Walter K Schmidt
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Explore the profile of Walter K Schmidt including associated specialties, affiliations and a list of published articles.
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37
Citations
643
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Recent Articles
1.
Sarkar A, Hildebrandt E, Patel K, Mai E, Shah S, Kim J, et al.
G3 (Bethesda)
. 2024 Jun;
14(8).
PMID: 38839053
Many proteins undergo a post-translational lipid attachment, which increases their hydrophobicity, thus strengthening their membrane association properties or aiding in protein interactions. Geranylgeranyltransferase-I (GGTase-I) is an enzyme involved in a...
2.
Hildebrandt E, Sarkar A, Ravishankar R, Kim J, Schmidt W
Dis Model Mech
. 2024 May;
17(5).
PMID: 38818856
Prenylated proteins are prevalent in eukaryotic biology (∼1-2% of proteins) and are associated with human disease, including cancer, premature aging and infections. Prenylated proteins with a C-terminal CaaX sequence are...
3.
Schey G, Hildebrandt E, Wang Y, Diwan S, Passetti H, Potts G, et al.
Int J Mol Sci
. 2024 May;
25(10).
PMID: 38791363
Protein farnesylation is a post-translational modification where a 15-carbon farnesyl isoprenoid is appended to the C-terminal end of a protein by farnesyltransferase (FTase). This process often causes proteins to associate...
4.
Hildebrandt E, Hussain S, Sieburg M, Ravishankar R, Asad N, Gore S, et al.
Bioorg Chem
. 2024 Apr;
147:107316.
PMID: 38583246
Ras GTPases and other CaaX proteins undergo multiple post-translational modifications at their carboxyl-terminus. These events initiate with prenylation of a cysteine and are followed by endoproteolytic removal of the 'aaX'...
5.
Sarkar A, Hildebrandt E, Patel K, Mai E, Shah S, Kim J, et al.
bioRxiv
. 2024 Mar;
PMID: 38496651
Many proteins undergo a post-translational lipid attachment, which increases their hydrophobicity, thus strengthening their membrane association properties or aiding in protein interactions. Geranylgeranyltransferase-I (GGTase-I) is an enzyme involved in a...
6.
Hildebrandt E, Sarkar A, Ravishankar R, Kim J, Schmidt W
bioRxiv
. 2023 Oct;
PMID: 37786692
The C-terminal CaaX sequence (cysteine-aliphatic-aliphatic-any of several amino acids) is subject to isoprenylation on the conserved cysteine and is estimated to occur in 1-2% of proteins within yeast and human...
7.
Kim J, Hildebrandt E, Sarkar A, Yeung W, Waldon L, Kannan N, et al.
G3 (Bethesda)
. 2023 Apr;
13(7).
PMID: 37119806
The current understanding of farnesyltransferase (FTase) specificity was pioneered through investigations of reporters like Ras and Ras-related proteins that possess a C-terminal CaaX motif that consists of 4 amino acid...
8.
Ravishankar R, Hildebrandt E, Greenway G, Asad N, Gore S, Dore T, et al.
Microbiol Spectr
. 2023 Jan;
11(1):e0269222.
PMID: 36602340
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). Some CAAX proteins, however, undergo...
9.
Berger B, Yeung W, Goyal A, Zhou Z, Hildebrandt E, Kannan N, et al.
PLoS One
. 2022 Jun;
17(6):e0270128.
PMID: 35749383
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...
10.
Schey G, Buttery P, Hildebrandt E, Novak S, Schmidt W, Hougland J, et al.
Int J Mol Sci
. 2021 Nov;
22(21).
PMID: 34769472
Protein farnesylation is a post-translational modification where a 15-carbon farnesyl isoprenoid is appended to the C-terminal end of a protein by farnesyltransferase (FTase). This modification typically causes proteins to associate...