Results 31 to 40 of about 349,791 (266)

Structural Complementation of the Catalytic Domain of Pseudomonas Exotoxin A [PDF]

open access: yesJournal of Molecular Biology, 2014
The catalytic moiety of Pseudomonas exotoxin A (domain III or PE3) inhibits protein synthesis by ADP-ribosylation of eukaryotic elongation factor 2. PE3 is widely used as a cytocidal payload in receptor-targeted protein toxin conjugates. We have designed and characterized catalytically inactive fragments of PE3 that are capable of structural ...
Boland, Erin L.   +4 more
openaire   +3 more sources

Biochemical and structural analysis of a site directed mutant of manganese dependent aminopeptidase P from Streptomyces lavendulae [PDF]

open access: yesJournal of BioScience and Biotechnology, 2015
Aminopeptidase P (APP) removes N-terminal amino acids from peptides and proteins when the penultimate residue is proline. To understand the structure-function relationships of aminopeptidase P of Streptomyces lavendulae, a conserved arginine residue was ...
ARYA NANDAN, KESAVAN M. NAMPOOTHIRI
doaj  

Polyhydroxyalkanoate synthase (PhaC): The key enzyme for biopolyester synthesis

open access: yesCurrent Research in Biotechnology, 2022
Polyhydroxyalkanoates (PHAs) are considered good candidates in replacing commercial petrochemical plastics in certain applications like single-use packaging since they are biodegradable, biocompatible and share similar properties with conventional ...
Soon Zher Neoh   +6 more
doaj   +1 more source

Autoantibodies against the catalytic domain of BRAF are not specific serum markers for rheumatoid arthritis. [PDF]

open access: yesPLoS ONE, 2011
BACKGROUND: Autoantibodies to the catalytic domain of v-raf murine sarcoma viral oncogene homologue B1 (BRAF) have been recently identified as a new family of autoantibodies involved in rheumatoid arthritis (RA).
Wenli Li   +8 more
doaj   +1 more source

A Catalytic Domain of Eukaryotic DNA Topoisomerase I [PDF]

open access: yesJournal of Biological Chemistry, 1998
Eukaryotic type IB topoisomerases catalyze the cleavage and rejoining of DNA strands through a DNA-(3'-phosphotyrosyl)-enzyme intermediate. The 314-amino acid vaccinia topoisomerase is the smallest member of this family and is distinguished from its cellular counterparts by its specificity for cleavage at the target sequence 5'-CCCTT downward arrow ...
C, Cheng, S, Shuman
openaire   +2 more sources

Mutational analysis of a ras catalytic domain. [PDF]

open access: yesMolecular and Cellular Biology, 1986
We used linker insertion-deletion mutagenesis to study the catalytic domain of the Harvey murine sarcoma virus v-rasH transforming protein, which is closely related to the cellular rasH protein. The mutants displayed a wide range of in vitro biological activity, from those that induced focal transformation of NIH 3T3 cells with approximately the same ...
Willumsen, B M   +7 more
openaire   +2 more sources

Two Catalytic Domains Are Required for Protein Deacetylation [PDF]

open access: yesJournal of Biological Chemistry, 2006
Histone deacetylase (HDAC)-6 was recently identified as a dual substrate, possibly multisubstrate, deacetylase that can act both on acetylated histone tails and on alpha-tubulin acetylated on Lys40. HDAC-6 is unique among deacetylases in having two hdac domains, and we have used this enzyme as a useful model to dissect the structural requirements for ...
Zhang, Yu   +3 more
openaire   +4 more sources

A small molecule inhibitor of leucine carboxyl methyltransferase-1 inhibits cancer cell survival

open access: yesFrontiers in Drug Discovery
Reversible phosphorylation is the basis for signal transduction in eukaryotic cells, and this is tightly controlled by the complex interplay of kinases and phosphatases.
O. A. Arosarena   +4 more
doaj   +1 more source

Identification of residues in the heme domain of soluble guanylyl cyclase that are important for basal and stimulated catalytic activity. [PDF]

open access: yesPLoS ONE, 2011
Nitric oxide signals through activation of soluble guanylyl cyclase (sGC), a heme-containing heterodimer. NO binds to the heme domain located in the N-terminal part of the β subunit of sGC resulting in increased production of cGMP in the catalytic domain
Padmamalini Baskaran   +3 more
doaj   +1 more source

Complementary function of the two catalytic domains of APOBEC3G

open access: yesVirology, 2005
The HIV-1 viral accessory protein Vif prevents the encapsidation of the antiviral cellular cytidine deaminases APOBEC3F and APOBEC3G by inducing their proteasomal degradation. In the absence of Vif, APOBEC3G is encapsidated and blocks virus replication by deaminating cytosines of the viral cDNA.
Navarro, Francisco   +6 more
openaire   +2 more sources

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