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Protein ubiquitylation is essential for the schizont to merozoite transition in Plasmodium falciparum blood-stage development

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/0471250953.bi1315s35openalex-snapshot

Biological Sequence Motif Discovery Using motif‐x

inferredcites →https://doi.org/10.1002/pmic.201400508openalex-snapshot

Extensive differential protein phosphorylation as intraerythrocytic Plasmodium falciparum schizonts develop into extracellular invasive merozoites

inferredcites →https://doi.org/10.1016/0166-6851(84)90090-2openalex-snapshot

Time-course of synthesis, transport and incorporation of a protein identified in purified membranes of host erythrocytes infected with a knob-forming strain of Plasmodium falciparum

inferredcites →https://doi.org/10.1016/0166-6851(88)90152-1openalex-snapshot

MESA is a Plasmodium falciparum phosphoprotein associated with the erythrocyte membrane skeleton

inferredcites →https://doi.org/10.1016/0166-6851(93)90007-kopenalex-snapshot

Cloning and characterization of a Plasmodium falciparum gene encoding a novel high-molecular weight host membrane-associated protein, PfEMP3

inferredcites →https://doi.org/10.1016/j.cell.2008.04.051openalex-snapshot

Exported Proteins Required for Virulence and Rigidity of Plasmodium falciparum-Infected Human Erythrocytes

inferredcites →https://doi.org/10.1016/j.celrep.2016.04.047openalex-snapshot

Multiomic Analysis of the UV-Induced DNA Damage Response

inferredcites →https://doi.org/10.1016/j.chembiol.2019.03.015openalex-snapshot

Structure-Guided Identification of Resistance Breaking Antimalarial N‑Myristoyltransferase Inhibitors

inferredcites →https://doi.org/10.1016/j.chom.2012.09.010openalex-snapshot

Uncovering Common Principles in Protein Export of Malaria Parasites

inferredcites →https://doi.org/10.1016/j.chom.2015.10.014openalex-snapshot

The Ubiquitin Proteome of Toxoplasma gondii Reveals Roles for Protein Ubiquitination in Cell-Cycle Transitions

inferredcites →https://doi.org/10.1016/j.coph.2018.06.003openalex-snapshot

Mechanisms of artemisinin resistance in Plasmodium falciparum malaria

inferredcites →https://doi.org/10.1016/j.ijpddr.2011.12.001openalex-snapshot

The proteasome of malaria parasites: A multi-stage drug target for chemotherapeutic intervention?

inferredcites →https://doi.org/10.1016/j.jprot.2016.03.004openalex-snapshot

New insights into host-parasite ubiquitin proteome dynamics in P. falciparum infected red blood cells using a TUBEs-MS approach

inferredcites →https://doi.org/10.1016/j.molbiopara.2004.03.013openalex-snapshot

A novel Plasmodium falciparum ring stage protein, REX, is located in Maurer’s clefts

inferredcites →https://doi.org/10.1016/j.molcel.2009.12.024openalex-snapshot

Substrate-Assisted Inhibition of Ubiquitin-like Protein-Activating Enzymes: The NEDD8 E1 Inhibitor MLN4924 Forms a NEDD8-AMP Mimetic In Situ

inferredcites →https://doi.org/10.1016/j.molcel.2011.08.025openalex-snapshot

Systematic and Quantitative Assessment of the Ubiquitin-Modified Proteome

inferredcites →https://doi.org/10.1016/j.pt.2006.04.008openalex-snapshot

Progress in in silico functional genomics: the malaria Metabolic Pathways database

inferredcites →https://doi.org/10.1016/j.pt.2016.05.010openalex-snapshot

Artemisinin Action and Resistance in Plasmodium falciparum

inferredcites →https://doi.org/10.1016/j.pt.2017.05.009openalex-snapshot

Protein Degradation Systems as Antimalarial Therapeutic Targets

inferredcites →https://doi.org/10.1016/j.str.2017.05.001openalex-snapshot

Dissecting the Specificity of Adenosyl Sulfamate Inhibitors Targeting the Ubiquitin-Activating Enzyme

inferredcites →https://doi.org/10.1016/s0091-679x(08)61853-1openalex-snapshot

Chapter 11: Purification of Plasmodium falciparum Merozoites for Analysis of the Processing of Merozoite Surface Protein-1

inferredcites →https://doi.org/10.1016/s0166-6851(99)00174-7openalex-snapshot

Intraerythrocytic polyubiquitin expression in Plasmodium falciparum is subjected to developmental and heat-hock control☆

inferredcites →https://doi.org/10.1016/s0378-1119(01)00776-4openalex-snapshot

Deciphering apicoplast targeting signals – feature extraction from nuclear-encoded precursors of Plasmodium falciparum apicoplast proteins

inferredcites →https://doi.org/10.1017/s003118200500747xopenalex-snapshot

The proteasome inhibitor MLN-273 blocks exoerythrocytic and erythrocytic development of Plasmodium parasites

inferredcites →https://doi.org/10.1017/s0031182096008621openalex-snapshot

The histones of Plasmodium falciparum: identification, purification and a possible role in the pathology of malaria

inferredcites →https://doi.org/10.1021/acs.jmedchem.8b01161openalex-snapshot

Target Validation and Identification of Novel Boronate Inhibitors of the Plasmodium falciparum Proteasome

inferredcites →https://doi.org/10.1021/acs.jproteome.6b00366openalex-snapshot

Dynamic and Combinatorial Landscape of Histone Modifications during the Intraerythrocytic Developmental Cycle of the Malaria Parasite

inferredcites →https://doi.org/10.1021/acs.jproteome.7b00025openalex-snapshot

Quantitative Analysis of Human Red Blood Cell Proteome

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Andromeda: A Peptide Search Engine Integrated into the MaxQuant Environment

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The Plasmodium falciparum Schizont Phosphoproteome Reveals Extensive Phosphatidylinositol and cAMP-Protein Kinase A Signaling

inferredcites →https://doi.org/10.1021/pr5009724openalex-snapshot

Comprehensive Profiling of the Rice Ubiquitome Reveals the Significance of Lysine Ubiquitination in Young Leaves

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Global Histone Analysis by Mass Spectrometry Reveals a High Content of Acetylated Lysine Residues in the Malaria Parasite Plasmodium falciparum

inferredcites →https://doi.org/10.1038/embor.2012.105openalex-snapshot

LUBAC synthesizes linear ubiquitin chains via a thioester intermediate

inferredcites →https://doi.org/10.1038/nature14412openalex-snapshot

A molecular mechanism of artemisinin resistance in Plasmodium falciparum malaria

inferredcites →https://doi.org/10.1038/nature16936openalex-snapshot

Structure- and function-based design of Plasmodium-selective proteasome inhibitors

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Flexible guide-RNA design for CRISPR applications using Protospacer Workbench

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A small-molecule inhibitor of the ubiquitin activating enzyme for cancer treatment

inferredcites →https://doi.org/10.1038/nprot.2009.36openalex-snapshot

A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics

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Protein neddylation: beyond cullin–RING ligases

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Preclinical evaluation of the selective small-molecule UBA1 inhibitor, TAK-243, in acute myeloid leukemia

inferredcites →https://doi.org/10.1038/s41467-018-06221-1openalex-snapshot

Artemisinin kills malaria parasites by damaging proteins and inhibiting the proteasome

inferredcites →https://doi.org/10.1038/s41598-017-03984-3openalex-snapshot

Generating conditional gene knockouts in Plasmodium – a toolkit to produce stable DiCre recombinase-expressing parasite lines using CRISPR/Cas9

inferredcites →https://doi.org/10.1038/s41598-017-15781-zopenalex-snapshot

Photosensitized INA-Labelled protein 1 (PhIL1) is novel component of the inner membrane complex and is required for Plasmodium parasite development

inferredcites →https://doi.org/10.1038/srep21800openalex-snapshot

A versatile strategy for rapid conditional genome engineering using loxP sites in a small synthetic intron in Plasmodium falciparum

inferredcites →https://doi.org/10.1039/c3mb70506dopenalex-snapshot

The ubiquitin system: an essential component to unlocking the secrets of malaria parasite biology

inferredcites →https://doi.org/10.1074/jbc.m109.072405openalex-snapshot

Characterization and Structural Studies of the Plasmodium falciparum Ubiquitin and Nedd8 Hydrolase UCHL3

inferredcites →https://doi.org/10.1074/jbc.m111.238790openalex-snapshot

Unraveling the Ubiquitome of the Human Malaria Parasite

inferredcites →https://doi.org/10.1074/jbc.m111.279984openalex-snapshot

Mechanistic Studies of Substrate-assisted Inhibition of Ubiquitin-activating Enzyme by Adenosine Sulfamate Analogues

inferredcites →https://doi.org/10.1074/jbc.m117.802769openalex-snapshot

Compositional and expression analyses of the glideosome during the Plasmodium life cycle reveal an additional myosin light chain required for maximum motility

inferredcites →https://doi.org/10.1093/bioinformatics/btn250openalex-snapshot

Ontologizer 2.0—a multifunctional tool for GO term enrichment analysis and data exploration

inferredcites →https://doi.org/10.1093/nar/gky1106openalex-snapshot

The PRIDE database and related tools and resources in 2019: improving support for quantification data

inferredcites →https://doi.org/10.1096/fj.14-256057openalex-snapshot

A Plasmodium falciparum PHIST protein binds the virulence factor PfEMP1 and comigrates to knobs on the host cell surface

inferredcites →https://doi.org/10.1107/s0021889892009944openalex-snapshot

PROCHECK: a program to check the stereochemical quality of protein structures

inferredcites →https://doi.org/10.1107/s1399004714002910openalex-snapshot

Structure of the ubiquitin-activating enzyme loaded with two ubiquitin molecules

inferredcites →https://doi.org/10.1111/mmi.12193openalex-snapshot

Novel P lasmodium falciparum M aurer's clefts protein families implicated in the release of infectious merozoites

inferredcites →https://doi.org/10.1111/mmi.12206openalex-snapshot

Robust inducible Cre recombinase activity in the human malaria parasite P lasmodium falciparum enables efficient gene deletion within a single asexual erythrocytic growth cycle

inferredcites →https://doi.org/10.1126/science.1102452openalex-snapshot

Targeting Malaria Virulence and Remodeling Proteins to the Host Erythrocyte

inferredcites →https://doi.org/10.1126/science.1102737openalex-snapshot

A Host-Targeting Signal in Virulence Proteins Reveals a Secretome in Malarial Infection

inferredcites →https://doi.org/10.1128/aac.01748-15openalex-snapshot

Imidazopyridazine Inhibitors of Plasmodium falciparum Calcium-Dependent Protein Kinase 1 Also Target Cyclic GMP-Dependent Protein Kinase and Heat Shock Protein 90 To Kill the Parasite at Different Stages of Intracellular Development

inferredcites →https://doi.org/10.1128/ec.00083-09openalex-snapshot

An Unusual ERAD-Like Complex Is Targeted to the Apicoplast ofPlasmodium falciparum

inferredcites →https://doi.org/10.1128/iai.70.10.5779-5789.2002openalex-snapshot

Variation in the Expression of a Plasmodium falciparum Protein Family Implicated in Erythrocyte Invasion

inferredcites →https://doi.org/10.1182/blood-2017-11-814665openalex-snapshot

Remodeling of the malaria parasite and host human red cell by vesicle amplification that induces artemisinin resistance

inferredcites →https://doi.org/10.1186/1475-2875-12-160openalex-snapshot

A member of the Plasmodium falciparum PHIST family binds to the erythrocyte cytoskeleton component band 4.1

inferredcites →https://doi.org/10.1186/gb-2006-7-2-r12openalex-snapshot

Lineage-specific expansion of proteins exported to erythrocytes in malaria parasites

inferredcites →https://doi.org/10.1186/s12936-015-0708-1openalex-snapshot

Development of two novel high-throughput assays to quantify ubiquitylated proteins in cell lysates: application to screening of new anti-malarials

inferredcites →https://doi.org/10.1186/s12936-016-1675-xopenalex-snapshot

New developments in anti-malarial target candidate and product profiles

inferredcites →https://doi.org/10.1186/s40360-017-0147-4openalex-snapshot

Inhibitors of ubiquitin E3 ligase as potential new antimalarial drug leads

inferredcites →https://doi.org/10.1242/jcs.178830openalex-snapshot

Haemoglobin degradation underpins the sensitivity of early ring stage Plasmodium falciparum to artemisinins

inferredcites →https://doi.org/10.1371/journal.pbio.1002132openalex-snapshot

Targeting the Cell Stress Response of Plasmodium falciparum to Overcome Artemisinin Resistance

inferredcites →https://doi.org/10.1371/journal.pbio.2005895openalex-snapshot

Integrative proteomics and bioinformatic prediction enable a high-confidence apicoplast proteome in malaria parasites

inferredcites →https://doi.org/10.1371/journal.pgen.1004382openalex-snapshot

A HECT Ubiquitin-Protein Ligase as a Novel Candidate Gene for Altered Quinine and Quinidine Responses in Plasmodium falciparum

inferredcites →https://doi.org/10.1371/journal.pone.0002386openalex-snapshot

Deciphering the Ubiquitin-Mediated Pathway in Apicomplexan Parasites: A Potential Strategy to Interfere with Parasite Virulence

inferredcites →https://doi.org/10.1371/journal.pone.0013984openalex-snapshot

Enrichment Map: A Network-Based Method for Gene-Set Enrichment Visualization and Interpretation

inferredcites →https://doi.org/10.1371/journal.ppat.1003426openalex-snapshot

An Apicoplast Localized Ubiquitylation System Is Required for the Import of Nuclear-encoded Plastid Proteins

inferredcites →https://doi.org/10.1371/journal.ppat.1003546openalex-snapshot

Identification of New PNEPs Indicates a Substantial Non-PEXEL Exportome and Underpins Common Features in Plasmodium falciparum Protein Export

inferredcites →https://doi.org/10.1371/journal.ppat.1007722openalex-snapshot

Covalent Plasmodium falciparum-selective proteasome inhibitors exhibit a low propensity for generating resistance in vitro and synergize with multiple antimalarial agents

inferredcites →https://doi.org/10.15252/embr.201642641openalex-snapshot

Molecular insights into RBR E3 ligase ubiquitin transfer mechanisms

inferredcites →https://doi.org/10.2307/3280287openalex-snapshot

Synchronization of Plasmodium falciparum Erythrocytic Stages in Culture

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1016/j.jprot.2021.104279openalex-snapshot

The main post-translational modifications and related regulatory pathways in the malaria parasite Plasmodium falciparum: An update

inferred← citeshttps://doi.org/10.1101/576116openalex-snapshot

Publicly available transcriptomes provide the opportunity for dual RNA-Seq meta-analysis in Plasmodium infection

inferred← citeshttps://doi.org/10.1128/msystems.00182-21openalex-snapshot

Dual RNA Sequencing Meta-analysis in Plasmodium Infection Identifies Host-Parasite Interactions

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