active enzymes.
Yuri Nozawa   +4 more
doaj   +1 more source

Structural and functional analysis of a phospho-dependent molecular switch: Rv1827 from Mycobacterium tuberculosis [PDF]

open access: yes, 2009
Forkhead-associated (FHA) domains have gained considerable prominence as ubiquitous phosphothreonine-dependent binding modules; however, their precise roles in Ser/Thr kinase pathways and mechanisms of regulation remain unclear.
Nott, T J, Nott, T.J.
core  

FAK catalytic domain binds multiple phosphatidylinositol phosphates.

open access: yes, 2017
Fusion proteins were incubated with BODIPY labeled short acyl chain (C6) phospholipids and florescence anisotropy was measured. A) ΔmP for BODIPY labeled PI, PI(4)P, PI(4,5)P2 and PI(3,4,5)P3 in the presence of 100 μM GST, GST wild type catalytic domain ...
Michael D. Schaller (2101708)   +1 more
core   +1 more source

Heterozygous loss‐of‐function alleles associate the conserved 3′‐5′ exoribonuclease EXOSC10 with hypersensitivity to the anticancer drug 5‐fluorouracil

open access: yesMolecular Oncology, EarlyView.
EXOSC10, an essential nuclear RNA exosome‐associated 3′‐5′ exoribonuclease, is inhibited by the anticancer drug 5‐fluorouracil (5‐FU), and EXOSC10 depletion increases 5‐FU sensitivity. The colon‐cancer variant EXOSC10S402T, located in a proteolysis motif, is stable and nuclear but nonfunctional in vivo.
Radhika Sain   +10 more
wiley   +1 more source

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