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A Conserved Family of Enzymes That Phosphorylate Inositol Hexakisphosphate
Oleh:
Mulugu, Sashidhar
;
Bai, Wenli
;
Fridy, Peter C
;
Bastidas, Robert J
;
Otto, James C.
;
Haystead, Timothy A.
;
Ribeiro, Anthony A.
;
York, John D.
Jenis:
Article from Bulletin/Magazine
Dalam koleksi:
SCIENCE (keterangan: ada di Proquest) vol. 316 no. 5821 (Apr. 2007)
,
page 106.
Ketersediaan
Perpustakaan FK
Nomor Panggil:
S01.K.2007.04
Non-tandon:
1 (dapat dipinjam: 0)
Tandon:
tidak ada
Lihat Detail Induk
Isi artikel
Inositol pyrophosphates are a diverse group of high-energy signaling molecules whose cellular roles remain an active area of study. We report a previously uncharacterized class of inositol pyrophosphate synthase and find it is identical to yeast Vipl and Aspl proteins, regulators of actin-related protein-2/3 (ARP 2/3) complexes. Vipl and Aspl acted as enzymes that encode inositol hexakisphosphate (JP6) and inositol heptakisphosphate (JP7) kinase activities. Alterations in kinase activity led to defects in cell growth, morphology, and interactions with ARP complex members. The functionality of Aspl and Vipl may provide cells with increased signaling capacity through metabolism of IP6.
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