J Rajan Prabu
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Explore the profile of J Rajan Prabu including associated specialties, affiliations and a list of published articles.
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23
Citations
630
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Recent Articles
1.
Horn-Ghetko D, Hopf L, Tripathi-Giesgen I, Du J, Kostrhon S, Vu D, et al.
Nat Struct Mol Biol
. 2024 Apr;
31(7):1083-1094.
PMID: 38605244
Ubiquitin ligation is typically executed by hallmark E3 catalytic domains. Two such domains, 'cullin-RING' and 'RBR', are individually found in several hundred human E3 ligases, and collaborate with E2 enzymes...
2.
Li J, Purser N, Liwocha J, Scott D, Byers H, Steigenberger B, et al.
Mol Cell
. 2024 Feb;
84(7):1304-1320.e16.
PMID: 38382526
Cullin-RING ligases (CRLs) ubiquitylate specific substrates selected from other cellular proteins. Substrate discrimination and ubiquitin transferase activity were thought to be strictly separated. Substrates are recognized by substrate receptors, such...
3.
Liwocha J, Li J, Purser N, Rattanasopa C, Maiwald S, Krist D, et al.
Nat Struct Mol Biol
. 2024 Feb;
31(2):378-389.
PMID: 38326650
E3 ubiquitin ligases, in collaboration with E2 ubiquitin-conjugating enzymes, modify proteins with poly-ubiquitin chains. Cullin-RING ligase (CRL) E3s use Cdc34/UBE2R-family E2s to build Lys48-linked poly-ubiquitin chains to control an enormous...
4.
Chrustowicz J, Sherpa D, Li J, Langlois C, Papadopoulou E, Vu D, et al.
Mol Cell
. 2023 Dec;
84(2):293-308.e14.
PMID: 38113892
Ubiquitylation is catalyzed by coordinated actions of E3 and E2 enzymes. Molecular principles governing many important E3-E2 partnerships remain unknown, including those for RING-family GID/CTLH E3 ubiquitin ligases and their...
5.
Wallace I, Baek K, Prabu J, Vollrath R, von Gronau S, Schulman B, et al.
Nat Commun
. 2023 Dec;
14(1):7970.
PMID: 38042859
The attachment of the ubiquitin-like protein ISG15 to substrates by specific E1-E2-E3 enzymes is a well-established signalling mechanism of the innate immune response. Here, we present a 3.45 Å cryo-EM...
6.
Hehl L, Horn-Ghetko D, Prabu J, Vollrath R, Vu D, Perez Berrocal D, et al.
Nat Chem Biol
. 2023 Aug;
20(2):190-200.
PMID: 37620400
Ubiquitin (Ub) chain formation by homologous to E6AP C-terminus (HECT)-family E3 ligases regulates vast biology, yet the structural mechanisms remain unknown. We used chemistry and cryo-electron microscopy (cryo-EM) to visualize...
7.
Chrustowicz J, Sherpa D, Teyra J, Loke M, Popowicz G, Basquin J, et al.
J Mol Biol
. 2021 Nov;
434(2):167347.
PMID: 34767800
N-degron E3 ubiquitin ligases recognize specific residues at the N-termini of substrates. Although molecular details of N-degron recognition are known for several E3 ligases, the range of N-terminal motifs that...
8.
Kostrhon S, Prabu J, Baek K, Horn-Ghetko D, von Gronau S, Klugel M, et al.
Nat Chem Biol
. 2021 Sep;
17(10):1075-1083.
PMID: 34518685
An emerging mechanism of ubiquitylation involves partnering of two distinct E3 ligases. In the best-characterized E3-E3 pathways, ARIH-family RING-between-RING (RBR) E3s ligate ubiquitin to substrates of neddylated cullin-RING E3s. The...
9.
Sherpa D, Chrustowicz J, Qiao S, Langlois C, Hehl L, Gottemukkala K, et al.
Mol Cell
. 2021 Apr;
81(11):2445-2459.e13.
PMID: 33905682
How are E3 ubiquitin ligases configured to match substrate quaternary structures? Here, by studying the yeast GID complex (mutation of which causes deficiency in glucose-induced degradation of gluconeogenic enzymes), we...
10.
Horn-Ghetko D, Krist D, Prabu J, Baek K, Mulder M, Klugel M, et al.
Nature
. 2021 Feb;
590(7847):671-676.
PMID: 33536622
E3 ligases are typically classified by hallmark domains such as RING and RBR, which are thought to specify unique catalytic mechanisms of ubiquitin transfer to recruited substrates. However, rather than...