Results 241 to 250 of about 6,423,741 (359)

Enhanced production and biodeinking application of β-glucosidase from Aspergillus niger S1 via submerged fermentation using office paper waste through conventional and statistical approaches. [PDF]

BMC Biotechnol
Ali D, Hasanin MS, Abdelraof M, Othman AM, Abdel Karim GSA, Elsayed AM.   +5 more
europepmc   +1 more source

Evolutionarily divergent DUF4465 domains have a common vitamin B12‐binding function

FEBS Open Bio, EarlyView.
We show that DUF4465 family proteins, widespread across bacteria from gut microbiomes, hydrothermal vents, and soil, share a common vitamin B12‐binding function. These augmented β‐jellyroll proteins bind vitamin B12 via extended loops. Our findings establish sequence‐diverse DUF4465 proteins as a widespread class of B12‐binding proteins, highlighting ...
Charlea Clarke, Michal Banasik, Rokas Juodeikis, Martin J. Warren, Richard W. Pickersgill   +4 more
wiley   +1 more source

Systemic dysregulation of apolipoproteins in amyotrophic lateral sclerosis serum

FEBS Open Bio, EarlyView.
Amyotrophic lateral sclerosis (ALS) is a fatal disease that damages motor neurons. This study found that people with ALS show significant changes in blood fats and the proteins that carry them. Several apolipoproteins were higher, lipid balances were altered, and normal protein–lipid relationships were disrupted.
Finula I. Isik, Russell Pickford, Hannah C. Timmins, Olivier Piguet, Glenda M. Halliday, Matthew C. Kiernan, Woojin Scott Kim   +6 more
wiley   +1 more source

Computer-Based Design to Improve Bacillus thuringiensis Chitinase for Industrial Applications. [PDF]

ChemistryOpen
Sree Agash SG, Chandrasekhar G, Vinutha AS, Akshay S, Kanishk P, Rajasekaran R.   +5 more
europepmc   +1 more source

Large‐scale bidirectional arrayed genetic screens identify OXR1 and EMC4 as modifiers of αSynuclein aggregation

FEBS Open Bio, EarlyView.
Activation of the mitochondrial protein OXR1 increases pSyn129 αSynuclein aggregation by lowering ATP levels and altering mitochondrial membrane potential, particularly in response to MSA‐derived fibrils. In contrast, ablation of the ER protein EMC4 enhances autophagic flux and lysosomal clearance, broadly reducing α‐synuclein aggregates.
Sandesh Neupane, Lea Nikolić, Lorenzo Maraio, Thomas Goiran, Nathan Karpilovsky, Stefano Sellitto, Vangelis Bouris, Jiang‐An Yin, Ronald Melki, Edward A Fon, Adriano Aguzzi, Elena De Cecco   +11 more
wiley   +1 more source

Multienzyme Platform for the Synthesis of UDP Sugars and Human Milk Oligosaccharides. [PDF]

Chembiochem
Hoang TS, Lange F, Kleeberg SB, Thomas L, Hoang NH, Reichl U, Rexer TFT.   +6 more
europepmc   +1 more source

Mass spectrometry based identification of AMP‐O‐Tris generated by Thermococcus onnurineus Cas10

FEBS Open Bio, EarlyView.
Isolated Thermococcus onnurineus Cas10 generates the noncanonical ATP‐derived product AMP‐O‐Tris while in Tris‐containing buffer as identified via mass spectrometry, revealing relaxed nucleophile selectivity under isolated conditions. These findings suggest that multiprotein Csm complex assembly restricts Cas10 reactivity toward canonical cyclic ...
Su‐Jin Lee, Ga Seul Lee, JinHan Kim, Kwang‐Hyun Park, Seong‐Ryung Go, Jeong Hee Moon, Eui‐Jeon Woo   +6 more
wiley   +1 more source

Enhanced fibrinolytic enzyme production by Oidiodendron maius through green bioprocessing of agro-industrial residue. [PDF]

PLoS One
Sajid H, Iqbal M, Gull-E-Faran.
europepmc   +1 more source

Intercompartmental communication in senescence

FEBS Open Bio, EarlyView.
Senescent cells experience structural changes in the plasma membrane, endoplasmic reticulum, mitochondria, lysosomes, nucleus, and cytoskeleton. These alterations disrupt crosstalk among cellular compartments, impairing vesicular trafficking, contact sites, and molecular flow.
Krystyna Mazan‐Mamczarz, Eleanor J. Wind, Jixiang Leng, Myriam Gorospe   +3 more
wiley   +1 more source

Safety evaluation of an extension of use of the food enzyme cellulase from the genetically modified <i>Trichoderma reesei</i> strain AR-852. [PDF]

EFSA J
EFSA Panel on Food Enzymes (FEZ), Zorn H, Barat Baviera JM, Bolognesi C, Catania F, Gadermaier G, Greiner R, Mayo B, Mortensen A, Roos YH, Solano MLM, Van Loveren H, Vernis L, Cavanna D, Liu Y.   +14 more
europepmc   +1 more source