Results 1 to 10 of about 43,549 (203)
Protein Prenylation in Plants: Mechanisms and Functional Implications. [PDF]
Protein prenylation is a crucial post-translational modification that involves the formation of a covalent bond between isoprenoid lipids and the cysteine residues of specific proteins.
Tian C, Wang Q.
europepmc +2 more sources
Impact of protein prenylation inhibition on Mycobacterium leprae viability and IL-1β production in infected macrophages. [PDF]
Leprosy is a chronic infectious disease caused by Mycobacterium leprae and M. lepromatosis. Brazil consistently ranks among the countries with the highest number of leprosy cases. Data from our group showed that M.
da Silva Rocha M +11 more
europepmc +2 more sources
Uncovering protein prenylation in Th1 cells: novel prenylation sites and insights into statin and farnesyltransferase inhibition. [PDF]
Background T helper 1 (Th1) cell activation is an essential process for immune responses and is tightly regulated, including the prenylation of proteins critical for T cell function.
Koch J +9 more
europepmc +2 more sources
Dual-Ligand Strategy in Rh-Catalyzed Sequential Hydrofunctionalization of Valylene. [PDF]
Controlling regio‐ and chemo‐selectivity in transition‐metal‐catalyzed reactions involving coupling reagents with multiple reactive sites remains a significant challenge.
Mei YK, Xu SY, Wang ZH, Ji DW, Chen QA.
europepmc +2 more sources
Heavy metal-associated isoprenylated plant proteins (HIPPs) are a metallochaperone-like protein family comprising a combination of structural features unique to vascular plants.
Zoe Kathleen Barr +2 more
doaj +1 more source
Protein prenylation by farnesyltransferase (FTase) is often described as the targeting of a cysteine-containing motif (CaaX) that is enriched for aliphatic amino acids at the a1 and a2 positions, while quite flexible at the X position.
Brittany M Berger +6 more
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Specific Disruption of Ras2 CAAX Proteolysis Alters Its Localization and Function
Many CAAX proteins, such as Ras GTPase, undergo a series of posttranslational modifications at their carboxyl terminus (i.e., cysteine prenylation, endoproteolysis of AAX, and carboxylmethylation).
Rajani Ravishankar +6 more
doaj +1 more source
Chloroplastic prenylated proteins [PDF]
By in vivo [3H]mevalonate labelling of spinach combined with biochemical analysis, evidence is provided for the existence of protein prenylation in chloroplasts. Approximately 20 prenylated polypeptides were resolved by SDS‐PAGE followed by autoradiography.
Parmryd, Ingela +4 more
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Single prenyl-binding site on protein prenyl transferases [PDF]
Three distinct protein prenyl transferases, one protein farnesyl transferase (FTase) and two protein geranylgeranyl transferases (GGTase), catalyze prenylation of many cellular proteins. One group of protein substrates contains a C-terminal C AAX motif (C is Cys, A is aliphatic, and
L, Desnoyers, M C, Seabra
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Prenylated flavins: structures and mechanisms [PDF]
The UbiX/UbiD system is widespread in microbes and responsible for the reversible decarboxylation of unsaturated carboxylic acids. The UbiD enzyme catalyzes this unusual reaction using a prenylated flavin (prFMN) as cofactor, the latter formed by the flavin prenyltransferase UbiX.
Bloor, Samuel +3 more
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