Results 91 to 100 of about 574,974 (306)
The cysteine protease TcCYSPR04 T. cacao accumulates in senescent leaves and change the biotrophic phase for saprophytic tissues infected by M. perniciosa [PDF]
, 2011 A cysteine proteinase named TcCYSPR04 was identified in a cDNA library of the Theobroma cacao-Moniliophthora perniciosa interaction, in the ESTtik-CIRAD database and in the cacao genome of MARS. TcCYSPR04 presents an ORF of 1068 bp encoding protein with:
Cardoso, Thyago Hermylly Santana +5 more
core
Activities and properties of calcineurin catalytic domain
Chinese 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
FEBS Letters, EarlyView.This study reveals a unique active site enriched in methionine residues and demonstrates that these residues play a critical role by stabilizing carbocation intermediates through novel sulfur–cation interactions. Structure‐guided mutagenesis further revealed variants with significantly altered product profiles, enhancing pseudopterosin formation. These
Marion Ringel +13 more
wiley +1 more source
BiomoleculesThe 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
BMC 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
p97 Disease Mutations Modulate Nucleotide-Induced Conformation to Alter Protein-Protein Interactions. [PDF]
, 2016 The AAA+ ATPase p97/VCP adopts at least three conformations that depend on the binding of ADP and ATP and alter the orientation of the N-terminal protein-protein interaction (PPI) domain into up and down conformations.
Arkin, Michelle +2 more
core
Structure of rabbit liver fructose 1,6-bisphosphatase at 2.3 Å resolution [PDF]
, 1999 The three-dimensional structure of the R form of rabbit liver fructose 1,6-bisphosphatase (Fru-1,6-Pase; E.C. 3.1.3.11) has been determined by a combination of heavy-atom and molecular-replacement methods.
Erman, M. +5 more
core +2 more sources
Catalytic domains in porous catalysts
, 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]
Journal 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
FEBS Letters, EarlyView.Biomolecular condensates formed by fused in sarcoma (FUS) are dissolved by high ATP concentrations yet persist in cells. Using a reconstituted system, we demonstrate that valosin‐containing protein (VCP), an AAA+ ATPase, counteracts ATP‐driven dissolution of FUS condensates through its D2 ATPase activity.
Hitomi Kimura +2 more
wiley +1 more source