Importing from Reference Manager

sjones0123 · October 21, 2024

I have a Reference Manager database with 33,000 entries that dates to the early 1990's that is indexed by "Reference ID #" (RID) with many very-useful-to-me printed out pdf's filed by RID#. These files take up more than a couple of file cabinet drawers. Is there any way preserve access to this filing system with Zotero? Can this RID# be imported into a Zotero database and retained as the primary method of indexing, searching, and filed-pdf access?

bwiernik · October 21, 2024

What export formats does Reference Manager have available (RIS, XML, BibTeX, etc)?

adamsmith · October 21, 2024

Whether the RID can be imported depends on whether it's exported -- you'd want to look at the Reference Manger export (likely RIS?) and open it in a text editor to see if the RID is there. If it isn't, that'd pretty much the end of it.

If it is, it can likely be imported and stored somehow, though would almost certainly require customization to do so.
I'm not sure what

retained as the primary method of indexing, searching, and filed-pdf access?

exactly means -- Zotero has its own item keys, so I guess the answer would be no, but really depends on what, specifically, you need in terms of functionality..

Gntts · 2024-11-03T03:03:00+00:00

Reference Manager has the following formats available:
RIS, MEDLARS, Comma Delimited, Tab Delimited.
As well as I understand, out of these formats only RIS can be used to import to Zotero.
Reference Manager exports all information about the reference, including Reference ID.
When importing by default, Zotero understand the majority of Ref. Manager fields correctly, but does not import Ref. ID.
The question is whether it is possible to configure Zotero import to transfer Ref. ID into Number (or other field)?

adamsmith · 2024-11-03T03:49:07+00:00

How is the Ref ID esxported in the RIS? Easiest would probably to just post one exported entry here.
Do you have a preference where Zotero should import it to (note there are no custom fields, so it'd need to be something that currently exists in ZOtero).

Gntts · 2024-11-03T11:44:33+00:00

Below, there is the example of the entry exported from Reference Manager in the RIS and then imported into Zotero.
At the bottom, I attached images of entries in Ref. Manager and Zotero. By the way, I like more both more compact layout of entry and more readable text background color/contrast in Ref Manager than in Zotero.
Customizable fields (like User Defined ones in Ref. manager) would be useful.

RIS generated by Reference Manager:

TY - JOUR
ID - 10102
T1 - Ionic signalling by growth factor receptors
A1 - Moolenaar,W.H.
A1 - Defize,L.H.K.
A1 - Laat,S.W.D.
Y1 - 1986/09/01/
KW - activation
KW - agonists
KW - antibodies
KW - binding
KW - Ca2+
KW - cell division
KW - cell proliferation
KW - cells
KW - channel
KW - culture
KW - cytoplasmic pH
KW - DNA
KW - DNA synthesis
KW - esters
KW - factor
KW - Growth
KW - growth factors
KW - human
KW - In vivo
KW - Mechanism
KW - membrane
KW - pH
KW - plasma membrane
KW - proliferation
KW - protein
KW - protein kinase C
KW - Receptor
KW - receptors
KW - stimulation
RP - IN FILE
SP - 359
EP - 373
JA - J.Exp.Biol.
VL - 124
IS - 1
U2 - 10.1242/jeb.124.1.359

N2 - The proliferation of cells in vivo and in culture is regulated by polypeptide growth factors, such as epidermal growth factor (EGF) and platelet-derived growth factor (PDGF). Growth factors initiate their action by binding to specific cell surface receptors. Receptor occupancy triggers a cascade of physiological changes in the target cell which ultimately lead to DNA synthesis and cell division. Immediate consequences of receptor activation include tyrosine-specific protein phosphorylations, a sustained increase in cytoplasmic pH (pH,) and a transient rise in free Ca2+. The rise in pH, has a permissive effect on DNA synthesis and is mediated by an otherwise quiescent Na+/H+ exchange mechanism in the plasma membrane, which is turned on by protein kinase C, the cellular receptor for phorbol esters. The rapid Ca2+ signal is due to either release from internal stores (PDGF) or net entry via a voltage-independent channel in the plasma membrane (EGF). Phorbol esters, acting via kinase C, inhibit the growth factor-induced Ca2+ signals without affecting resting Ca2+ levels. Monoclonal antibodies against the human EGF receptor can act as partial agonists in that they activate the tyrosine-specific protein kinase without inducing any of the ionic signals. These antibodies fail to induce DNA synthesis when added to quiescent fibroblasts, indicating that the Ca2+ and pH, signals can be dissociated from tyrosine kinase activity and suggesting that these signals are indispensable for the stimulation of cell proliferation
SN - Print ISSN: 0022-0949, Online ISSN: 1477-9145,
AD - Hubrecht Laboratory, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands

UR - https://doi.org/10.1242/jeb.124.1.359
L1 - https://journals.biologists.com/jeb/article-pdf/124/1/359/2863461/jexbio_124_1_359.pdf

L2 - https://journals.biologists.com/jeb/article/124/1/359/4876/Ionic-Signalling-by-Growth-Factor-Receptors

ER -
======================================

RIS generated by Zotero from the reference imported from the above file generated by Ref. Manager:

TY - JOUR
TI - Ionic signalling by growth factor receptors
AU - Moolenaar, W.H.
AU - Defize, L.H.K.
AU - Laat, S.W.D.
T2 - J.Exp.Biol.
AB - The proliferation of cells in vivo and in culture is regulated by polypeptide growth factors, such as epidermal growth factor (EGF) and platelet-derived growth factor (PDGF). Growth factors initiate their action by binding to specific cell surface receptors. Receptor occupancy triggers a cascade of physiological changes in the target cell which ultimately lead to DNA synthesis and cell division. Immediate consequences of receptor activation include tyrosine-specific protein phosphorylations, a sustained increase in cytoplasmic pH (pH,) and a transient rise in free Ca2+. The rise in pH, has a permissive effect on DNA synthesis and is mediated by an otherwise quiescent Na+/H+ exchange mechanism in the plasma membrane, which is turned on by protein kinase C, the cellular receptor for phorbol esters. The rapid Ca2+ signal is due to either release from internal stores (PDGF) or net entry via a voltage-independent channel in the plasma membrane (EGF). Phorbol esters, acting
via kinase C, inhibit the growth factor-induced Ca2+ signals without affecting resting Ca2+ levels. Monoclonal antibodies against the human EGF receptor can act as partial agonists in that they activate the tyrosine-specific protein kinase without inducing any of the ionic signals. These antibodies fail to induce DNA synthesis when added to quiescent fibroblasts, indicating that the Ca2+ and pH, signals can be dissociated from tyrosine kinase activity and suggesting that these signals are indispensable for the stimulation of cell proliferation
DA - 1986/09/01/
PY - 1986
VL - 124
IS - 1
SP - 359
EP - 373
J2 - J.Exp.Biol.
SN - Print ISSN: 0022-0949, Online ISSN: 1477-9145,
UR - https://doi.org/10.1242/jeb.124.1.359
L1 - https://journals.biologists.com/jeb/article-pdf/124/1/359/2863461/jexbio_124_1_359.pdf
L2 - https://journals.biologists.com/jeb/article/124/1/359/4876/Ionic-Signalling-by-Growth-Factor-Receptors
L4 - files/31269/Moolenaar_from_Ref_Manager.txt
L4 - files/31271/Moolenaar_from_Ref_Manager.txt
KW - DNA
KW - cells
KW - human
KW - pH
KW - protein
KW - activation
KW - membrane
KW - Ca2+
KW - factor
KW - binding
KW - proliferation
KW - stimulation
KW - Mechanism
KW - channel
KW - plasma membrane
KW - agonists
KW - culture
KW - Growth
KW - In vivo
KW - receptors
KW - cell proliferation
KW - antibodies
KW - Receptor
KW - esters
KW - protein kinase C
KW - DNA synthesis
KW - growth factors
KW - cytoplasmic pH
KW - cell division
ER -

https://s3.amazonaws.com/zotero.org/images/forums/u15617258/tx74kizvlr0bb7m9sls3.png
https://s3.amazonaws.com/zotero.org/images/forums/u15617258/vycm35lgnhmvxxrvafvh.png

adamsmith · 2024-11-03T13:35:44+00:00

You didn't answer the 2nd part of my question about where to import the ID to