Nucleation - OmicsDI

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UNIPROT ID/AC

P37840 (1)
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CHEBI ID

CHEBI:60425 (2)
CHEBI:46905 (2)
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Metabolite Name

L-isoleucine (2)
L-glutamic acid (2)
L-cysteinylglycine (1)
N6-acetyl-L-lysine (1)
1-heptadecanoyl-2,3-dioleoyl-sn-glycerol (1)
1-oleoyl-2-linoleoyl-sn-glycero-3-phosphoethanolamine zwitterion (1)
1,2-di-[(9E)-octadecenoyl]-sn-glycero-3-phosphoethanolamine (1)
Tristearoylglycerol (1)
1-(9Z)-hexadecenoyl-2-(13Z,16Z)-docosadienoyl-sn-glycero-3-phosphocholine (1)
Lysophosphatidylethanolamine (18:2/0:0) (1)
1-icosanoyl-sn-glycero-3-phosphoethanolamine (1)
1-octadecanoyl-2,3-dioleoyl-sn-glycerol (1)
Tripalmitin (1)
1-hexadecanoyl-2-(4E,7E,10E,13E,16E,19E-docosahexaenoyl)-sn-glycero-3-phosphocholine (1)
1,2-dioleoyl-3-[(11Z)-icosenoyl]-sn-glycerol (1)
TG(18:1(9Z)/18:1(11Z)/18:2(9Z,12Z))[iso6] (1)
TG(18:2(9Z,12Z)/18:2(9Z,12Z)/20:2(11Z,14Z))[iso3] (1)
1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho-(1'-sn-glycerol)(1-) (1)
N-heptadecanoylsphingosine-1-phosphocholine (1)
1-oleoyl-2,3-di-linoleoyl-sn-glycerol (1)
1,2,3-trilinoleoylglycerol (1)
1-tetradecanoyl-2-[(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl]-sn-glycero-3-phosphocholine (1)
TG(16:0/16:0/18:1(11Z))[iso3] (1)
1-[(9Z)-octadecenoyl]-2-[(6Z,9Z)-octadecadienoyl]-sn-glycero-3-phosphocholine (1)
1,2-di-[(9Z,12Z)-octadecadienoyl]-sn-glycero-3-phosphocholine (1)
1-tetradecanoyl-2,3-dihexadecanoyl-sn-glycerol (1)
1-palmitoyl-2-octadecadienoyl-sn-glycero-3-phosphocholine (1)
1,2-dioleoyl-sn-glycero-3-phospho-(1'-sn-glycerol) (1)
1-[(9Z,12Z)-octadecadienoyl]-2-octadecanoyl-sn-glycero-3-phosphocholine (1)
TG(16:1(9Z)/16:1(9Z)/18:1(9Z))[iso3] (1)

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Modelling Approach

Ordinary differential equation model (7)

Lab affiliation

University of Padova (2)
ESPCI Paris, Université PSL, UAR2051 CNRS, 75005, Paris, France (2)
MRC - Laboratory of Molecular Biology (2)
Utrecht University (2)
School of Basic Medical Science, Central South University (1)
1Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh 2Chair of Bioanalytics, Institute of Biotechnology, Technische Universität Berlin, Berlin, 13355, Germany (1)
Group Leader Department Cell and Developmental Biology John Innes Centre Norwich, UK (1)
Institute of Physiological Chemistry, Medical Faculty of TU Dresden, Fiedlerstrasse 42 01307 Dresden, Germany (1)
Laboratory of Systems Biology and Genetics, Institute of Bioengineering, School of Life Sciences, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland (1)
Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz, Im Neuenheimer Feld 282, 69120 Heidelberg, Germany (1)
Max Perutz Labs Vienna, Department of Biochemistry and Cell Biology, University of Vienna, Vienna BioCenter, Austria (1)
Department of Nanophysiology Technische Universität Kaiserslautern Paul-Ehrlich-Strasse 23 (Room 151) 67663 Kaiserslautern, Germany (1)
Department of Genetics and Developmental Biology, The Rappaport Faculty of Medicine and Research Institute, Technion – Israel Institute of Technology, Haifa 31096, Israel (1)
Massachusetts General Hospital Center for Cancer Research and Department of Medicine Harvard Medical School Charlestown, MA, 02129, USA (1)
Max Perutz Labs, Department of Biochemistry and Cell Biology, University of Vienna, Vienna BioCenter, Austria (1)
Max Planck Institute for Infection Biology, Berlin, Germany (1)
Core Facility for Mass Spectrometry & Proteomics Center for Molecular Biology of Heidelberg University (ZMBH 69120 Heidelberg (1)
Department of Parasitology, Faculty of Science, Charles University, BIOCEV, Prague, Czech Republic (1)
Institute of Physiology II, Universität Freiburg, Germany (1)
Department for Molecular and Applied Microbiology, Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute Jena, Leibniz-HKI (1)
Zentrum für Molekulare Biologie (ZMBH) Universität Heidelberg Germany (1)
School of Chemistry, Raymond & Beverly Sackler Faculty of Exact Sciences and Center for Physics and Chemistry of Living Systems, Tel Aviv University, Tel Aviv, Israel (1)
MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK. (1)
Department of Genetics and Developmental Biology, The Rappaport Faculty of Medicine and Research Institute, Technion – Israel Institute of Technology (1)
Facility Head, Discovery Proteomics Facility University of Oxford (1)
Associate Professor Department of Microbiology and Immunology The G.W. Hooper Research Foundation The University of California, at San Francisco 513 Parnassus Ave, HSW 1532, Box 0552 San Francisco, CA 94143 (1)
scientist F Rajiv Gandhi Centre for Biotechnology (1)
Oncode Institute, Hubrecht Institute, Royal Netherlands Academy of Arts and Sciences (KNAW) and University Medical Center Utrecht, the Netherland Department of Bionanoscience, Kavli Institute of Nanoscience Delft, Technische Universiteit Delft, Van der Maasweg 9, 2629 HZ Delft, the Netherlands. (1)
Research Group Bioanalytical Mass Spectrometry, Max Planck Institute for Multidisciplinary Sciences, Germany; Bioanalytics, Department of Clinical Chemistry, University Medical Center Goettingen, Germany (1)
Department of Chemistry, Department of Biology (by courtesy), Thomas C.Jenkins Department of Biophysics (by courtesy), Johns Hopkins University (1)

IsPrivate

False (7)

Model Flag

Sbml Extended (1)

Classification

protozoa (4)
fungi (2)
bacteria (1)

Study type

ChIP-seq (14)
Transcription profiling by array (13)
RNA-seq of coding RNA (5)
ChIP-chip by tiling array (3)
CLIP-Seq (2)
Comparative genomic hybridization by array (2)
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Other (1)
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Ice nucleation of lichen and fungi from Hyytiälä.

PRJEB44236 | ENA

Nucleation and spreading rejuvenate polycomb domains every cell cycle

PRJNA862526 | ENA

A genome-wide analysis reveals that the Drosophila transcription factor, Lola, promotes axon growth in part by suppressing expression of the actin nucleation factor, Spire

This SuperSeries is composed of the following subset Series: GSE34121: A genome-wide analysis reveals that the Drosophila transcription factor, Lola, promotes axon growth in part by suppressing expression of the actin nucleation factor, Spire (allele lola_ORE76) GSE34122: A genome-wide analysis reve...

ORGANISM(S): Drosophila melanogaster

2011-12-03 | E-GEOD-34123 | biostudies-arrayexpress

CAMSAP-driven microtubule release from γ-TuRC and its regulation by nucleation-promoting factors

γ-tubulin ring complex (γ-TuRC) is the major microtubule-nucleating factor. After nucleation, microtubules can be released from γ-TuRC and stabilized by other proteins, such as CAMSAPs, but the biochemical cross-talk between minus-end regulation pathways is poorly understood. Here, we reconstituted ...

ORGANISM(S): Homo sapiens (Human)

2024-01-30 | PXD048637 | Pride