Results 1 to 10 of about 43,549 (203)

Protein Prenylation in Plants: Mechanisms and Functional Implications. [PDF]

open access: yesPlants (Basel)
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]

open access: yesJ Bacteriol
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]

open access: yesBMC Biol
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]

open access: yesAdv Sci (Weinh)
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) at Plasmodesmata: Exploring the Link between Localization and Function

open access: yesPlants, 2023
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

Functional classification and validation of yeast prenylation motifs using machine learning and genetic reporters.

open access: yesPLoS ONE, 2022
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
doaj   +1 more source

Specific Disruption of Ras2 CAAX Proteolysis Alters Its Localization and Function

open access: yesMicrobiology Spectrum, 2023
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]

open access: yesFEBS Letters, 1997
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
openaire   +2 more sources

Single prenyl-binding site on protein prenyl transferases [PDF]

open access: yesProceedings of the National Academy of Sciences, 1998
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
openaire   +2 more sources

Prenylated flavins: structures and mechanisms [PDF]

open access: yesThe FEBS Journal, 2022
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
openaire   +3 more sources

Home - About - Disclaimer - Privacy