Unhandled tags when importing from Zotero RIS file

Bug report:
I tried importing references from an RIS file that I exported directly from the Zotero web interface. I got a number of errors, listed below. The most important error was that the field “T2” (the journal title) was being imported as the reference title, and so any other references in the same journal were not imported (since the title must be unique, I assume).

An example of the Zotero RIS file import is below, and the fields that were not recognised were:

AB (abstract)
DA (not important - to me)
DO (doi)
DP (not important - to me)
J2 (journal abbreviation)
ST (short title)

Further, ISBN numbers were not imported correctly – leading zeros were stripped, and only the first half of the ISBN up to the hyphen was included. For example, ISBN 0022-2836 was imported as 22.

Foreign characters in author names were not recognised. For example: Taştan was imported as Ta?tan

And finally, some journals using (for example) Pt 2 or Suppl 3A instead of a simple number for issue number was not imported to the Issue number field correctly.

Example file:

TY  - JOUR
TI  - Oligomeric structure of nitrilases: effect of mutating interfacial residues on activity
AU  - Sewell, B T
AU  - Thuku, R N
AU  - Zhang, X
AU  - Benedik, M J
T2  - Annals of the New York Academy of Sciences
AB  - Nitrilases are important industrial enzymes that convert nitriles into their corresponding acids or, occasionally, amides. Atomic resolution structures of four members of the nitrilase superfamily have been determined, but these differ from microbial nitrilases in that they do not form typical large homo-oligomeric complexes. At least two nitrilases, the cyanide dihydratases from Pseudomonas stutzeri AK61 and Bacillus pumilus C1, form unusual spiral structures of 14 and 18 subunits, respectively. Evidence suggests that the formation of the spiral structure is essential for activity. Sequence analysis reveals that the nitrilases differ from the nonspiral-forming homologs by two insertions of between 12 and 14 amino acids and a C-terminal extension of up to 35 amino acids. The insertions are positioned at an intermolecular interface in the spiral and probably contribute to its formation. The other interfaces responsible for the formation and/or stabilization of the spirals can also be identified. Comparative structure modeling enables identification of the residues involved in these interacting surfaces, which are remote from the active site. Mutation of these interacting residues usually leads to loss of activity. The effect of the mutations on activity in most cases can be rationalized in terms of a possible effect on spiral formation.
DA  - 2005/11//
PY  - 2005
DO  - 10.1196/annals.1352.025
DP  - NCBI PubMed
VL  - 1056
SP  - 153
EP  - 159
J2  - Ann. N. Y. Acad. Sci.
SN  - 0077-8923
ST  - Oligomeric structure of nitrilases
KW  - Amino Acid Sequence
KW  - Aminohydrolases
KW  - Bacillus
KW  - Bacterial Proteins
KW  - Kinetics
KW  - Models, Molecular
KW  - Molecular Sequence Data
KW  - Mutagenesis, Site-Directed
KW  - Protein Conformation
KW  - Pseudomonas stutzeri
KW  - Recombinant Proteins
ER  -

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