Biological adhesive

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Unknown (824)
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Organisms

Andropogon gerardi (41)
Bacteria (41)
Canis lupus familiaris (41)
Chromatiales bacterium OalgGamma1 (41)
Clavibacter nebraskensis NCPPB 2581 (41)
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Organisms

Homo sapiens (14)
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Orbilia oligospora ATCC 24927 (1)
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Orbilia oligospora (1)
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Repository

biostudies-arrayexpress (83)
pride (41)
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Tissue

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Feces (1)
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Pedal muscle (1)
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Permanent cell line cell (1)
Platelet (1)
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Secretion (1)
Skin epithelium (1)
Sublingual gland (1)
Submandibular gland (1)
Synovium (1)
Tissues (1)

Disease

Chronic lymphocytic leukemia (3)
Cervix carcinoma (2)
Disease free (2)
Chronic infection with geohelminth ascaris lumbricoides (1)
Non-diabetic (1)
Invasive ductal carcinoma (1)
Colon cancer (1)
Crohn's disease (1)
Idiopathic pulmonary fibrosis (1)
Neck carcinoma (1)
Rheumatoid arthritis (1)

Technology Type

Mass Spectrometry (41)
Shotgun proteomics (25)
Bottom-up proteomics (7)
Mass spectrometry (4)
Gel-based experiment (4)
Data-independent acquisition (3)
Affinity purification coupled with mass spectrometry proteomics (2)
Data-dependent acquisition (2)
Top-down proteomics (2)
Mass spectrometry assay (1)
All-ion fragmentation (1)
DiaPASEF (1)
Immunopeptidomics (1)
MSE (1)
SWATH MS (1)

Instrument Platform

Illumina NovaSeq 6000 (2)
Illumina HiSeq 2000 (1)
Illumina HiSeq 4000 (1)
Easy n-LC and LTQ Orbitrap XL mass spectrometers (both from Thermo Fisher, San Jose, CA, USA) (1)
Nano-electrospray source, were used for nano LC-MS/MS (1)
Orbitrap Fusion Lumos (1)
TripleTOF 6600 (1)
MALDI MS (Imaging MS) (1)
LMJ-SSP/ESI MS (Imaging MS) (1)
Quattro micro API (Waters) (1)
Agilent 5975E GC/MSD (Agilent) (1)
API 4000 QTRAP (AB Sciex) (1)
Liquid Chromatography MS - negative (1)
Liquid Chromatography MS - positive - reverse-phase (1)
Liquid Chromatography MS - positive - reverse phase (1)

Publication Date

2013 (14)
2010 (14)
2023 (12)
2019 (10)
2015 (10)
2014 (10)
2025 (9)
2016 (8)
2011 (7)
2009 (7)
2024 (6)
2012 (6)
2021 (5)
2017 (5)
2022 (4)
2020 (4)
2008 (4)
2026 (3)
2018 (3)
2006 (2)
2007 (1)
2004 (1)
2003 (1)

CHEBI ID

CHEBI:17436 (2)
CHEBI:17256 (2)
CHEBI:17521 (2)
CHEBI:16356 (2)
CHEBI:16192 (2)
CHEBI:12962 (2)
CHEBI:18261 (2)
CHEBI:16811 (2)
CHEBI:15676 (2)
CHEBI:16742 (2)
CHEBI:27470 (2)
CHEBI:16349 (2)
CHEBI:16119 (2)
CHEBI:28044 (2)
CHEBI:17497 (2)
CHEBI:17242 (2)
CHEBI:16704 (2)
CHEBI:17621 (2)
CHEBI:6650 (2)
CHEBI:16856 (2)
CHEBI:17713 (2)
CHEBI:17172 (2)
CHEBI:16695 (2)
CHEBI:15741 (2)
CHEBI:44897 (2)
CHEBI:17553 (2)
CHEBI:15729 (2)
CHEBI:16750 (2)
CHEBI:17858 (2)
CHEBI:15428 (2)

Metabolite Name

4.Phaeophorbide a M+H (1)
2-(6-Chlorobenzoxazole-2-yl)-3-[2-[2-(acetylamino)-4-(dipropylamino)phenylazo]-4-(4-methylpiperazino)-5-thiazolyl]acrylonitrile (1)
2,5-Dimethylpyrimidin-4-amine (1)
(31R)-9,45-Seco-10-demercapto-9,10-didehydro-2-decarboxy-2-hydroxy-31-methyl-39-noracanthifolicin (1)
Cyclo[N(Me)Ala-D-N(Me)Phe-D-aIle-D-Val-Val-N(Me)Val-Leu] (1)
4-Quinazolone (1)
4-(1,2,4a,5-tetramethyl-7-oxo-1,2,3,4,4a,7,8,8a-octahydronaphthalen-1-yl)-2-methylidenebutanal (1)
Spectral Match to PAF C-16 from NIST14 M+H (1)
N-formyl-Val-Thr-Leu-Val-Pip-Leu-Pip (1)
4-[(1S,4S)-4-(3,4-dichlorophenyl)-1,2,3,4-tetrahydronaphthalen-1-yl]morpholine (1)
Spectral Match to 1-Hexadecanoyl-sn-glycerol from NIST14 M+H (1)
MGMG 16:0 (1)
1-(9Z-nonadecenoyl)-glycero-3-phosphocholine M+H (1)
Naftalina (1)
Spectral Match to 1-Palmitoyl-2-hydroxy-sn-glycero-3-phosphoethanolamine from NIST14 M+H (1)
PE(16:0/0:0); [M+H]+ C21H45N1O7P1 M+H (1)
Spectral Match to Monolinolenin (9c,12c,15c) from NIST14 M+H (1)
Stearylbis(2-hydroxyethyl)aminium (1)
PE(16:1/0:0); [M+H]+ C21H43N1O7P1 M+H (1)
Spectral Match to Monopalmitolein (9c) from NIST14 M+H-H2O (1)
LDGTS 18:4 (1)
PC(18:3/0:0); [M+H]+ C26H49N1O7P1 M+H (1)
2,3-dihydroxypropyl (9E,11E,13E)-hexadeca-9,11,13-trienoate (1)
MGMG 16:4 (1)
LDGTS 16:3 (1)
Canangalia H M+H (1)
2-hydroxy-3-{[3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy}propyl hexadeca-4,7,10,13-tetraenoate (1)
LDGTS 16:4 (1)
NCGC00385642-01!1,4-dihydroxyheptadec-16-en-2-yl acetate [IIN-based: Match] (1)
LPE 16:3 (1)

First Public Date

2014 (9)
2023 (5)
2019 (5)
2025 (3)
2024 (3)
2021 (3)
2026 (2)
2022 (2)
2015 (2)
2018 (1)
2017 (1)

Classification

bacteria (3)
fungi (1)

Study type

Transcription profiling by array (72)
RNA-seq of coding RNA (5)
Transcription profiling by RT-PCR (2)
RNA-seq of total RNA (2)
Genotyping by array (1)
ChIP-seq (1)

Release Date

2022 (78)
2025 (76)
2024 (72)
2023 (71)
2021 (66)
2019 (61)
2020 (59)
2017 (53)
2015 (49)
2018 (44)
2014 (40)
2010 (40)
2016 (38)
2013 (33)
2011 (32)
2012 (23)
2009 (21)
2008 (15)
2006 (8)
2026 (8)
2007 (6)
2003 (3)
2005 (3)
2004 (2)
2000 (2)
2002 (1)
2001 (1)
1999 (1)
1998 (1)

Lab affiliation

Institute of Zoology and Center of Molecular Bioscience Innsbruck, University of Innsbruck, 6020 Innsbruck, Austria (2)
B CUBE, Technical University, Dresden, Germany (1)
Biomolecular Mass Spectrometry and Proteomics Bijvoet Center for Biomolecular Reseach and Utrecht Institute of Pharmaceutical Sciences Utrecht University Padualaan 8, 3584 CH Utrecht, The Netherland (1)
CRCM (Marseille Protéomique), Inserm U1068, Institut Paoli-Calmettes, Aix-Marseille Université, UM105, CNRS UMR7258, Marseille (1)
Central European Institute of Technology, Masaryk University, Kamenice 753/5, 62500 Brno, Czech Republic National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 753/5, 62500 Brno, Czech Republic (1)
City University of New York Advanced Science Research Center - Nanoscience Department, USA City University of New York Hunter College -Chemistry & Biochemistry Department, USA (1)
College of Marine Life Sciences, Ocean University of China, Qingdao, China (1)
Department of Biochemistry, University of Missouri, Columbia, Missouri (1)
Department of Chemical Sciences, University of Naples Federico II (1)
Department of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio 43210, United States (1)
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599 USA (1)
Department of Pathology, Johns Hopkins School of Medicine, United States of America (1)
Department of Plasma Proteins, Sanquin Research, Amsterdam, The Netherlands (1)
Head of the Curie Institute Mass Spectrometry Platform (1)
Institut Pasteur, 25 rue du Dr. Roux, 75724 Paris cedex 15, France (1)
Institut Pasteur, Université Paris Cité, CNRS UMR3528, Biological NMR and HDX-MS Technological Platform, 75015, Paris, France. (1)
Institute for Microbiology Department of Microbial Proteomics and Mass Spectrometry Ernst-Moritz-Arndt-University Greifswald F.-L.-Jahn-Str. 15 17489 Greifswald (1)
Institute of Zoology, University of Innsbruck, Innsbruck, Austria (1)
Kunming Institute of Botany, Chinese Academy of Sciences (1)
Lab of Proteome Research, Department of Molecular Biology and Genetics, Federal Research and Clinical Center of Physical-Chemical Medicine of Federal Medical Biological Agency, Moscow, Russia (1)
Laboratory of Biology of Marine Organisms and Biomimetics Institute for Biosciences University of Mons Belgium (1)
Lopukhin Federal Research and Clinical Center of Physical-Chemical Medicine of Federal Medical Biological Agency (Lopukhin FRCC PCM), Head of the Proteomic Analysis Laboratory (1)
MRC Centre for Drug Safety Science, Dept Molecular & Clinical Pharmacology (1)
MRC Centre for Drug Safety Science, Dept Molecular & Clinical Pharmacology, University of Liverpool (1)
MRC Centre for Drug Safety Science, Dept Molecular and Clincal Pharmacology, University of Liverpool (1)
Michigan State University (1)
Molecular and Applied Microbiology, Leibniz Institute for Natural Product Research and Infection Biology / Hans Knöll Institute Jena (Leibniz-HKI), Jena, Germany (1)
Molecular and Cellular Biology Department, University of Guelph, 50 Stone Rd. E., Guelph, ON, N1H 2W1 (1)
Naval Research Laboratory (1)
Ocean University of China (1)

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Amphora coffeaeformis adhesive trail proteomics

Throughout all kingdoms of life, a large number of adhesive biomolecules have evolved to allow organisms to adhere to surfaces underwater. Proteins play an important role in the adhesion of numerous marine invertebrates (e.g. mussels, sea stars, sea urchins) whereas much less is known about the biol...

ORGANISM(S): Amphora coffeiformis

2021-09-08 | PXD013773 | Pride

Adhesive Diatom

A Natural Biological Adhesive from Snail Mucus for Wound Repair

PRJNA849232 | ENA

A Natural Biological Adhesive from Snail Mucus for Wound Repair

The information of main proteins from the two d-SMGs were identified

ORGANISM(S): Stylommatophora environmental sample

2022-12-12 | PXD036781 | Pride

Snail mucus，achatina fulica，helix lucorum，protein Biological adhesive

A Natural Biological Adhesive from Snail Mucus for Wound Repair

The discovery of the natural adhesion phenomena and mechanisms has advanced the information and development of a new generation of tissue adhesives in recent decades. In this study, we developed a natural biological adhesive from snail mucus consisting of a positively charged protein network and a p...

ORGANISM(S): Rattus norvegicus

2022-11-27 | GSE206113 | GEO

A molecular model of sea urchin reversible adhesion based on quantitative proteomics

Marine bioadhesives have unmatched performances especially in wet environments, being valuable sources of inspiration for industrial and biomedical applications. In sea urchins specialized adhesive organs, called tube feet, mediate adhesion. These are composed by a disc, which produces adhesive and ...

ORGANISM(S): Paracentrotus lividus (Common sea urchin)

2016-03-21 | PXD003122 | Pride

Sea urchin Echinoderm Tube foot adhesive protein Reversible adhesion Paracentrotus lividus Quantitative proteomics

Streptococcus pneumoniae in a biofilm are hyper-adhesive, avirulent, and when used as a killed whole-cell vaccine confers protection against lethal challenge

For Streptococcus pneumoniae, biofilms have been suggested to promote long-term colonization of the nasopharynx and contribute to the pathology of recurrent middle ear infections. To date numerous studies have investigated the contribution of specific genetic determinants for the development of pneu...

ORGANISM(S): Streptococcus pneumoniae

2013-04-01 | E-GEOD-26976 | biostudies-arrayexpress

Analysis of the Amphibalanus amphitrite adhesive proteome using pressure cycling technology: Method development and the effect of extraction solvents

Background: Marine biofouling negatively impacts industries reliant upon submerged stationary surfaces. The acorn barnacle Amphibalanus amphitrite is a major biofouler that permanently attaches to a wide array of substrates by producing a proteinaceous adhesive at the surface interface. These interf...

ORGANISM(S): Amphibalanus amphitrite (Striped barnacle) (Balanus amphitrite)

2019-07-04 | PXD012730 | Pride

Proteomics Amphibalanus amphitrite Bioadhesion Pressure cycling technology Biofouling

Transcriptomic analysis of adhesive capsulitis of the shoulder

PRJNA590709 | ENA

A natural biological adhesive from snail mucus for wound repair.

Not available

S-EPMC9873654 | biostudies-literature

Shear-sensitive adhesion enables size-independent adhesive performance in stick insects.

Not available

S-EPMC6834048 | biostudies-literature

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