Zobrazeno 1 - 9
of 9
pro vyhledávání: '"M C, Seabra"'
Autor:
J B, Pereira-Leal, M C, Seabra
Publikováno v:
Journal of molecular biology. 301(4)
The Rab/Ypt/Sec4 family forms the largest branch of the Ras superfamily of GTPases, acting as essential regulators of vesicular transport pathways. We used the large amount of information in the databases to analyse the mammalian Rab family. We defin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4dcbd8e7893832a6366054dd0e40d0d2
https://pubmed.ncbi.nlm.nih.gov/10966806
https://pubmed.ncbi.nlm.nih.gov/10966806
Autor:
M C, Seabra, G L, James
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 84
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::cec1c16e803b83669bcf479da3bb40ff
https://pubmed.ncbi.nlm.nih.gov/9666454
https://pubmed.ncbi.nlm.nih.gov/9666454
Autor:
M C, Seabra
Publikováno v:
The Journal of biological chemistry. 271(24)
Geranylgeranylation of Rab GTPases is an essential post-translational modification that enables Rabs to associate with intracellular membranes where they regulate exocytic and endocytic pathways. Geranylgeranylation is initiated by formation of a sta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bc573a6cc35d502be1a4e2d4458f36e4
https://pubmed.ncbi.nlm.nih.gov/8662963
https://pubmed.ncbi.nlm.nih.gov/8662963
Autor:
F, Shen, M C, Seabra
Publikováno v:
The Journal of biological chemistry. 271(7)
Rab proteins are Ras-related small GTPases that are digeranylgeranylated at carboxyl-terminal cysteines, a modification essential for their action as molecular switches regulating intracellular vesicular transport. Geranylgeranylation of Rabs is a co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4e572872fd9826a7ebfd24e4fe790f1e
https://pubmed.ncbi.nlm.nih.gov/8631982
https://pubmed.ncbi.nlm.nih.gov/8631982
Publikováno v:
Methods in enzymology. 257
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::30e9774d748f4b464f461d1599bfd1f1
https://pubmed.ncbi.nlm.nih.gov/8583933
https://pubmed.ncbi.nlm.nih.gov/8583933
Publikováno v:
The Journal of biological chemistry. 269(3)
Rab escort proteins (REPs) bind to newly synthesized Rab proteins and remain bound during and after the attachment of a geranylgeranyl (GG) group by the catalytic component of the Rab GG transferase. Transfer of the GG group is absolutely dependent o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8b514e13511322ed31e047a57e251259
https://pubmed.ncbi.nlm.nih.gov/8294464
https://pubmed.ncbi.nlm.nih.gov/8294464
Publikováno v:
The Journal of biological chemistry. 268(16)
Rab geranylgeranyl transferase (Rab GG transferase) attaches 20-carbon geranylgeranyl groups to cysteine residues in Rab proteins that contain the COOH-terminal sequence Cys-X-Cys or Cys-Cys. Rab GG transferase consists of two components that are sep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::fb599fe369f2a6f49fc2b1044b5c662d
https://pubmed.ncbi.nlm.nih.gov/8505342
https://pubmed.ncbi.nlm.nih.gov/8505342
Publikováno v:
The Journal of biological chemistry. 267(20)
Rab proteins are membrane-bound prenylated GTP-binding proteins required for the targeted movement of membrane vesicles from one organelle to another. In the current paper we have characterized and purified an enzyme that attaches geranylgeranyl resi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::01d4218383714570a306ecfd2c6d2d0c
https://pubmed.ncbi.nlm.nih.gov/1321151
https://pubmed.ncbi.nlm.nih.gov/1321151
Publikováno v:
The Journal of biological chemistry. 266(16)
The protein farnesyltransferase purified from rat brain contains two nonidentical subunits, alpha and beta. The holoenzyme forms a stable complex with [3H]farnesyl pyrophosphate (FPP) that can be isolated by gel filtration. The [3H]FPP is not covalen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::80fe7a850bebbee6a8249e319544a603
https://pubmed.ncbi.nlm.nih.gov/2037606
https://pubmed.ncbi.nlm.nih.gov/2037606