Results 101 to 110 of about 4,561,775 (254)

The domain architecture of large guanine nucleotide exchange factors for the small GTP-binding protein Arf

open access: yesBMC Genomics, 2005
Background Small G proteins, which are essential regulators of multiple cellular functions, are activated by guanine nucleotide exchange factors (GEFs) that stimulate the exchange of the tightly bound GDP nucleotide by GTP.
Geldner Niko   +8 more
doaj   +1 more source

The centrosomal deubiquitylase USP21 regulates Gli1 transcriptional activity and stability [PDF]

open access: yes, 2016
USP21 is a centrosome-associated deubiquitylase (DUB) that has been implicated in the formation of primary cilia - crucial organelles for the regulation of the Hedgehog (Hh) signaling pathway in vertebrates. Here, we identify KCTD6 - a cullin-3 E3-ligase
Bertsoulaki, Erithelgi   +6 more
core   +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

Functional Characterization of the SHIP1-Domains Regarding Their Contribution to Inositol 5-Phosphatase Activity

open access: yesBiomolecules
The Src homology 2 domain-containing inositol 5-phosphatase 1 (SHIP1) is a multidomain protein consisting of two protein–protein interaction domains, the Src homology 2 (SH2) domain, and the proline-rich region (PRR), as well as three phosphoinositide ...
Spike Murphy Müller   +2 more
doaj   +1 more source

Evidence for disulfide bonds in SR Protein Kinase 1 (SRPK1) that are required for activity and nuclear localization. [PDF]

open access: yesPLoS ONE, 2017
Serine/arginine protein kinases (SRPKs) phosphorylate Arg/Ser dipeptide-containing proteins that play crucial roles in a broad spectrum of basic cellular processes.
Maria Koutroumani   +4 more
doaj   +1 more source

A new subfamily of fungal subtilases: structural and functional analysis of a Pleurotus ostreatus member [PDF]

open access: yes, 2005
Pleurotus ostreatus produces several extracellular proteases which are believed to be involved in the regulation of the ligninolytic activities of this fungus. Recently, purification and characterization of the most abundant P.
FARACO, VINCENZA   +5 more
core   +2 more sources

Catalytic domains in porous catalysts

open access: yes, 2018
Understanding of the catalytic domains within porous catalysts is essential for control of these systems in order to obtain desired reaction yields and selectivities. This body of work consists of studies on two types of porous catalysts, mesoporous silica and zeolites, that can have interesting cooperative catalytic interactions between the inorganic ...
openaire   +3 more sources

1.92 Angstrom Zinc-Free APOBEC3F Catalytic Domain Crystal Structure [PDF]

open access: yesJournal of Molecular Biology, 2016
The APOBEC3 family of DNA cytosine deaminases is capable of restricting the replication of HIV-1 and other pathogens. Here, we report a 1.92 Å resolution crystal structure of the Vif-binding and catalytic domain of APOBEC3F (A3F). This structure is distinct from the previously published APOBEC and phylogenetically related deaminase structures, as it is
Shaban, Nadine M.   +4 more
openaire   +2 more sources

Mutational analysis of two residues in the DYRK homology box of the protein kinase DYRK1A

open access: yesBMC Research Notes, 2018
Objective Dual specificity tyrosine phosphorylation-regulated kinases (DYRK) contain a characteristic sequence motif (DYRK homology box, DH box) that is located N-terminal of the catalytic domain and supports the autophosphorylation of a conserved ...
Esti Wahyu Widowati   +2 more
doaj   +1 more source

The enzymatic processing of α-dystroglycan by MMP-2 is controlled by two anchoring sites distinct from the active site. [PDF]

open access: yesPLoS ONE, 2018
Dystroglycan (DG) is a membrane receptor, belonging to the dystrophin-glycoprotein complex (DGC) and formed by two subunits, α-dystroglycan (α-DG) and β-dystroglycan (β -DG).
Magda Gioia   +12 more
doaj   +1 more source

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