Fibrocystin interacts with CAML, a protein involved in Ca2+ signaling
about
Transmembrane and ubiquitin-like domain containing 1 (Tmub1) regulates locomotor activity and wakefulness in mice and interacts with CAMLG.MUC1 mucin interacts with calcium-modulating cyclophilin ligand.Abnormalities in focal adhesion complex formation, regulation, and function in human autosomal recessive polycystic kidney disease epithelial cellsActivation of Trpv4 reduces the hyperproliferative phenotype of cystic cholangiocytes from an animal model of ARPKD.Autosomal recessive polycystic kidney disease and congenital hepatic fibrosis: summary statement of a first National Institutes of Health/Office of Rare Diseases conferenceThe cAMP effectors Epac and protein kinase a (PKA) are involved in the hepatic cystogenesis of an animal model of autosomal recessive polycystic kidney disease (ARPKD).Diagnosis, pathogenesis, and treatment prospects in cystic kidney disease.Molecular and cellular pathogenesis of autosomal recessive polycystic kidney disease.Ciliary dysfunction in polycystic kidney disease: an emerging model with polarizing potentialPrimary cilia and kidney injury: current research status and future perspectivesTherapeutic Targets in Polycystic Liver Disease.Activation of the AKT/mTOR pathway in autosomal recessive polycystic kidney disease (ARPKD).Conditional deletion of calcium-modulating cyclophilin ligand causes deafness in mice.Pathways, perspectives and pursuits in polycystic kidney disease.TMUB1 Inhibits BRL-3A Hepatocyte Proliferation by Interfering with the Binding of CAML to Cyclophilin B through its TM1 Hydrophobic Domain.
P2860
Q28751305-A2566FB9-394E-4C29-A36F-019F1A0AF63AQ33398890-841E303F-7156-4A54-83E2-A5B3C6BDBD97Q33783518-2E0C0611-D8B9-4D98-9D0D-D8852BAC02D6Q33987179-43E24EF9-EAD8-4B94-9D9B-472019786AF1Q34052964-91DA8FBE-733F-4801-AF30-580549DF5954Q34717186-A23F79F1-1FDF-4D4D-8963-8049838710C4Q36505469-1840EC8E-D5F8-4CCC-8059-E752E86B5487Q36679348-F15F8CCA-8A59-4948-84F6-377DEBA76DDCQ37175323-E9AA1E17-9823-4C2B-A1B5-BAC93791997CQ37234721-65091FA0-B9F2-47AA-BC2D-BCD0545157D7Q38443908-C8E2658E-0C17-4D92-948F-ACEFE6035131Q46142296-C6AFD67A-3065-4718-B7A2-A8D9F9D58DFDQ48777718-46884CB3-17F9-4CA8-A7D9-15921E5B9CC6Q53958174-513C545A-832F-40B1-A654-03510699D273Q55517627-C53F4427-18B2-46BA-B814-E6BF4B8D4222
P2860
Fibrocystin interacts with CAML, a protein involved in Ca2+ signaling
description
2005 nî lūn-bûn
@nan
2005 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Fibrocystin interacts with CAML, a protein involved in Ca2+ signaling
@ast
Fibrocystin interacts with CAML, a protein involved in Ca2+ signaling
@en
Fibrocystin interacts with CAML, a protein involved in Ca2+ signaling
@en-gb
Fibrocystin interacts with CAML, a protein involved in Ca2+ signaling
@nl
type
label
Fibrocystin interacts with CAML, a protein involved in Ca2+ signaling
@ast
Fibrocystin interacts with CAML, a protein involved in Ca2+ signaling
@en
Fibrocystin interacts with CAML, a protein involved in Ca2+ signaling
@en-gb
Fibrocystin interacts with CAML, a protein involved in Ca2+ signaling
@nl
prefLabel
Fibrocystin interacts with CAML, a protein involved in Ca2+ signaling
@ast
Fibrocystin interacts with CAML, a protein involved in Ca2+ signaling
@en
Fibrocystin interacts with CAML, a protein involved in Ca2+ signaling
@en-gb
Fibrocystin interacts with CAML, a protein involved in Ca2+ signaling
@nl
P2093
P1476
Fibrocystin interacts with CAML, a protein involved in Ca2+ signaling
@en
P2093
Christopher J Ward
Chunfa Huang
Junko Nagano
Kenichiro Kitamura
Kimio Tomita
Kristine M Hujer
R Tyler Miller
Richard J Bram
Ulrich Hopfer
P356
10.1016/J.BBRC.2005.10.022
P407
P577
2005-12-16T00:00:00Z