Network Dynamics as Fingerprints of Thermostability in an In Silico-Engineered DyP-Type Peroxidase. [PDF]
Rodrigues CF +5 more
europepmc +1 more source
Dismantling darkness: interdisciplinary perspectives on melanin degradation. [PDF]
Alcântara LM +9 more
europepmc +1 more source
Segmenting Older Adults by Their Acceptance of Digital Health Care Devices: Cross-Sectional Study Using the Augmented Technology Acceptance Model and K-Means Clustering. [PDF]
Koo T, Jo IH, Pyun DY, Yoo J.
europepmc +1 more source
Kraft Lignin Decomposition by Forest Soil Bacterium Pseudomonas kribbensis CHA-19. [PDF]
Kim D, Kim HW, Lee H.
europepmc +1 more source
Impact of Pharmacovigilance Sensitization on Knowledge and Attitude Amongst Medical and Paramedical Students in a Tertiary Care Teaching Hospital: A Questionnaire-Based Study. [PDF]
Thakare V +4 more
europepmc +1 more source
Short-term efficacy and safety of A-stream glaucoma shunt: a 6-month study. [PDF]
Park HM +5 more
europepmc +1 more source
Comparative Evaluation of Ashwagandha (<i>Withania somnifera</i>) Root Extract and Melatonin for Improving Sleep Quality in Adults: A Prospective, Randomized, Double-Blind, Placebo-Controlled Study. [PDF]
Movva N +4 more
europepmc +1 more source
DyP-Type Peroxidases: Recent Advances and Perspectives [PDF]
In this review, we chart the major milestones in the research progress on the DyP-type peroxidase family over the past decade. Though mainly distributed among bacteria and fungi, this family actually exhibits more widespread diversity. Advanced tertiary structural analyses have revealed common and different features among members of this family ...
Yasushi Sugano, Toru Yoshida
exaly +4 more sources
Characterization of three novel DyP-type peroxidases from Streptomyces chartreusis NRRL 3882
\(\bf Aims\) Actinobacteria are known to produce extracellular enzymes including DyPs. We set out to identify and characterize novel peroxidases from Streptomyces chartreusis NRRL 3882, because \(\textit {S.
Julia E Bandow, Eckhard Hofmann
exaly +2 more sources
DyP-type peroxidases are a family of heme peroxidases named for their ability to degrade persistent anthraquinone dyes. DyP-type peroxidases are subclassified into three classes: classes P, I and V. Based on its genome sequence, Streptomyces avermitilis,
Yasushi Sugano +2 more
exaly +2 more sources

