Results 91 to 100 of about 1,757 (116)

Rab geranylgeranyl transferase activity is required for proper sterol biosynthesis in Arabidopsis thaliana. [PDF]

Plant Cell Physiol
Gutkowska M, Zajbt-Łuczniewska M, Buszewicz D, Anielska-Mazur A, Lipko A, Pączkowski C, Spólnik G, Sojka M, Jaźwiec R, Samborowska E, Swiezewska E, Hoffman M.   +11 more
europepmc   +1 more source

Pharmacophore- and QSAR-guided discovery of natural product inhibitors targeting dehydrosqualene synthase in Staphylococcus aureus. [PDF]

PLoS One
Amorim J, Ortega S, Rodas R, Vélez L, Arteaga D, Carpio J.   +5 more
europepmc   +1 more source

Structure-function insights into the dual role of African swine fever virus pB318L: A typical geranylgeranyl-diphosphate synthase and a nuclear import protein. [PDF]

Virol Sin
Zhao HF, Wang Y, Liu XH, Liu XH, Geng Z, Gao ZQ, Huang L, Weng CJ, Dong YH, Zhang H.   +9 more
europepmc   +1 more source

Ubiquitin specific peptidase 32 acts as an oncogene in epithelial ovarian cancer by deubiquitylating farnesyl-diphosphate farnesyltransferase 1

Ubiquitin specific peptidase 32 acts as an oncogene in epithelial ovarian cancer by deubiquitylating farnesyl-diphosphate farnesyltransferase 1
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Ubiquitin specific peptidase 32 acts as an oncogene in epithelial ovarian cancer by deubiquitylating farnesyl-diphosphate farnesyltransferase 1

Biochemical and Biophysical Research Communications, 2021
Epithelial ovarian cancer (EOC) is the seventh most common cancer worldwide and the deadliest gynecological malignancy because of its aggressiveness and high recurrence rate. To discover new therapeutic targets for EOC, we combined public EOC microarray datasets with our previous in vivo shRNA screening dataset.
Kenjiro Sawada, Tadashi Kimura, Aya Nakae   +2 more
exaly   +3 more sources

Protein farnesyltransferase inhibitors interfere with farnesyl diphosphate binding by rubber transferase

FEBS Journal, 2003
Rubber transferase, a cis‐prenyltransferase, catalyzes the addition of thousands of isopentenyl diphosphate (IPP) molecules to an allylic diphosphate initiator, such as farnesyl diphosphate (FPP, 1), in the presence of a divalent metal cofactor. In an effort to characterize the catalytic site of rubber transferase, the effects of two types of protein ...
Katrina Cornish
exaly   +3 more sources

Ras farnesylation as a target for novel antitumor agents: Potent and selective farnesyl diphosphate analog inhibitors of farnesyltransferase

Drug Development Research, 1995
AbstractProtein prenylation is increasingly recognized as an important mechanism by which functional association of proteins to membranes is mediated. Ras proteins, regulators of cell proliferation and differentiation, are among the proteins that undergo farnesylation, one of the two prenylation modifications known.
Mariano Barbacid
exaly   +2 more sources

A New Class of Highly Potent Farnesyl Diphosphate-Competitive Inhibitors of Farnesyltransferase

Journal of Medicinal Chemistry, 1998
Y Iwasawa
exaly   +3 more sources

Farnesyl-diphosphate farnesyltransferase

1997
Dietmar Schomburg, Dörte Stephan
exaly   +2 more sources

Cocrystal Structure of Protein Farnesyltransferase Complexed with a Farnesyl Diphosphate Substrate^,

Biochemistry, 1998
Protein farnesyltransferase (FTase) catalyzes the transfer of the hydrophobic farnesyl group from farnesyl diphosphate (FPP) to cellular proteins such as Ras at a cysteine residue near their carboxy-terminus. This process is necessary for the subcellular localization of these proteins to the plasma membrane and is required for the transforming activity
S B, Long, P J, Casey, L S, Beese
openaire   +2 more sources