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FNTB protein, human
Known as:
CAAX Box Farnesyltransferase Beta
, Protein Farnesyltransferase Beta Subunit
, CAAX Box Farnesyltransferase Beta Subunit
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Protein farnesyltransferase subunit beta (437 aa, ~49 kDa) is encoded by the human FNTB gene. This protein plays a role in protein farnesylation.
National Institutes of Health
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Related topics
Related topics
7 relations
Enzyme Gene
FNTB gene
FNTB wt Allele
Protein Complex Subunit
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
2020
2020
Rce1 suppresses invasion and metastasis of hepatocellular carcinoma via epithelial‐mesenchymal transition induced by the TGF‐β1/H‐Ras signaling pathway
Chaoqun Ma
,
Yan Yang
,
Lei Xu
,
Wei Tu
,
Feng Chen
,
Jianming Wang
Journal of Cellular Physiology
2020
Corpus ID: 202556412
Ras converting enzyme 1 (Rce1) plays an important role in invasion and metastasis of malignancy. However, the mechanism has not…
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2020
2020
Combining mutagenesis on Glu281 of prenyltransferase NovQ and metabolic engineering strategies for the increased prenylated activity towards menadione
Wenfeng Ni
,
Zhiming Zheng
,
+7 authors
Genhai Zhao
Applied Microbiology and Biotechnology
2020
Corpus ID: 211729567
Prenyltransferase NovQ is a vital class involved in the biosynthesis of secondary metabolites such as clorobiocin and novobiocin…
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2014
2014
The regulator of G protein signaling (RGS) domain of G protein–coupled receptor kinase 5 (GRK5) regulates plasma membrane localization and function
Hua Xu
,
Xiaoshan Jiang
,
Ke Shen
,
Christopher C. Fischer
,
P. Wedegaertner
Molecular Biology of the Cell
2014
Corpus ID: 2624380
GRK5/GRK4 chimeras and point mutations in GRK5 identify a short sequence within the RGS domain in GRK5 that is critical for GRK5…
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Highly Cited
2011
Highly Cited
2011
Splice variant–specific cellular function of the formin INF2 in maintenance of Golgi architecture
Vinay Ramabhadran
,
F. Korobova
,
G. Rahme
,
H. Higgs
Molecular Biology of the Cell
2011
Corpus ID: 14123585
INF2 is a unique formin that can both polymerize and depolymerize actin. One INF2 splice variant localizes in an actin-dependent…
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2011
2011
Computational analysis of the fructosyltransferase enzymes in plants, fungi and bacteria.
C. Alméciga-Díaz
,
A. Gutierrez
,
Isabella Bahamon
,
Alexander Rodríguez
,
M. A. Rodríguez
,
O. Sánchez
Gene
2011
Corpus ID: 5379097
2011
2011
FPTB, a novel CA‐4 derivative, induces cell apoptosis of human chondrosarcoma cells through mitochondrial dysfunction and endoplasmic reticulum stress pathways
Ju-Fang Liu
,
Y. Fong
,
Kai-Wei Chang
,
S. Kuo
,
Chih-Shiang Chang
,
Chih-Hsin Tang
Journal of Cellular Biochemistry
2011
Corpus ID: 29438734
Chondrosarcoma is a malignant primary bone tumor that responds poorly to both chemotherapy and radiation therapy. The aim of this…
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Highly Cited
2006
Highly Cited
2006
Rap1-Mediated Activation of Extracellular Signal-Regulated Kinases by Cyclic AMP Is Dependent on the Mode of Rap1 Activation
Zhiping Wang
,
Tara J. Dillon
,
+4 authors
P. Stork
Molecular and Cellular Biology
2006
Corpus ID: 42976186
ABSTRACT Like other small G proteins of the Ras superfamily, Rap1 is activated by distinct guanine nucleotide exchange factors…
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Highly Cited
2002
Highly Cited
2002
Socius Is a Novel Rnd GTPase-Interacting Protein Involved in Disassembly of Actin Stress Fibers
H. Katoh
,
A. Harada
,
K. Mori
,
M. Negishi
Molecular and Cellular Biology
2002
Corpus ID: 37965068
ABSTRACT Rho family small GTPases are key regulators of the actin cytoskeleton in various cell types. The Rnd proteins, Rnd1…
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1997
1997
Synthesis and biological activity of semipeptoid farnesyltransferase inhibitors.
H. Reuveni
,
A. Gitler
,
E. Poradosu
,
C. Gilon
,
A. Levitzki
Bioorganic & Medicinal Chemistry
1997
Corpus ID: 5875020
1993
1993
Protein Farnesyltransferase in Plants (Molecular Cloning and Expression of a Homolog of the [beta] Subunit from the Garden Pea)
Z. Yang
,
C. Cramer
,
J. Watson
Plant Physiology
1993
Corpus ID: 24428787
Protein farnesyltransferase is a heterodimeric enzyme that attaches a farnesyl moiety to C-terminal cysteine residues. Both the…
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