Results 11 to 20 of about 32,326 (169)

Biochemistry of protein prenylation.

Journal of Lipid Research, 1992
Covalent modification by isoprenoid lipids (prenylation) is now recognized as a mechanism to promote membrane interactions and biological activities of a variety of cellular proteins. Both the 15-carbon farnesyl and 20-carbon geranylgeranyl isoprenoids are involved in these modifications, which occur on carboxyl-terminal cysteine residues of proteins ...
PJ Casey
doaj   +3 more sources

Increased core body temperature exacerbates defective protein prenylation in mouse models of mevalonate kinase deficiency [PDF]

The Journal of Clinical Investigation, 2022
Mevalonate kinase deficiency (MKD) is characterized by recurrent fevers and flares of systemic inflammation, caused by biallelic loss-of-function mutations in MVK.
Marcia A. Munoz, Oliver P. Skinner, Etienne Masle-Farquhar, Julie Jurczyluk, Ya Xiao, Emma K. Fletcher, Esther Kristianto, Mark P. Hodson, Seán I. O’Donoghue, Sandeep Kaur, Robert Brink, David G. Zahra, Elissa K. Deenick, Kristen A. Perry, Avril A.B. Robertson, Sam Mehr, Pravin Hissaria, Catharina M. Mulders-Manders, Anna Simon, Michael J. Rogers   +19 more
doaj   +2 more sources

The role of protein prenylation inhibition through targeting FPPS by zoledronic acid in the prevention of renal fibrosis in rats [PDF]

Scientific Reports
Renal fibrosis (RF) represents the most widespread pathological condition in chronic kidney disease (CKD). Recently, protein prenylation has been implicated in the fibrosis’s progression. The research examined the renoprotective effect of zoledronic acid
Reham Hussein Mohamed, Dina S. Abdelrahim, Nesma Hussein Abdel Hay, Nesma Mohamed Fawzy, Doaa Karem M. M., Dalia Ahmed Yousef Yehia, Omnia M. AbdelMaksoud, Yomna M. Tamim   +7 more
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Deciphering protein prenylation in endocytic trafficking in Toxoplasma gondii [PDF]

mBio
Toxoplasma gondii is a widespread intracellular protozoan pathogen infecting virtually all warm-blooded animals. This parasite acquires host-derived resources to support its replication inside a membrane-bound parasitophorous vacuole within infected host
Vern B. Carruthers, Zhicheng Dou
doaj   +2 more sources

Impact of protein prenylation inhibition on Mycobacterium leprae viability and IL-1β production in infected macrophages [PDF]

Journal of Bacteriology
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.
Matheus da Silva Rocha, Antônio Marcos Rodrigues Pereira, Plínio Marcos Freire dos Santos, André Alves Dias, Melissa Pontes Pereira, Patrícia Sammarco Rosa, Daniele F. F. Bertoluci, John T. Belisle, Fabricio da Mota Ramalho Costa, Cristiana Santos de Macedo, Maria Cristina Vidal Pessolani, Marcia Berrêdo-Pinho   +11 more
doaj   +2 more sources

Dual chemical probes enable quantitative system-wide analysis of protein prenylation and prenylation dynamics. [PDF]

Nat Chem, 2019
Post-translational farnesylation or geranylgeranylation at a C-terminal cysteine residue regulates the localization and function of over 100 proteins, including the Ras isoforms, and is a therapeutic target in diseases including cancer and infection. Here, we report global and selective profiling of prenylated proteins in living cells enabled by the ...
Storck EM, Morales-Sanfrutos J, Serwa RA, Panyain N, Lanyon-Hogg T, Tolmachova T, Ventimiglia LN, Martin-Serrano J, Seabra MC, Wojciak-Stothard B, Tate EW.   +10 more
europepmc   +6 more sources

Case Report: Clinical application of an in vitro prenylation assay in the diagnosis of an early-onset case of mevalonate kinase deficiency harbouring a novel MVK variant [PDF]

Frontiers in Pediatrics
Mevalonate kinase deficiency (MKD) is a systemic autoinflammatory disease caused by biallelic mutations in MVK. Individuals with MKD present with a recurrent fever syndrome, often including a skin rash, gastrointestinal symptoms and lymphadenopathy.
Alice Burleigh, Ovgu Kul Cinar, Paul Torpiano, Marcia A. Munoz, Marcia A. Munoz, Charlotte Abell-King, Charlotte Abell-King, Michael J. Rogers, Michael J. Rogers, Despina Eleftheriou, Despina Eleftheriou, Paul A. Brogan, Paul A. Brogan   +12 more
doaj   +2 more sources

Targeting protein prenylation for cancer therapy. [PDF]

Nat Rev Cancer, 2011
Protein farnesylation and geranylgeranylation, together referred to as prenylation, are lipid post-translational modifications that are required for the transforming activity of many oncogenic proteins, including some RAS family members. This observation prompted the development of inhibitors of farnesyltransferase (FT) and geranylgeranyl-transferase 1
Berndt N, Hamilton AD, Sebti SM.
europepmc   +4 more sources

Chloroplastic prenylated proteins [PDF]

FEBS 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, Shipton, Catherine Ann, Swiezewska, Ewa, Dallner, Gustav, Andersson, Bertil   +4 more
openaire   +2 more sources

Regulation of protein prenylation

Biomedicine & Pharmacotherapy, 2023
Prenyltransferases (PTases) are known to play a role in embryonic development, normal tissue homeostasis and cancer by posttranslationally modifying proteins involved in these processes. They are being discussed as potential drug targets in an increasing number of diseases, ranging from Alzheimer's disease to malaria.
Dominik Jung, Hagen S. Bachmann
openaire   +2 more sources