Merge pull request #99 from petersclarke/patch-7

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citations.tsv

@@ -478,6 +478,14 @@ DOI:10.1021/ja8019005	DOI:10.1021/ja8019005	doi:10.1021/ja8019005	OVsIcoNm
 DOI:10.1016/j.jasms.2004.11.001	DOI:10.1016/j.jasms.2004.11.001	doi:10.1016/j.jasms.2004.11.001	xhXJM8vz
 DOI:10.1021/acs.analchem.7b04810	DOI:10.1021/acs.analchem.7b04810	doi:10.1021/acs.analchem.7b04810	rqc6ScJr
 DOI:10.1002/mas.21560	DOI:10.1002/mas.21560	doi:10.1002/mas.21560	HNURrSN7
+DOI:https://doi.org/10.1021/ja011335z	DOI:https://doi.org/10.1021/ja011335z	doi:https://doi.org/10.1021/ja011335z	W7m8UNum
+DOI:https://doi.org/10.1021/acs.analchem.5b00162	DOI:https://doi.org/10.1021/acs.analchem.5b00162	doi:https://doi.org/10.1021/acs.analchem.5b00162	BG48TsdY
+DOI:10.1002/mas.21442	DOI:10.1002/mas.21442	doi:10.1002/mas.21442	ekbZzMCZ
+DOI:10.1021/acs.analchem.9b05388	DOI:10.1021/acs.analchem.9b05388	doi:10.1021/acs.analchem.9b05388	16lajpfJg
+DOI:10.1021/jacs.1c10757	DOI:10.1021/jacs.1c10757	doi:10.1021/jacs.1c10757	kcIkQ9U2
+DOI:10.1002/ange.201206232	DOI:10.1002/ange.201206232	doi:10.1002/ange.201206232	dRBXpy4q
+DOI:10.1021/acs.analchem.2c03030	DOI:10.1021/acs.analchem.2c03030	doi:10.1021/acs.analchem.2c03030	aQmCzpPg
+DOI:10.1021/acs.bioconjchem.3c00254	DOI:10.1021/acs.bioconjchem.3c00254	doi:10.1021/acs.bioconjchem.3c00254	o0OmLG1e
 DOI:10.1021/acs.analchem.8b01901	DOI:10.1021/acs.analchem.8b01901	doi:10.1021/acs.analchem.8b01901	UqS9JT46
 DOI:10.1021/acs.jproteome.7b00622	DOI:10.1021/acs.jproteome.7b00622	doi:10.1021/acs.jproteome.7b00622	1Gs2JKxdE
 DOI:10.1021/jasms.0c00425	DOI:10.1021/jasms.0c00425	doi:10.1021/jasms.0c00425	Vu5rNLFc

manuscript.md

@@ -40,8 +40,8 @@ header-includes: |
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@@ -133,9 +133,9 @@ header-includes: |
   <meta name="citation_fulltext_html_url" content="https://jessegmeyerlab.github.io/proteomics-tutorial/" />
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@@ -157,9 +157,9 @@ manubot-clear-requests-cache: false
 
 <small><em>
 This manuscript
-([permalink](https://jessegmeyerlab.github.io/proteomics-tutorial/v/d1d4f9366ec30517532fcba1db654a10ca827e02/))
+([permalink](https://jessegmeyerlab.github.io/proteomics-tutorial/v/e0a10c44dc2f0bc5c926778d3f8deceaa4e68ec6/))
 was automatically generated
-from [jessegmeyerlab/proteomics-tutorial@d1d4f93](https://github.com/jessegmeyerlab/proteomics-tutorial/tree/d1d4f9366ec30517532fcba1db654a10ca827e02)
+from [jessegmeyerlab/proteomics-tutorial@e0a10c4](https://github.com/jessegmeyerlab/proteomics-tutorial/tree/e0a10c44dc2f0bc5c926778d3f8deceaa4e68ec6)
 on October 27, 2023.
 </em></small>
 
@@ -1896,6 +1896,7 @@ The most popular of these alternative dissociation methods are electron-based di
 In both of these, peptide cations capture thermal electrons (ECD [@DOI:10.1021/ja973478k]) or abstract an electron from a reagent anion (ETD [@DOI:10.1073/pnas.0402700101]) to generate radical-driven dissociation of the N-Ca bond that predominantly generates sequence-informative c- and z-type product ions (**Figure 14C**).
 The mechanisms of ExD methods have been widely explored [@DOI:10.1021/ja8019005; @DOI:10.1016/j.jasms.2004.11.001], and the preferential cleavage of N-Ca bonds along the peptide backbone have been particularly useful for PTM-modified species because the modifications remain largely intact even during peptide backbone bond fragmentation.
 ExD methods have shown promise for analysis of numerous PTMs, including phosphorylation, glycosylation, ADP-ribosylation, and more [@DOI:10.1021/acs.analchem.7b04810; @DOI:10.1002/mas.21560].
+Electron-based dissociation is also more suitable than collision-based dissociation for MS analyses of intact proteins [@DOI:https://doi.org/10.1021/ja011335z; @DOI:https://doi.org/10.1021/acs.analchem.5b00162] and larger oligonucleotides [@DOI:10.1002/mas.21442; @DOI:10.1021/acs.analchem.9b05388; @DOI:10.1021/jacs.1c10757; @DOI:10.1002/ange.201206232; @DOI:10.1021/acs.analchem.2c03030; @DOI:10.1021/acs.bioconjchem.3c00254]
 
 Two fundamental challenges exist with ExD methods.
 First, ExD implementation requires instruments that can manipulate cations and anions (or free electrons) within the same scan sequence and can trap both simultaneously for electron capture/transfer events to occur.