Search Results - "Plechanovová, Anna"

Reaction Mechanism of Glutamate Carboxypeptidase II Revealed by Mutagenesis, X-ray Crystallography, and Computational Methods by Klusák, Vojtěch, Bařinka, Cyril, Plechanovová, Anna, Mlčochová, Petra, Konvalinka, Jan, Rulíšek, Lubomír, Lubkowski, Jacek

“…Glutamate carboxypeptidase II (GCPII, EC 3.4.17.21) is a zinc-dependent exopeptidase and an important therapeutic target for neurodegeneration and prostate…”
Get full text

Novel Substrate-Based Inhibitors of Human Glutamate Carboxypeptidase II with Enhanced Lipophilicity by Plechanovová, Anna, Byun, Youngjoo, Alquicer, Glenda, Škultétyová, L'ubica, Mlčochová, Petra, Němcová, Adriana, Kim, Hyung-Joon, Navrátil, Michal, Mease, Ronnie, Lubkowski, Jacek, Pomper, Martin, Konvalinka, Jan, Rulíšek, Lubomír, Bařinka, Cyril

“…Virtually all low molecular weight inhibitors of human glutamate carboxypeptidase II (GCPII) are highly polar compounds that have limited use in settings where…”
Get full text

Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis by Plechanovová, Anna, Jaffray, Ellis G., Tatham, Michael H., Naismith, James H., Hay, Ronald T.

“…Ubiquitin modification is mediated by a large family of specificity determining ubiquitin E3 ligases. To facilitate ubiquitin transfer, RING E3 ligases bind…”
Get full text

Functional 3D architecture in an intrinsically disordered E3 ligase domain facilitates ubiquitin transfer by Murphy, Paul, Xu, Yingqi, Rouse, Sarah L., Jaffray, Ellis G., Plechanovová, Anna, Matthews, Steve J., Carlos Penedo, J., Hay, Ronald T.

“…The human genome contains an estimated 600 ubiquitin E3 ligases, many of which are single-subunit E3s (ssE3s) that can bind to both substrate and…”
Get full text

Structural basis for the RING-catalyzed synthesis of K63-linked ubiquitin chains by Branigan, Emma, Plechanovová, Anna, Jaffray, Ellis G, Naismith, James H, Hay, Ronald T

“…Structural analyses capture RING E3 ligase RNF4 bound to Ube2V2–Ubc13 E2 complex charged with ubiquitin and, along with functional assays, reveal the basis for…”
Get full text

Mechanism of ubiquitylation by dimeric RING ligase RNF4 by Hay, Ronald T, Plechanovová, Anna, Jaffray, Ellis G, McMahon, Stephen A, Johnson, Kenneth A, Navrátilová, Iva, Naismith, James H

“…RNF4 is an E3 ligase involved in ubiquitinating poly-SUMOylated proteins. The structure of the RNF4 dimer, along with modeling and functional analyses, now…”
Get full text

RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation by Geoffroy, Marie-Claude, Hay, Ronald T, Hattersley, Neil, Jaffray, Ellis G, Palvimo, Jorma J, Shen, Linnan, Plechanovova, Anna, Tatham, Michael H

“…In acute promyelocytic leukaemia (APL), the promyelocytic leukaemia (PML) protein is fused to the retinoic acid receptor α (RAR). This disease can be treated…”
Get full text

Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4 by Xu, Yingqi, Plechanovová, Anna, Simpson, Peter, Marchant, Jan, Leidecker, Orsolya, Kraatz, Sebastian, Hay, Ronald T., Matthews, Steve J.

“…The small ubiquitin-like modifier (SUMO) can form polymeric chains that are important signals in cellular processes such as meiosis, genome maintenance and…”
Get full text

Ube2W conjugates ubiquitin to α-amino groups of protein N-termini by Tatham, Michael H, Plechanovová, Anna, Jaffray, Ellis G, Salmen, Helena, Hay, Ronald T

“…The covalent attachment of the protein ubiquitin to intracellular proteins by a process known as ubiquitylation regulates almost all major cellular systems,…”
Get more information

Purification and identification of endogenous polySUMO conjugates by Bruderer, Roland, Tatham, Michael H, Plechanovova, Anna, Matic, Ivan, Garg, Amit K, Hay, Ronald T

“…The small ubiquitin‐like modifier (SUMO) can undergo self‐modification to form polymeric chains that have been implicated in cellular processes such as…”
Get full text

SUMO Chain-Induced Dimerization Activates RNF4 by Rojas-Fernandez, Alejandro, Plechanovová, Anna, Hattersley, Neil, Jaffray, Ellis, Tatham, Michael H., Hay, Ronald T.

“…Dimeric RING E3 ligases interact with protein substrates and conformationally restrain the ubiquitin-E2-conjugating enzyme thioester complex such that it is…”
Get full text

Glycosylation Directs Targeting and Activation of Cystatin F from Intracellular and Extracellular Sources by Colbert, Jeff D, Plechanovová, Anna, Watts, Colin

“…Cystatin F is a cysteine protease inhibitor that is selectively expressed in immune cells and unlike other cystatin family members is targeted to a significant…”
Get full text

Structural Insight into the Pharmacophore Pocket of Human Glutamate Carboxypeptidase II by Bařinka, Cyril, Rovenská, Miroslava, Mlčochová, Petra, Hlouchová, Klára, Plechanovová, Anna, Majer, Pavel, Tsukamoto, Takashi, Slusher, Barbara S, Konvalinka, Jan, Lubkowski, Jacek

“…Inhibition of glutamate carboxypeptidase II (GCPII) has been shown to be neuroprotective in multiple preclinical models in which dysregulated glutamatergic…”
Get full text

Mapping of the active site of glutamate carboxypeptidase II by site-directed mutagenesis by Mlčochová, Petra, Plechanovová, Anna, Bařinka, Cyril, Mahadevan, Daruka, Saldanha, Jose W, Rulíšek, Lubomír, Konvalinka, Jan

“…Human glutamate carboxypeptidase II [GCPII (EC 3.4.17.21)] is recognized as a promising pharmacological target for the treatment and imaging of various…”
Get full text

Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis by Plechanovova, Anna, Jaffray, Ellis G, Tatham, Michael H, Naismith, James H, Hay, Ronald T

“…Ubiquitin modification is mediated by a large family of specificity determining ubiquitin E3 ligases. To facilitate ubiquitin transfer, RING E3 ligases bind…”
Get full text