Are there other online bibtex getters besides Zotero? I found another case that may be a "pattern"

[Mike Marchywka]

If anyone know of other services I can check them too. This is great for  development.
Also, in at least one case I found a website was blocking headless chrome but took
wget with ua="Firefox" and Zotero failed on that site too. Presumably they are using a
self-identifying headless chrome. Its amazing that publishers make it hard to cite there
work but news sites will happily send full article text even if the browser puts up a paywall- I think
they get to count those as page views :) 

It may be important for some users to customize or edit or retain extra fields in their
bibtex and it looks like generally Zotero filters stuff out without notice. 

For some reason, theses can be hard. If you have the pdf open, most places I've found don't have links  or
embedded DOI's. Here is a case in point, 

https://bonndoc.ulb.uni-bonn.de/xmlui/bitstream/handle/20.500.11811/8036/5508.pdf;jsessionid=8EE2D4C371DD10838C62271A1D5CEC0E?sequence=1

Zotero throws an error as did my code at first.  It turns out though you can mutate the url into
a useful one, 

https://bonndoc.ulb.uni-bonn.de/xmlui/handle/20.500.11811/8036

For this, Zotero gves the reasonable result, 

@article{liphardt_characterization_2019,
	title = {Characterization of {VKORC1L1} with respect to {VKORC1}},
	copyright = {In Copyright},
	url = {https://bonndoc.ulb.uni-bonn.de/xmlui/handle/20.500.11811/8036},
	abstract = {Vitamin K reduction is essential and catalyzed by two enzymes in vitro. Vitamin K 2,3-epoxide reductase complex subunit 1 (VKORC1) reduces vitamin K to sustain γ-carboxylation of vitamin K dependent (VKD) proteins. This modification is important to physiologically activate all VKD proteins, which are involved in blood coagulation, bone and glucose metabolism. Inhibition of VKORC1 by oral anticoagulants (OACs) is clini-cally used in therapy and prevention of thrombosis. However, OACs also inhibit the isozyme VKORC1-like1 (VKORC1L1), which may have antioxidative properties and is suspected to reduce vitamin K to scavenge reactive oxygen species. {\textless}br /{\textgreater} Specific inhibition data for various OACs were examined by means genetically engi-neered VKOR deficient HEK 293T cells. Inhibition profile differed in terms of therapeutic OACs with 4-hydroxycoumarin and 1,3-indandione backbone. In contrast, rodenti-cides investigated showed similar susceptibility for both enzymes. To explain the distinct inhibition pattern in silico and in vitro analysis was performed which identified a warfarin binding site in VKORC1L1 other than VKORC1 binding site.{\textless}br /{\textgreater} The function of VKORC1L1 in vivo is still unclear. In order to check the effect of the absence of the enzyme, we generated Vkorc1l1-/- mouse by CRISPR/Cas9 gene edit-ing. Those mice were viable in homozygous state, in contrast to Vkorc1-/- mice, and showed normal fertility. However, they were slender and smaller in size and showed reduced cholesterol and glucose levels in plasma compared to their wild type littermates. Further phenotyping is needed to describe those mice in more detail.},
	language = {eng},
	urldate = {2021-06-13},
	author = {Liphardt, Kerstin},
	month = jul,
	year = {2019},
}

My code will now automatically mutate it and pickup the other fields although it did not change note
to abstract and if the "all" option is specified some results are spurious, 

% mjmhandler: toobib guessbonndoc<-handleisbib
% date 2021-06-13:10:47:01 Sun Jun 13 10:47:01 EDT 2021
% srcurl: https://bonndoc.ulb.uni-bonn.de/xmlui/handle/20.500.11811/8036 https://bonndoc.ulb.uni-bonn.de/xmlui/bitstream/handle/20.500.11811/8036/5508.pdf;jsessionid=8EE2D4C371DD10838C62271A1D5CEC0E?sequence=1
% citeurl: https://bonndoc.ulb.uni-bonn.de/xmlui/handle/20.500.11811/8036
   @phdthesis{handle:20.500.11811/8036,
   author = {{Kerstin Liphardt}},
   title = {Characterization of VKORC1L1 with respect to VKORC1},
   school = {Rheinische Friedrich-Wilhelms-Universitt Bonn},
   year = 2019,
   month = jul,
   note = {Vitamin K reduction is essential and catalyzed by two enzymes in vitro. Vitamin K 2,3-epoxide reductase complex subunit 1 (VKORC1) reduces vitamin K to sustain �-carboxylation of vitamin K dependent (VKD) proteins. This modification is important to physiologically activate all VKD proteins, which are involved in blood coagulation, bone and glucose metabolism. Inhibition of VKORC1 by oral anticoagulants (OACs) is clini-cally used in therapy and prevention of thrombosis. However, OACs also inhibit the isozyme VKORC1-like1 (VKORC1L1), which may have antioxidative properties and is suspected to reduce vitamin K to scavenge reactive oxygen species.
   Specific inhibition data for various OACs were examined by means genetically engi-neered VKOR deficient HEK 293T cells. Inhibition profile differed in terms of therapeutic OACs with 4-hydroxycoumarin and 1,3-indandione backbone. In contrast, rodenti-cides investigated showed similar susceptibility for both enzymes. To explain the distinct inhibition pattern in silico and in vitro analysis was performed which identified a warfarin binding site in VKORC1L1 other than VKORC1 binding site.
   The function of VKORC1L1 in vivo is still unclear. In order to check the effect of the absence of the enzyme, we generated Vkorc1l1-/- mouse by CRISPR/Cas9 gene edit-ing. Those mice were viable in homozygous state, in contrast to Vkorc1-/- mice, and showed normal fertility. However, they were slender and smaller in size and showed reduced cholesterol and glucose levels in plasma compared to their wild type littermates. Further phenotyping is needed to describe those mice in more detail.},
   url = {http://hdl.handle.net/20.500.11811/8036}
   ,
srcurl={https://bonndoc.ulb.uni-bonn.de/xmlui/bitstream/handle/20.500.11811/8036/5508.pdf;jsessionid=8EE2D4C371DD10838C62271A1D5CEC0E?sequence=1},
xsrcurl={https://bonndoc.ulb.uni-bonn.de/xmlui/handle/20.500.11811/8036},
citeurl={https://bonndoc.ulb.uni-bonn.de/xmlui/handle/20.500.11811/8036}
}




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 Mike Marchywka 306 Charles Cox Drive Canton, GA 30115
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