The amino acid sequence of protein II and its phosphorylation site for protein kinase C; the domain structure Ca2+-modulated lipid binding proteins.

The amino acid sequence of protein II and its phosphorylation site for protein kinase C; the domain structure Ca2+-modulated lipid binding proteins.

Item
http://www.wikidata.org/entity/Q41340792
Characterization of Ca2(+)-dependent phospholipid binding, vesicle aggregation and membrane fusion by annexinsA strategy for isolation of cDNAs encoding proteins affecting human intestinal epithelial cell growth and differentiation: characterization of a novel gut-specific N-myristoylated annexinAnnexin A4 self-association modulates general membrane protein mobility in living cells.A 32 kDa lipocortin from human mononuclear cells appears to be identical with the placental inhibitor of blood coagulationPrimary structure of the human, membrane-associated Ca2+-binding protein p68 a novel member of a protein familyCalcium channel activity of purified human synexin and structure of the human synexin geneBiosynthesis, secretion and extracellular localization of anchorin CII, a collagen-binding protein of the calpactin family.Distinct cellular expression pattern of annexins in Hydra vulgaris.p36, the major cytoplasmic substrate of src tyrosine protein kinase, binds to its p11 regulatory subunit via a short amino-terminal amphiphatic helix.Expression of annexins as a function of cellular growth stateMonoclonal antibodies specific to a Ca2(+)-bound form of lipocortin I distinguish its Ca2(+)-dependent phospholipid-binding ability from its ability to inhibit phospholipase A2.Identification of the 32 kDa components of bovine lens EDTA-extractable protein as endonexins I and II.Activated protein kinase C alpha associates with annexin VI from skeletal muscle.Purification and partial sequence analysis of plant annexins.Ca2+ concentration during binding determines the manner in which annexin V binds to membranesA 36 kDa monomeric protein and its complex with a 10 kDa protein both isolated from bovine aorta are calpactin-like proteins that differ in their Ca2+-dependent calmodulin-binding and actin-severing properties.
P2860

The amino acid sequence of protein II and its phosphorylation site for protein kinase C; the domain structure Ca2+-modulated lipid binding proteins.

Item
http://www.wikidata.org/entity/Q41340792
description
1987 nî lūn-bûn
@nan
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
1987年论文
@zh
1987年论文
@zh-cn
name
The amino acid sequence of pro ...... ulated lipid binding proteins.
@en
type
label
The amino acid sequence of pro ...... ulated lipid binding proteins.
@en
prefLabel
The amino acid sequence of pro ...... ulated lipid binding proteins.
@en
P1433
P1476
P2093
P2860
P304
P31
P407
P433
P478
P577
P698
P921
P932
P1433
P1476
The amino acid sequence of pro ...... ulated lipid binding proteins.
@en
P2093
P2860
P304
P31
P407
P433
P478
P577
P698
P921
P932