Example of Journal of Mass Spectrometry format
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Example of Journal of Mass Spectrometry format Example of Journal of Mass Spectrometry format Example of Journal of Mass Spectrometry format Example of Journal of Mass Spectrometry format Example of Journal of Mass Spectrometry format Example of Journal of Mass Spectrometry format
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Example of Journal of Mass Spectrometry format Example of Journal of Mass Spectrometry format Example of Journal of Mass Spectrometry format Example of Journal of Mass Spectrometry format Example of Journal of Mass Spectrometry format Example of Journal of Mass Spectrometry format
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open access Open Access

Journal of Mass Spectrometry — Template for authors

Publisher: Wiley
Categories Rank Trend in last 3 yrs
Spectroscopy #45 of 74 down down by 19 ranks
journal-quality-icon Journal quality:
Medium
calendar-icon Last 4 years overview: 450 Published Papers | 1303 Citations
indexed-in-icon Indexed in: Scopus
last-updated-icon Last updated: 18/06/2020
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Journal Performance & Insights

Impact Factor

CiteRatio

Determines the importance of a journal by taking a measure of frequency with which the average article in a journal has been cited in a particular year.

A measure of average citations received per peer-reviewed paper published in the journal.

1.671

26% from 2018

Impact factor for Journal of Mass Spectrometry from 2016 - 2019
Year Value
2019 1.671
2018 2.267
2017 2.112
2016 2.422
graph view Graph view
table view Table view

2.9

15% from 2019

CiteRatio for Journal of Mass Spectrometry from 2016 - 2020
Year Value
2020 2.9
2019 3.4
2018 3.9
2017 4.2
2016 4.4
graph view Graph view
table view Table view

insights Insights

  • Impact factor of this journal has decreased by 26% in last year.
  • This journal’s impact factor is in the top 10 percentile category.

insights Insights

  • CiteRatio of this journal has decreased by 15% in last years.
  • This journal’s CiteRatio is in the top 10 percentile category.

SCImago Journal Rank (SJR)

Source Normalized Impact per Paper (SNIP)

Measures weighted citations received by the journal. Citation weighting depends on the categories and prestige of the citing journal.

Measures actual citations received relative to citations expected for the journal's category.

0.475

8% from 2019

SJR for Journal of Mass Spectrometry from 2016 - 2020
Year Value
2020 0.475
2019 0.515
2018 0.641
2017 0.65
2016 0.923
graph view Graph view
table view Table view

0.689

4% from 2019

SNIP for Journal of Mass Spectrometry from 2016 - 2020
Year Value
2020 0.689
2019 0.715
2018 0.824
2017 0.716
2016 0.88
graph view Graph view
table view Table view

insights Insights

  • SJR of this journal has decreased by 8% in last years.
  • This journal’s SJR is in the top 10 percentile category.

insights Insights

  • SNIP of this journal has decreased by 4% in last years.
  • This journal’s SNIP is in the top 10 percentile category.
Journal of Mass Spectrometry

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Wiley

Journal of Mass Spectrometry

The aim of JMS is to serve the scientific community with information provided and arranged to help senior investigators to better stay abreast of new discoveries and studies in their own field, to make them aware of events and developments in associated fields, and to provide ...... Read More

Spectroscopy

Chemistry

i
Last updated on
17 Jun 2020
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ISSN
1076-5174
i
Impact Factor
High - 1.001
i
Open Access
Yes
i
Sherpa RoMEO Archiving Policy
Yellow faq
i
Plagiarism Check
Available via Turnitin
i
Endnote Style
Download Available
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Bibliography Name
apa
i
Citation Type
Numbered
[25]
i
Bibliography Example
Beenakker, C.W.J. (2006) Specular andreev reflection in graphene.Phys. Rev. Lett., 97 (6), 067 007. URL 10.1103/PhysRevLett.97.067007.

Top papers written in this journal

Journal Article DOI: 10.1002/JMS.1777
MassBank: a public repository for sharing mass spectral data for life sciences.

Abstract:

MassBank is the first public repository of mass spectra of small chemical compounds for life sciences (<3000 Da). The database contains 605 electron-ionization mass spectrometry (EI-MS), 137 fast atom bombardment MS and 9276 electrospray ionization (ESI)-MS(n) data of 2337 authentic compounds of metabolites, 11 545 EI-MS and ... MassBank is the first public repository of mass spectra of small chemical compounds for life sciences (<3000 Da). The database contains 605 electron-ionization mass spectrometry (EI-MS), 137 fast atom bombardment MS and 9276 electrospray ionization (ESI)-MS(n) data of 2337 authentic compounds of metabolites, 11 545 EI-MS and 834 other-MS data of 10,286 volatile natural and synthetic compounds, and 3045 ESI-MS(2) data of 679 synthetic drugs contributed by 16 research groups (January 2010). ESI-MS(2) data were analyzed under nonstandardized, independent experimental conditions. MassBank is a distributed database. Each research group provides data from its own MassBank data servers distributed on the Internet. MassBank users can access either all of the MassBank data or a subset of the data by specifying one or more experimental conditions. In a spectral search to retrieve mass spectra similar to a query mass spectrum, the similarity score is calculated by a weighted cosine correlation in which weighting exponents on peak intensity and the mass-to-charge ratio are optimized to the ESI-MS(2) data. MassBank also provides a merged spectrum for each compound prepared by merging the analyzed ESI-MS(2) data on an identical compound under different collision-induced dissociation conditions. Data merging has significantly improved the precision of the identification of a chemical compound by 21-23% at a similarity score of 0.6. Thus, MassBank is useful for the identification of chemical compounds and the publication of experimental data. read more read less

Topics:

Mass spectrometry (50%)50% related to the paper, Mass spectrum (50%)50% related to the paper
1,689 Citations
Journal Article DOI: 10.1002/JMS.856
The Orbitrap: a new mass spectrometer
Qizhi Hu1, Robert J. Noll1, Hongyan Li1, Alexander Makarov2, Mark Hardman2, R. Graham Cooks1

Abstract:

Research areas such as proteomics and metabolomics are driving the demand for mass spectrometers that have high performance but modest power requirements, size, and cost. This paper describes such an instrument, the Orbitrap, based on a new type of mass analyzer invented by Makarov. The Orbitrap operates by radially trapping ... Research areas such as proteomics and metabolomics are driving the demand for mass spectrometers that have high performance but modest power requirements, size, and cost. This paper describes such an instrument, the Orbitrap, based on a new type of mass analyzer invented by Makarov. The Orbitrap operates by radially trapping ions about a central spindle electrode. An outer barrel-like electrode is coaxial with the inner spindlelike electrode and mass/charge values are measured from the frequency of harmonic ion oscillations, along the axis of the electric field, undergone by the orbitally trapped ions. This axial frequency is independent of the energy and spatial spread of the ions. Ion frequencies are measured non-destructively by acquisition of time-domain image current transients, with subsequent fast Fourier transforms (FFTs) being used to obtain the mass spectra. In addition to describing the Orbitrap mass analyzer, this paper also describes a complete Orbitrap-based mass spectrometer, equipped with an electrospray ionization source (ESI). Ions are transferred from the ESI source through three stages of differential pumping using RF guide quadrupoles. The third quadrupole, pressurized to less than 10(-3) Torr with collision gas, acts as an ion accumulator; ion/neutral collisions slow the ions and cause them to pool in an axial potential well at the end of the quadrupole. Ion bunches are injected from this pool into the Orbitrap analyzer for mass analysis. The ion injection process is described in a simplified way, including a description of electrodynamic squeezing, field compensation for the effects of the ion injection slit, and criteria for orbital stability. Features of the Orbitrap at its present stage of development include high mass resolution (up to 150,000), large space charge capacity, high mass accuracy (2-5 ppm), a mass/charge range of at least 6000, and dynamic range greater than 10(3). Applications based on electrospray ionization are described, including characterization of transition-metal complexes, oligosaccharides, peptides, and proteins. Use is also made of the high-resolution capabilities of the Orbitrap to confirm the presence of metaclusters of serine octamers in ESI mass spectra and to perform H/D exchange experiments on these ions in the storage quadrupole. read more read less

Topics:

Orbitrap (72%)72% related to the paper, Hybrid mass spectrometer (67%)67% related to the paper, Quadrupole mass analyzer (65%)65% related to the paper, Mass spectrometry (62%)62% related to the paper, Mass spectrum (62%)62% related to the paper
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1,309 Citations
Journal Article DOI: 10.1002/JMS.1383
Ion mobility-mass spectrometry.
Abu B. Kanu1, Prabha Dwivedi1, Maggie Tam1, Laura M. Matz1, Herbert H. Hill1

Abstract:

This review article compares and contrasts various types of ion mobility-mass spectrometers available today and describes their advantages for application to a wide range of analytes. Ion mobility spectrometry (IMS), when coupled with mass spectrometry, offers value-added data not possible from mass spectra alone. Separation ... This review article compares and contrasts various types of ion mobility-mass spectrometers available today and describes their advantages for application to a wide range of analytes. Ion mobility spectrometry (IMS), when coupled with mass spectrometry, offers value-added data not possible from mass spectra alone. Separation of isomers, isobars, and conformers; reduction of chemical noise; and measurement of ion size are possible with the addition of ion mobility cells to mass spectrometers. In addition, structurally similar ions and ions of the same charge state can be separated into families of ions which appear along a unique mass-mobility correlation line. This review describes the four methods of ion mobility separation currently used with mass spectrometry. They are (1) drift-time ion mobility spectrometry (DTIMS), (2) aspiration ion mobility spectrometry (AIMS), (3) differential-mobility spectrometry (DMS) which is also called field-asymmetric waveform ion mobility spectrometry (FAIMS) and (4) traveling-wave ion mobility spectrometry (TWIMS). DTIMS provides the highest IMS resolving power and is the only IMS method which can directly measure collision cross-sections. AIMS is a low resolution mobility separation method but can monitor ions in a continuous manner. DMS and FAIMS offer continuous-ion monitoring capability as well as orthogonal ion mobility separation in which high-separation selectivity can be achieved. TWIMS is a novel method of IMS with a low resolving power but has good sensitivity and is well intergrated into a commercial mass spectrometer. One hundred and sixty references on ion mobility-mass spectrometry (IMMS) are provided. read more read less

Topics:

Ion-mobility spectrometry–mass spectrometry (67%)67% related to the paper, Ion-mobility spectrometry (66%)66% related to the paper, Mass spectrometry (62%)62% related to the paper, Selected reaction monitoring (60%)60% related to the paper, Mass spectrum (54%)54% related to the paper
1,034 Citations
Journal Article DOI: 10.1002/BMS.1200160119
Contributions of mass spectrometry to peptide and protein structure.
Klaus Biemann1

Abstract:

With the advent of recombinant deoxyribonucleic acid (DNA) technology which allows a wide range of manipulation of genes and their expression in cell lines other than the natural ones, many aspects of protein structure have become more important than ever. In addition to the determination of the amino acid sequence questions ... With the advent of recombinant deoxyribonucleic acid (DNA) technology which allows a wide range of manipulation of genes and their expression in cell lines other than the natural ones, many aspects of protein structure have become more important than ever. In addition to the determination of the amino acid sequence questions relating to homogeneity, the nature of post-translational modifications, the verification of the structure of a protein produced by a synthetically modified gene or the detection of a natural mutant are all questions that are more and more frequently asked and with the demand for more detail. Mass spectrometry has emerged as an important contributor to this field, particularly since the advent of fast atom bombardment (FAB) ionization, which makes it possible to ionize directly large polar molecules such as peptides and small proteins. As such, FAB mass spectrometry provides mainly molecular weight information which, in itself, often sufficies to answer certain questions, particularly because the mass of many peptides can be determined directly from a single mass spectrum of a mixture. However, in order to obtain detailed structural information, such as the amino acid sequence, fragmentation has to be induced by collision processes and the product ions separated, preferably in the second mass spectrometer of a tandem system. This approach is particularly suited for the determination of the sequence of N-blocked peptides and the nature of the blocking group; the type and location of modified (i.e. phosphorylated, sulfated, glycosylated) amino acids; detection or verification of amino acid replacements; confirmation of the structure of synthetic peptides; and last but not least, the determination of the primary structure of proteins. read more read less

Topics:

Protein mass spectrometry (64%)64% related to the paper, Bottom-up proteomics (59%)59% related to the paper, Isobaric labeling (58%)58% related to the paper, Peptide sequence (58%)58% related to the paper, Protein structure (57%)57% related to the paper
994 Citations
Mobile and localized protons: a framework for understanding peptide dissociation
Vicki H. Wysocki1, George Tsaprailis1, Lori L. Smith1, Linda Breci1

Abstract:

Protein identification and peptide sequencing by tandem mass spectrometry requires knowledge of how peptides fragment in the gas phase, specifically which bonds are broken and where the charge(s) resides in the products. For many peptides, cleavage at the amide bonds dominate, producing a series of ions that are designated b ... Protein identification and peptide sequencing by tandem mass spectrometry requires knowledge of how peptides fragment in the gas phase, specifically which bonds are broken and where the charge(s) resides in the products. For many peptides, cleavage at the amide bonds dominate, producing a series of ions that are designated b and y. For other peptides, enhanced cleavage occurs at just one or two amino acid residues. Surface-induced dissociation, along with gas-phase collision-induced dissociation performed under a variety of conditions, has been used to refine the general 'mobile proton' model and to determine how and why enhanced cleavages occur at aspartic acid residues and protonated histidine residues. Enhanced cleavage at acidic residues occurs when the charge is unavailable to the peptide backbone or the acidic side-chain. The acidic H of the side-chain then serves to initiate cleavage at the amide bond immediately C-terminal to Asp (or Glu), producing an anhydride. In contrast, enhanced cleavage occurs at His when the His side-chain is protonated, turning His into a weak acid that can initiate backbone cleavage by transferring a proton to the backbone. This allows the nucleophilic nitrogen of the His side-chain to attack and form a cyclic structure that is different from the 'typical' backbone cleavage structures. read more read less

Topics:

Collision-induced dissociation (53%)53% related to the paper, Peptide bond (53%)53% related to the paper, Peptide sequence (51%)51% related to the paper, Peptide (51%)51% related to the paper, Tandem mass spectrometry (50%)50% related to the paper
956 Citations
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Journal of Mass Spectrometry format uses apa citation style.

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Frequently asked questions

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Yes, the template is compliant with the Journal of Mass Spectrometry guidelines. Our experts at SciSpace ensure that. If there are any changes to the journal's guidelines, we'll change our algorithm accordingly.

3. Can I cite my article in multiple styles in Journal of Mass Spectrometry?

Of course! We support all the top citation styles, such as APA style, MLA style, Vancouver style, Harvard style, and Chicago style. For example, when you write your paper and hit autoformat, our system will automatically update your article as per the Journal of Mass Spectrometry citation style.

4. Can I use the Journal of Mass Spectrometry templates for free?

Sign up for our free trial, and you'll be able to use all our features for seven days. You'll see how helpful they are and how inexpensive they are compared to other options, Especially for Journal of Mass Spectrometry.

5. Can I use a manuscript in Journal of Mass Spectrometry that I have written in MS Word?

Yes. You can choose the right template, copy-paste the contents from the word document, and click on auto-format. Once you're done, you'll have a publish-ready paper Journal of Mass Spectrometry that you can download at the end.

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After writing your paper autoformatting in Journal of Mass Spectrometry, you can download it in multiple formats, viz., PDF, Docx, and LaTeX.

12. Is Journal of Mass Spectrometry's impact factor high enough that I should try publishing my article there?

To be honest, the answer is no. The impact factor is one of the many elements that determine the quality of a journal. Few of these factors include review board, rejection rates, frequency of inclusion in indexes, and Eigenfactor. You need to assess all these factors before you make your final call.

13. What is Sherpa RoMEO Archiving Policy for Journal of Mass Spectrometry?

SHERPA/RoMEO Database

We extracted this data from Sherpa Romeo to help researchers understand the access level of this journal in accordance with the Sherpa Romeo Archiving Policy for Journal of Mass Spectrometry. The table below indicates the level of access a journal has as per Sherpa Romeo's archiving policy.

RoMEO Colour Archiving policy
Green Can archive pre-print and post-print or publisher's version/PDF
Blue Can archive post-print (ie final draft post-refereeing) or publisher's version/PDF
Yellow Can archive pre-print (ie pre-refereeing)
White Archiving not formally supported
FYI:
  1. Pre-prints as being the version of the paper before peer review and
  2. Post-prints as being the version of the paper after peer-review, with revisions having been made.

14. What are the most common citation types In Journal of Mass Spectrometry?

The 5 most common citation types in order of usage for Journal of Mass Spectrometry are:.

S. No. Citation Style Type
1. Author Year
2. Numbered
3. Numbered (Superscripted)
4. Author Year (Cited Pages)
5. Footnote

15. How do I submit my article to the Journal of Mass Spectrometry?

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16. Can I download Journal of Mass Spectrometry in Endnote format?

Yes, SciSpace provides this functionality. After signing up, you would need to import your existing references from Word or Bib file to SciSpace. Then SciSpace would allow you to download your references in Journal of Mass Spectrometry Endnote style according to Elsevier guidelines.

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