Full-text prior art and chemical structure searching in e-journals and on the internet - A patent information professional's perspective

In depth analysis of non-patent literature prior art is a crucial step in checking patentability of new inventions and validity of competitor's patents, since by patent law relevant subject matter disclosed in non-patent literature is as important as any patent document. E-journal articles, as well as any scientific and technical information published on the web are an important source of prior art that is very often insufficiently covered and indexed by commercial databases. This article reviews search and display capabilities of e-journal search sites of different publishers and hosts, as well as their value for full-text prior art analysis to enhance retrieval from commercial databases. Moreover, current developments and future prospects of chemical structure searching both in e-journals and on the internet are discussed.Non-patent literature Full-text searching Prior art Patentability Novelty Validity E-journals Chemical structure searching Chemical identifier InChI Chemical data mining

An alternative amino-terminus expressed in the central nervous system converts agrin to a type II transmembrane protein

Agrin is a basal lamina-associated heparansulfate proteoglycan that is a key molecule in the formation of the vertebrate neuromuscular junction. The carboxy-terminal part of agrin is involved in its synaptogenic activity. The amino-terminal end of chick agrin consists of a signal sequence, required for the targeting of the protein to the secretory pathway, and the amino-terminal agrin (NtA) domain that binds to basal lamina-associated laminins. The cDNA encoding rat agrin lacks this NtA domain and instead codes for a shorter amino-terminal end. While the NtA domain is conserved in several species, including human, sequences homologous to the amino-terminus of rat agrin have not been described. In this work, we have characterized these amino-terminal sequences in mouse and chick. We show that they all serve as a noncleaved signal anchor that immobilizes the protein in a N(cyto)/C(exo) orientation in the plasma membrane. Like the secreted form, this transmembrane form of agrin is highly glycosylated indicative of a heparansulfate proteoglycan. The structure of the 5' end of the mouse agrin gene suggests that a distinct promoter drives expression of the transmembrane form. Agrin transcripts encoding this form are enriched in the embryonic brain, particularly in neurons. To our knowledge, this is the first example of a molecule that is synthesized both as a basal lamina and a plasma membrane protein