Results 111 to 120 of about 19,935,117 (378)

Relation between Morphology and Porous Structure of SAPO-11 Molecular Sieves and Chemical and Phase Composition of Silicoaluminophosphate Gels [PDF]

, 2022
М. Р. Аглиуллин, R. Е. Yakovenko, Yu. G. Kolyagin, Д. В. Серебренников, Farkhad S. Vildanov, Т. Р. Просочкина, Б. И. Кутепов   +6 more
openalex   +1 more source

Structure formation in active networks

, 2011
Structure formation and constant reorganization of the actin cytoskeleton are key requirements for the function of living cells. Here we show that a minimal reconstituted system consisting of actin filaments, crosslinking molecules and molecular-motor ...
A Lau, Andreas R. Bausch, BD Hoffman, D Smith, D Vignjevic, DA Fletcher, DA Weitz, F Backouche, F Gallet, F Juelicher, GH Koenderink, IS Aranson, J-F Joanny, J-F Joanny, JA Spudich, JC Crocker, JC Effler, JS Langer, K Kruse, KM Schmoller, L LeGoff, LW Janson, MMAE Claessens, O Lieleg, PM Bendix, R Metzler, R Metzler, RE Kane, S MacLean-Fletcher, Simone Köhler, SS Margossian, T Guerin, T Viscek, TB Liverpool, TB Liverpool, Volker Schaller   +35 more
core   +1 more source

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

FEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes, Guilherme M. Azevedo, Amanda P. Barcellos, Diana Bahia   +3 more
wiley   +1 more source

Atomic Level Insight into Wetting and Structure of Ag Droplet on Graphene Coated Copper Substrate—Molecular Dynamics versus Experiment [PDF]

, 2021
Aleksandra Drewienkiewicz, Arkadiusz Żydek, Marcela E. Trybula, J. Pstruś   +3 more
openalex   +1 more source

First-principles molecular structure search with a genetic algorithm

, 2015
The identification of low-energy conformers for a given molecule is a fundamental problem in computational chemistry and cheminformatics. We assess here a conformer search that employs a genetic algorithm for sampling the low-energy segment of the ...
Baldauf, Carsten, Blum, Volker, Supady, Adriana   +2 more
core   +2 more sources

Structural insights into lacto‐N‐biose I recognition by a family 32 carbohydrate‐binding module from Bifidobacterium bifidum

FEBS Letters, EarlyView.
Bifidobacterium bifidum establishes symbiosis with infants by metabolizing lacto‐N‐biose I (LNB) from human milk oligosaccharides (HMOs). The extracellular multidomain enzyme LnbB drives this process, releasing LNB via its catalytic glycoside hydrolase family 20 (GH20) lacto‐N‐biosidase domain.
Xinzhe Zhang, Naoki Sunagawa, Toma Kashima, Kiyohiko Igarashi, Akimasa Miyanaga, Shinya Fushinobu   +5 more
wiley   +1 more source

NONEXPERIMENTAL SCREENING OF THE WATER SOLUBILITY, LIPOPHILICITY, BIOAVAILABILITY, MUTAGENICITY AND TOXICITY OF VARIOUS PESTICIDES WITH QSAR MODELS AID [PDF]

Chemistry Journal of Moldova: General, Industrial and Ecological Chemistry, 2013
In our study the dataset containing 489 pesticides and their active substances of different classes of organic compounds was used for analysis. For compounds of analyzed dataset the values of lipophilicity, water solubility, toxicity, bioavailability and
O.G. Kolumbin, L.N. Ognichenko, A.G. Artemenko, P.G. Polischuk, М.A. Kulinsky, Е.N. Мuratov, V.E. Kuz’min, V.A. Bobeica   +7 more
doaj  

The Caenorhabditis elegans DPF‐3 and human DPP4 have tripeptidyl peptidase activity

FEBS Letters, EarlyView.
The dipeptidyl peptidase IV (DPPIV) family comprises serine proteases classically defined by their ability to remove dipeptides from the N‐termini of substrates, a feature that gave the family its name. Here, we report the discovery of a previously unrecognized tripeptidyl peptidase activity in DPPIV family members from two different species.
Aditya Trivedi, Rajani Kanth Gudipati
wiley   +1 more source

Virtual Insights into Natural Compounds as Potential 5α-Reductase Type II Inhibitors: A Structure-Based Screening and Molecular Dynamics Simulation Study [PDF]

, 2023
Sibhghatulla Shaikh, Shahid Ali, Jeong Ho Lim, Khurshid Ahmad, Ki Soo Han, Eun Ju Lee, Inho Choi   +6 more
openalex   +1 more source

The zinc finger domains of PARP‐1 are selectively and potently inhibited by the Au(I)‐based drugs sodium aurothiomalate and aurothioglucose

FEBS Letters, EarlyView.
PARP‐1 is a key enzyme in the DNA damage response, and its inhibition induces cancer cell death via synthetic lethality. Au(I)‐based drugs, such as aurothioglucose and sodium aurothiomalate, block PARP‐1's DNA‐dependent activity by targeting its zinc finger domains.
Uliana Bashtanova, Melinda Jane Duer
wiley   +1 more source