Ron Heeren

Last updated
Ron M.A. Heeren
Ron Heeren.jpg
Ron Heeren in 2017
Born1965
Tilburg, Netherlands
NationalityDutch
Alma materUniversity of Amsterdam
AwardsHans Fisher Fellowship; Thomson Medal of IMSF; NWO-Physics Valorisation Prize; Brightlands Convention Award; Robert Feulgen lecturer, Society for Histochemistry; Distinguished Wiley Visiting Scientist award;
Scientific career
FieldsImaging Mass Spectrometry

Ron M.A. Heeren (born 1965, Tilburg) is a Dutch scientist in mass spectrometry imaging. He is currently a distinguished professor at Maastricht University and the scientific director of the Multimodal Molecular Imaging Institute (M4I), where he heads the division of Imaging Mass Spectrometry.

Contents

Scientific career

Heeren obtained a PhD degree in Technical Physics at the University of Amsterdam in 1992 under the supervision of Aart Kleyn.

He led a FOM-AMOLF research group on macromolecular ion physics and biomolecular imaging mass spectrometry (1995–2014). He was also professor at the chemistry faculty of Utrecht University in 2001–2019.

Between 1995 and 2015, he worked on new approaches towards high spatial resolution and high-throughput molecular imaging mass spectrometry using secondary ion mass spectrometry (SIMS) and matrix-assisted laser desorption and ionization (MALDI).

Heeren has coauthored over 300 peer-reviewed articles, which have been cited over 12,600 times (Google Scholar). [1]

Research

Heeren’s academic research interests are fundamental studies of the energetics of macromolecular systems, conformational studies of non-covalently bound protein complexes, translational imaging research, high-throughput bioinformatics, and the development and validation of new mass spectrometry–based proteomic imaging techniques for the life sciences.

During his postdoctoral fellowship, he worked on the development of innovative ion sources, vacuums systems, data acquisition systems and novel temperature-controlled ion cyclotron resonance cells. He used the FTICR-MS instrument for the study of collisional energy transfer and internal energy distributions. [2] [3] [4]  These methods were deployed to investigate their role in the determination of dissociation pathways of biomolecular systems. [5] [6]

As a project leader (1995–1997), Heeren led the application of high-resolution MS (FTICR-MS, FTIR imaging spectroscopy and SIMS) to the field of conservation science. He discovered and identified saponified pigment particulates in so-called protrusions in Rembrandt’s “The Anatomy Lesson of Dr. Nicolaes Tulp” in collaboration with the Mauritshuis museum in The Hague. [7] [8] [9]

Heeren and his group have pioneered the development of active pixelated detectors for mass spectrometry imaging. One such detector, the Medipix detector has been adapted to enable microscope-mode imaging mass spectrometry [10] for biomolecules to enable combined high-throughput and high-resolution molecular imaging using MALDI and SIMS.

Professional activities

From 2008 to 2013, Heeren was the research director for emerging technologies at the Netherlands Proteomics Centre. In 2014, he was appointed to his current position as one of the scientific directors of M4I at Maastricht University. [11] He was president of the Dutch Society of Mass Spectrometry between 2001–2005. [12] He is one of the founding members of the Mass Spectrometry Imaging Society, and was elected its president in 2017. [13]

Commercialization

Heeren holds 7 patents and has established two spin-off companies, Omics2Image/ASI and the Dutch Screening Group. In 2019, he was awarded the NWO Valorisation Prize in Physics. [14] [15]

Awards

Most cited publications

  1. Ščupáková, Klára; Dewez, Frédéric; Walch, Axel K.; Heeren, Ron M. A.; Balluff, Benjamin (2020-08-17). "Morphometric Cell Classification for Single-Cell MALDI-Mass Spectrometry Imaging". Angewandte Chemie International Edition. 59 (40): 17447–17450. doi:10.1002/anie.202007315. ISSN   1433-7851. PMC   7540554 . PMID   32668069.
  2. Ellis, Shane R.; Paine, Martin R. L.; Eijkel, Gert B.; Pauling, Josch K.; Husen, Peter; Jervelund, Mark W.; Hermansson, Martin; Ejsing, Christer S.; Heeren, Ron M. A. (2018-05-21). "Automated, parallel mass spectrometry imaging and structural identification of lipids". Nature Methods. 15 (7): 515–518. doi:10.1038/s41592-018-0010-6. ISSN   1548-7091. PMID   29786091. S2CID   29162438.
  3. Bruinen, Anne L.; Fisher, Gregory L.; Balez, Rachelle; van der Sar, Astrid M.; Ooi, Lezanne; Heeren, Ron M. A. (2018-06-12). "Identification and High-Resolution Imaging of α-Tocopherol from Human Cells to Whole Animals by TOF-SIMS Tandem Mass Spectrometry". Journal of the American Society for Mass Spectrometry. 29 (8): 1571–1581. Bibcode:2018JASMS..29.1571B. doi:10.1007/s13361-018-1979-x. ISSN   1044-0305. PMC   6060986 . PMID   29949055.
  4. Ščupáková, Klára; Soons, Zita; Ertaylan, Gökhan; Pierzchalski, Keely A.; Eijkel, Gert B.; Ellis, Shane R.; Greve, Jan W.; Driessen, Ann; Verheij, Joanne; De Kok, Theo M.; Olde Damink, Steven W. M. (17 April 2018). "Spatial Systems Lipidomics Reveals Nonalcoholic Fatty Liver Disease Heterogeneity". Analytical Chemistry. 90 (8): 5130–5138. doi:10.1021/acs.analchem.7b05215. ISSN   1520-6882. PMC   5906754 . PMID   29570976.
  5. Ellis, S. R.; Soltwisch, J.; Paine, M. R. L.; Dreisewerd, K.; Heeren, R. M. A. (2017). "Laser post-ionisation combined with a high resolving power orbitrap mass spectrometer for enhanced MALDI-MS imaging of lipids". Chemical Communications. 53 (53): 7246–7249. doi:10.1039/c7cc02325a. ISSN   1359-7345. PMID   28573274. S2CID   4627246.
  6. Ogrinc Potočnik, Nina; Porta, Tiffany; Becker, Michael; Heeren, Ron M. A.; Ellis, Shane R. (2015-10-28). "Use of advantageous, volatile matrices enabled by next-generation high-speed matrix-assisted laser desorption/ionization time-of-flight imaging employing a scanning laser beam". Rapid Communications in Mass Spectrometry. 29 (23): 2195–2203. Bibcode:2015RCMS...29.2195O. doi:10.1002/rcm.7379. ISSN   0951-4198. PMID   26522310.
  7. Ellis, Shane R.; Jungmann, Julia H.; Smith, Donald F.; Soltwisch, Jens; Heeren, Ron M. A. (2013-10-18). "Enhanced detection of high-mass proteins by using an active pixel detector". Angewandte Chemie International Edition in English. 52 (43): 11261–11264. doi:10.1002/anie.201305501. ISSN   1521-3773. PMID   24039122.
  8. Jungmann, Julia H.; Smith, Donald F.; MacAleese, Luke; Klinkert, Ivo; Visser, Jan; Heeren, Ron M. A. (2012-07-27). "Biological Tissue Imaging with a Position and Time Sensitive Pixelated Detector". Journal of the American Society for Mass Spectrometry. 23 (10): 1679–1688. arXiv: 1305.5437 . Bibcode:2012JASMS..23.1679J. doi:10.1007/s13361-012-0444-5. ISSN   1044-0305. PMID   22836864. S2CID   13480751.
  9. Jungmann, Julia H.; MacAleese, Luke; Visser, Jan; Vrakking, Marc J. J.; Heeren, Ron M. A. (2011-10-15). "High Dynamic Range Bio-Molecular Ion Microscopy with the Timepix Detector". Analytical Chemistry. 83 (20): 7888–7894. doi:10.1021/ac2017629. ISSN   0003-2700. PMID   21882854.
  10. Chughtai, Kamila; Heeren, Ron M. A. (2010-05-12). "Mass Spectrometric Imaging for Biomedical Tissue Analysis". Chemical Reviews. 110 (5): 3237–3277. doi:10.1021/cr100012c. ISSN   0009-2665. PMC   2907483 . PMID   20423155.

Related Research Articles

<span class="mw-page-title-main">Mass spectrometry</span> Analytical technique based on determining mass to charge ratio of ions

Mass spectrometry (MS) is an analytical technique that is used to measure the mass-to-charge ratio of ions. The results are presented as a mass spectrum, a plot of intensity as a function of the mass-to-charge ratio. Mass spectrometry is used in many different fields and is applied to pure samples as well as complex mixtures.

<span class="mw-page-title-main">Ion source</span> Device that creates charged atoms and molecules (ions)

An ion source is a device that creates atomic and molecular ions. Ion sources are used to form ions for mass spectrometers, optical emission spectrometers, particle accelerators, ion implanters and ion engines.

Fourier-transform ion cyclotron resonance mass spectrometry is a type of mass analyzer (or mass spectrometer) for determining the mass-to-charge ratio (m/z) of ions based on the cyclotron frequency of the ions in a fixed magnetic field. The ions are trapped in a Penning trap (a magnetic field with electric trapping plates), where they are excited (at their resonant cyclotron frequencies) to a larger cyclotron radius by an oscillating electric field orthogonal to the magnetic field. After the excitation field is removed, the ions are rotating at their cyclotron frequency in phase (as a "packet" of ions). These ions induce a charge (detected as an image current) on a pair of electrodes as the packets of ions pass close to them. The resulting signal is called a free induction decay (FID), transient or interferogram that consists of a superposition of sine waves. The useful signal is extracted from this data by performing a Fourier transform to give a mass spectrum.

<span class="mw-page-title-main">Matrix-assisted laser desorption/ionization</span> Ionization technique

In mass spectrometry, matrix-assisted laser desorption/ionization (MALDI) is an ionization technique that uses a laser energy-absorbing matrix to create ions from large molecules with minimal fragmentation. It has been applied to the analysis of biomolecules and various organic molecules, which tend to be fragile and fragment when ionized by more conventional ionization methods. It is similar in character to electrospray ionization (ESI) in that both techniques are relatively soft ways of obtaining ions of large molecules in the gas phase, though MALDI typically produces far fewer multi-charged ions.

<span class="mw-page-title-main">Liquid chromatography–mass spectrometry</span> Analytical chemistry technique

Liquid chromatography–mass spectrometry (LC–MS) is an analytical chemistry technique that combines the physical separation capabilities of liquid chromatography with the mass analysis capabilities of mass spectrometry (MS). Coupled chromatography – MS systems are popular in chemical analysis because the individual capabilities of each technique are enhanced synergistically. While liquid chromatography separates mixtures with multiple components, mass spectrometry provides spectral information that may help to identify each separated component. MS is not only sensitive, but provides selective detection, relieving the need for complete chromatographic separation. LC–MS is also appropriate for metabolomics because of its good coverage of a wide range of chemicals. This tandem technique can be used to analyze biochemical, organic, and inorganic compounds commonly found in complex samples of environmental and biological origin. Therefore, LC–MS may be applied in a wide range of sectors including biotechnology, environment monitoring, food processing, and pharmaceutical, agrochemical, and cosmetic industries. Since the early 2000s, LC–MS has also begun to be used in clinical applications.

<span class="mw-page-title-main">History of mass spectrometry</span>

The history of mass spectrometry has its roots in physical and chemical studies regarding the nature of matter. The study of gas discharges in the mid 19th century led to the discovery of anode and cathode rays, which turned out to be positive ions and electrons. Improved capabilities in the separation of these positive ions enabled the discovery of stable isotopes of the elements. The first such discovery was with the element neon, which was shown by mass spectrometry to have at least two stable isotopes: 20Ne and 22Ne. Mass spectrometers were used in the Manhattan Project for the separation of isotopes of uranium necessary to create the atomic bomb.

<span class="mw-page-title-main">Orbitrap</span> Type of ion separator used in mass spectrometry

In mass spectrometry, Orbitrap is an ion trap mass analyzer consisting of an outer barrel-like electrode and a coaxial inner spindle-like electrode that traps ions in an orbital motion around the spindle. The image current from the trapped ions is detected and converted to a mass spectrum by first using the Fourier transform of time domain of the harmonic to create a frequency signal which is converted to mass.

Surface-enhanced laser desorption/ionization (SELDI) is a soft ionization method in mass spectrometry (MS) used for the analysis of protein mixtures. It is a variation of matrix-assisted laser desorption/ionization (MALDI). In MALDI, the sample is mixed with a matrix material and applied to a metal plate before irradiation by a laser, whereas in SELDI, proteins of interest in a sample become bound to a surface before MS analysis. The sample surface is a key component in the purification, desorption, and ionization of the sample. SELDI is typically used with time-of-flight (TOF) mass spectrometers and is used to detect proteins in tissue samples, blood, urine, or other clinical samples, however, SELDI technology can potentially be used in any application by simply modifying the sample surface.

Soft laser desorption (SLD) is laser desorption of large molecules that results in ionization without fragmentation. "Soft" in the context of ion formation means forming ions without breaking chemical bonds. "Hard" ionization is the formation of ions with the breaking of bonds and the formation of fragment ions.

<span class="mw-page-title-main">MALDI imaging</span> Imaging system

MALDI mass spectrometry imaging (MALDI-MSI) is the use of matrix-assisted laser desorption ionization as a mass spectrometry imaging technique in which the sample, often a thin tissue section, is moved in two dimensions while the mass spectrum is recorded. Advantages, like measuring the distribution of a large amount of analytes at one time without destroying the sample, make it a useful method in tissue-based study.

<span class="mw-page-title-main">Protein mass spectrometry</span> Application of mass spectrometry

Protein mass spectrometry refers to the application of mass spectrometry to the study of proteins. Mass spectrometry is an important method for the accurate mass determination and characterization of proteins, and a variety of methods and instrumentations have been developed for its many uses. Its applications include the identification of proteins and their post-translational modifications, the elucidation of protein complexes, their subunits and functional interactions, as well as the global measurement of proteins in proteomics. It can also be used to localize proteins to the various organelles, and determine the interactions between different proteins as well as with membrane lipids.

<span class="mw-page-title-main">Time-of-flight mass spectrometry</span> Method of mass spectrometry

Time-of-flight mass spectrometry (TOFMS) is a method of mass spectrometry in which an ion's mass-to-charge ratio is determined by a time of flight measurement. Ions are accelerated by an electric field of known strength. This acceleration results in an ion having the same kinetic energy as any other ion that has the same charge. The velocity of the ion depends on the mass-to-charge ratio. The time that it subsequently takes for the ion to reach a detector at a known distance is measured. This time will depend on the velocity of the ion, and therefore is a measure of its mass-to-charge ratio. From this ratio and known experimental parameters, one can identify the ion.

Mass spectrometry imaging (MSI) is a technique used in mass spectrometry to visualize the spatial distribution of molecules, as biomarkers, metabolites, peptides or proteins by their molecular masses. After collecting a mass spectrum at one spot, the sample is moved to reach another region, and so on, until the entire sample is scanned. By choosing a peak in the resulting spectra that corresponds to the compound of interest, the MS data is used to map its distribution across the sample. This results in pictures of the spatially resolved distribution of a compound pixel by pixel. Each data set contains a veritable gallery of pictures because any peak in each spectrum can be spatially mapped. Despite the fact that MSI has been generally considered a qualitative method, the signal generated by this technique is proportional to the relative abundance of the analyte. Therefore, quantification is possible, when its challenges are overcome. Although widely used traditional methodologies like radiochemistry and immunohistochemistry achieve the same goal as MSI, they are limited in their abilities to analyze multiple samples at once, and can prove to be lacking if researchers do not have prior knowledge of the samples being studied. Most common ionization technologies in the field of MSI are DESI imaging, MALDI imaging, secondary ion mass spectrometry imaging and Nanoscale SIMS (NanoSIMS).

<span class="mw-page-title-main">Top-down proteomics</span>

Top-down proteomics is a method of protein identification that either uses an ion trapping mass spectrometer to store an isolated protein ion for mass measurement and tandem mass spectrometry (MS/MS) analysis or other protein purification methods such as two-dimensional gel electrophoresis in conjunction with MS/MS. Top-down proteomics is capable of identifying and quantitating unique proteoforms through the analysis of intact proteins. The name is derived from the similar approach to DNA sequencing. During mass spectrometry intact proteins are typically ionized by electrospray ionization and trapped in a Fourier transform ion cyclotron resonance, quadrupole ion trap or Orbitrap mass spectrometer. Fragmentation for tandem mass spectrometry is accomplished by electron-capture dissociation or electron-transfer dissociation. Effective fractionation is critical for sample handling before mass-spectrometry-based proteomics. Proteome analysis routinely involves digesting intact proteins followed by inferred protein identification using mass spectrometry (MS). Top-down MS (non-gel) proteomics interrogates protein structure through measurement of an intact mass followed by direct ion dissociation in the gas phase.

Sample preparation for mass spectrometry is used for the optimization of a sample for analysis in a mass spectrometer (MS). Each ionization method has certain factors that must be considered for that method to be successful, such as volume, concentration, sample phase, and composition of the analyte solution. Quite possibly the most important consideration in sample preparation is knowing what phase the sample must be in for analysis to be successful. In some cases the analyte itself must be purified before entering the ion source. In other situations, the matrix, or everything in the solution surrounding the analyte, is the most important factor to consider and adjust. Often, sample preparation itself for mass spectrometry can be avoided by coupling mass spectrometry to a chromatography method, or some other form of separation before entering the mass spectrometer. In some cases, the analyte itself must be adjusted so that analysis is possible, such as in protein mass spectrometry, where usually the protein of interest is cleaved into peptides before analysis, either by in-gel digestion or by proteolysis in solution.

<span class="mw-page-title-main">Matrix-assisted laser desorption electrospray ionization</span> Ambient ionization technique

Matrix-assisted laser desorption electrospray ionization (MALDESI) was first introduced in 2006 as a novel ambient ionization technique which combines the benefits of electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI). An infrared (IR) or ultraviolet (UV) laser can be utilized in MALDESI to resonantly excite an endogenous or exogenous matrix. The term 'matrix' refers to any molecule that is present in large excess and absorbs the energy of the laser, thus facilitating desorption of analyte molecules. The original MALDESI design was implemented using common organic matrices, similar to those used in MALDI, along with a UV laser. The current MALDESI source employs endogenous water or a thin layer of exogenously deposited ice as the energy-absorbing matrix where O-H symmetric and asymmetric stretching bonds are resonantly excited by a mid-IR laser.

<span class="mw-page-title-main">Desorption atmospheric pressure photoionization</span> Ambient ionization technique

Desorption atmospheric pressure photoionization (DAPPI) is an ambient ionization technique for mass spectrometry that uses hot solvent vapor for desorption in conjunction with photoionization. Ambient Ionization techniques allow for direct analysis of samples without pretreatment. The direct analysis technique, such as DAPPI, eliminates the extraction steps seen in most nontraditional samples. DAPPI can be used to analyze bulkier samples, such as, tablets, powders, resins, plants, and tissues. The first step of this technique utilizes a jet of hot solvent vapor. The hot jet thermally desorbs the sample from a surface. The vaporized sample is then ionized by the vacuum ultraviolet light and consequently sampled into a mass spectrometer. DAPPI can detect a range of both polar and non-polar compounds, but is most sensitive when analyzing neutral or non-polar compounds. This technique also offers a selective and soft ionization for highly conjugated compounds.

<span class="mw-page-title-main">Ambient ionization</span>

Ambient ionization is a form of ionization in which ions are formed in an ion source outside the mass spectrometer without sample preparation or separation. Ions can be formed by extraction into charged electrospray droplets, thermally desorbed and ionized by chemical ionization, or laser desorbed or ablated and post-ionized before they enter the mass spectrometer.

<span class="mw-page-title-main">Desorption/ionization on silicon</span> Soft laser desorption method

Desorption/ionization on silicon (DIOS) is a soft laser desorption method used to generate gas-phase ions for mass spectrometry analysis. DIOS is considered the first surface-based surface-assisted laser desorption/ionization (SALDI-MS) approach. Prior approaches were accomplished using nanoparticles in a matrix of glycerol, while DIOS is a matrix-free technique in which a sample is deposited on a nanostructured surface and the sample desorbed directly from the nanostructured surface through the adsorption of laser light energy. DIOS has been used to analyze organic molecules, metabolites, biomolecules and peptides, and, ultimately, to image tissues and cells.

References

  1. ↑ "Ron M.A. Heeren". scholar.google.nl. Retrieved 2020-12-18.
  2. ↑ Heeren, Ron M. A.; Vékey, Károly (1998-09-15). <1175::aid-rcm305>3.0.co;2-l "A novel method to determine collisional energy transfer efficiency by Fourier transform ion cyclotron resonance mass spectrometry". Rapid Communications in Mass Spectrometry. 12 (17): 1175–1181. doi:10.1002/(sici)1097-0231(19980915)12:17<1175::aid-rcm305>3.0.co;2-l. ISSN   0951-4198.
  3. ↑ Drahos, null; Heeren, null; Collette, null; De Pauw E, null; Vekey, null (December 1999). "Thermal energy distribution observed in electrospray ionization". Journal of Mass Spectrometry. 34 (12): 1373–1379. Bibcode:1999JMSp...34.1373D. doi:10.1002/(SICI)1096-9888(199912)34:12<1373::AID-JMS907>3.0.CO;2-#. ISSN   1096-9888. PMID   10587635.
  4. ↑ Guo, Xinghua; Duursma, Marc C.; Kistemaker, Piet G.; Nibbering, Nico M. M.; Vekey, Karoly; Drahos, Laszlo; Heeren, Ron M. A. (June 2003). "Manipulating internal energy of protonated biomolecules in electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry". Journal of Mass Spectrometry. 38 (6): 597–606. Bibcode:2003JMSp...38..597G. doi:10.1002/jms.480. ISSN   1076-5174. PMID   12827629.
  5. ↑ Koster, Sander; Duursma, Marc C.; Boon, Jaap J.; Nielen, Michel W. F.; de Koster, Chris G.; Heeren, Ron M. A. (2000). <739::aid-jms3>3.0.co;2-# "Structural analysis of synthetic homo- and copolyesters by electrospray ionization on a Fourier transform ion cyclotron resonance mass spectrometer". Journal of Mass Spectrometry. 35 (6): 739–748. Bibcode:2000JMSp...35..739K. doi:10.1002/1096-9888(200006)35:6<739::aid-jms3>3.0.co;2-#. ISSN   1076-5174. PMID   10862127.
  6. ↑ Kleinnijenhuis, Anne J.; Duursma, Marc C.; Breukink, Eefjan; Heeren, Ron M. A.; Heck, Albert J. R. (2003-07-01). "Localization of intramolecular monosulfide bridges in lantibiotics determined with electron capture induced dissociation". Analytical Chemistry. 75 (13): 3219–3225. doi:10.1021/ac0263770. hdl: 1874/14955 . ISSN   0003-2700. PMID   12964772. S2CID   17450996.
  7. ↑ Heeren, Ron M. A.; Boon, Jaap J.; Noble, Petria; Wadum, Jørgen (1999). "Integrating imaging FTIR and secondary ion mass spectrometry for the analysis of embedded paint cross-sections". ICOM-CC Triennial Meeting (12th), Lyon, 29 August-3 September 1999: Preprints.: 228–233.
  8. ↑ "Recitative after Rembrandt's "The Anatomy Lesson of Dr. Nicolaes Tulp"", 90 Miles, University of Pittsburgh Press, pp. 78–79, 2005-03-23, doi:10.2307/j.ctvthhc5r.38, ISBN   978-0-8229-8033-9 , retrieved 2020-12-18
  9. ↑ Van Der Weerd, J.; Brammer, H.; Boon, J. J.; Heeren, R. M. A. (March 2002). "Fourier Transform Infrared Microscopic Imaging of an Embedded Paint Cross-Section". Applied Spectroscopy. 56 (3): 275–283. Bibcode:2002ApSpe..56Q.275V. doi:10.1366/0003702021954683. ISSN   0003-7028. S2CID   95454503.
  10. ↑ Jungmann, Julia H.; MacAleese, Luke; Visser, Jan; Vrakking, Marc J. J.; Heeren, Ron M. A. (2011-10-15). "High Dynamic Range Bio-Molecular Ion Microscopy with the Timepix Detector". Analytical Chemistry. 83 (20): 7888–7894. doi:10.1021/ac2017629. ISSN   0003-2700. PMID   21882854.
  11. ↑ "Maastricht University Magazine October 2014". Issuu. 14 October 2014. Retrieved 2020-12-18.
  12. ↑ "History". NVMS. Retrieved 2020-12-18.
  13. ↑ "Mass Spectrometry Imaging Society – MS Imaging". ms-imaging.org. Retrieved 2020-12-18.
  14. ↑ "NWO Physics Valorisation Prize 2019 - Ron Heeren - YouTube". www.youtube.com. 8 January 2020. Retrieved 2020-12-18.
  15. ↑ "NWO Physics Valorisation Prize goes to Ron Heeren from Maastricht University | NWO". www.nwo.nl. Retrieved 2020-12-18.
  16. ↑ "Heeren, Ron M.A. - Institute for Advanced Study (IAS)". www.ias.tum.de (in German). Retrieved 2020-12-18.
  17. ↑ Maastricht, Minderbroedersberg 4-6 6211 LK (25 May 2020). "Thomson Medal 2020 awarded to Ron Heeren". www.maastrichtuniversity.nl. Retrieved 2020-12-18.{{cite web}}: CS1 maint: numeric names: authors list (link)
  18. ↑ "International Mass Spectronomy Foundation". www.imss.nl. Retrieved 2020-12-18.
  19. ↑ Redactie (2019-03-27). "Uitreiking Brightlands Convention Award 2018". Conference Matters (in Dutch). Retrieved 2020-12-18.
  20. ↑ "Society for Histochemistry". www.histochemistry.eu. Retrieved 2020-12-18.
  21. ↑ "Press release: Omics2Image wins Venture Challenge Spring 2013" (PDF).
  22. ↑ "iDirector interview with Ron Heeren - YouTube". www.youtube.com. 28 June 2012. Retrieved 2020-12-18.
  23. ↑ "New EMSL Visiting Scientists Named".
  24. ↑ "Rapid Communications in Mass Spectrometry". Wiley Online Library. Retrieved 2020-12-18.
This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.