Results 251 to 260 of about 4,369,824 (302)

Mesophyll protoplasts: a key tool for deciphering plant nutrient starvation pathways. [PDF]

Front Plant Sci
Yashan T, Jianju S, Jinhui L, Feng C, Zhuoran S, Jiayi L, Yan H, Junhan M, Guoting C, Yanfeng W, Fengfeng D.   +10 more
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Iron Deficiency Reduces Cadmium Translocation in Peanut by Increasing the Root Cell Wall Reservoir. [PDF]

Plants (Basel)
Liu R, Ma J, Zhang Q, Shi G.
europepmc   +1 more source

Metal thiosemicarbazonates as dual mR2 RNR and colchicine-site tubulin inhibitors: from biochemical inhibition to mitotic arrest in MCF-7 breast cancer cells.

Inorg Chem Front
Palamarciuc O, Ciubotaru BI, Stoica AC, Hejl M, Hammerstad M, Balan-Porcarasu M, Shova S, Gátszegi GT, Popović Bijelić A, Reynisson J, Jakupec MA, Zalibera M, Rapta P, Enyedy ÉA, Peptanariu D, Dascalu M, Cazacu M, Hamel E, Arion VB.   +18 more
europepmc   +1 more source

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Electrochemical Studies of the Mono-Fe, Fe−Zn, and Fe−Fe Metalloisoforms of Bacteriophage λ Protein Phosphatase

Biochemistry, 2003
Bacteriophage lambda protein phosphatase (lambdaPP) is a member of a large superfamily of metallophosphoesterases, including serine/threonine protein phosphatases, purple acid phosphatases, 5'-nucleotidase, and DNA repair enzymes such as Mre11. Members of this family share several common characteristics, including a common phosphoesterase motif ...
Tiffany A, Reiter, Frank, Rusnak
openaire   +2 more sources

Methods for Heterologous Overproduction of Fe-S Proteins

2021
Proteins carrying iron-sulfur ([Fe-S]) clusters are critical to the basic metabolism of all organisms. Structural and biochemical investigations of many such [Fe-S] cluster proteins depend on recombinant overproduction using heterologous bacterial hosts such as Escherichia coli .
Elliot I, Corless, Edwin, Antony
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The c-Fes Family of Protein-Tyrosine Kinases

Critical Reviews™ in Oncogenesis, 1998
The human c-fes protooncogene encodes a protein-tyrosine kinase (c-Fes) distinct from c-Src, c-Abl and other nonreceptor tyrosine kinases. Although originally identified as the cellular homolog of several transforming retroviral oncoproteins, Fes was later found to exhibit strong expression in myeloid hematopoietic cells and to play a direct role in ...
T E, Smithgall, J A, Rogers, K L, Peters, J, Li, S D, Briggs, J M, Lionberger, H, Cheng, A, Shibata, B, Scholtz, S, Schreiner, N, Dunham   +10 more
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Functional Models of [Fe—S] Nitrosyl Proteins.

ChemInform, 2004
AbstractFor Abstract see ChemInform Abstract in Full Text.
N. A. Sanina, S. M. Aldoshin
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The Bonding Nature of Fe–CO Complexes in Heme Proteins

Inorganic Chemistry, 2022
Although carbon monoxide (CO) has been known to bind to the ferrous heme in cytochrome P450 enzymes (P450s) since the earliest days of P450 research, details on the nature of the ferrous-CO bonding remain elusive. This study employed dispersion-corrected density functional theory (DFT) calculations and DFT-based theoretical analyses to investigate the ...
Shuyang Liu, Songyan Xia, Dongxiao Yue, Haoran Sun, Hajime Hirao   +4 more
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