3 files changed, 139 insertions, 0 deletions
diff --git a/tests/data/release/fy4tfzhcjnh7rj2r4v2mnyslne b/tests/data/release/fy4tfzhcjnh7rj2r4v2mnyslne
new file mode 100644
index 0000000..cd39efe
--- /dev/null
+++ b/tests/data/release/fy4tfzhcjnh7rj2r4v2mnyslne
@@ -0,0 +1,69 @@
+{
+  "abstracts": [
+    {
+      "content": "Extracellular matrix turnover is initiated, at least in part, by the regulated secretion of members of a family of matrix metalloproteinases. The authors show that interstitial collagenase, stromelysin, two gelatinases (the 72-kD and 92-kD type IV collagenases), and the tissue inhibitor of metalloproteinases (TIMP) are secreted into the culture medium of human retinal pigment epithelium (RPE). These enzymes and their inhibitor were identified by probing immunoblots of western transfers with specific polyclonal antibodies that were made against these proteins or against peptides containing unique sequences from these proteins. Stromelysin and the gelatinases are also active against substrates that are polymerized into polyacrylamide gel before electrophoresis and require metal ions (probably zinc and/or calcium) for activity. The phorbol mitogen, 12-tetradecanoylphorbol-13-acetate, differentially increases the levels of these metalloproteinases and TIMP found in retinal pigment epithelium culture medium with stromelysin and the 92-kD type IV collagenase responding most strongly and TIMP actually decreasing in certain cases. Additional changes in metalloproteinase profiles are observed after approximately 20 passage of several RPE lines in culture. Modulation of extracellular matrix turnover by changing RPE secretion of these matrix metalloproteinases and their TIMP, may play a central role in the normal function and in the pathology of the retina.",
+      "lang": "en",
+      "mimetype": "text/plain",
+      "sha1": "5d75572757018eb696c77b981078987d88e969c7"
+    }
+  ],
+  "container_id": "bktgmrvaorcfle3nbaxcwpsb44",
+  "contribs": [
+    {
+      "extra": {},
+      "given_name": "J P",
+      "index": 0,
+      "raw_affiliation": "Departments of Ophthalmology, Oregon Health Sciences University, Portland, 97201.",
+      "raw_name": "J P Alexander",
+      "role": "author",
+      "surname": "Alexander"
+    },
+    {
+      "extra": {},
+      "given_name": "J M",
+      "index": 1,
+      "raw_name": "J M Bradley",
+      "role": "author",
+      "surname": "Bradley"
+    },
+    {
+      "extra": {},
+      "given_name": "J D",
+      "index": 2,
+      "raw_name": "J D Gabourel",
+      "role": "author",
+      "surname": "Gabourel"
+    },
+    {
+      "extra": {},
+      "given_name": "T S",
+      "index": 3,
+      "raw_name": "T S Acott",
+      "role": "author",
+      "surname": "Acott"
+    }
+  ],
+  "ext_ids": {
+    "pmid": "2176183"
+  },
+  "extra": {
+    "pubmed": {
+      "pub_types": [
+        "Journal Article"
+      ]
+    }
+  },
+  "ident": "fy4tfzhcjnh7rj2r4v2mnyslne",
+  "issue": "12",
+  "language": "en",
+  "pages": "2520-8",
+  "refs": [],
+  "release_stage": "published",
+  "release_type": "article-journal",
+  "release_year": 1990,
+  "revision": "ca69676b-31bb-4900-87f3-4502dd3578d2",
+  "state": "active",
+  "title": "Expression of matrix metalloproteinases and inhibitor by human retinal pigment epithelium",
+  "volume": "31",
+  "work_id": "rjyxwziz2vcj5n4y6t2ofpkd6q"
+}
diff --git a/tests/data/release/n3ijnxlzzbf3tgz44ic2llutja b/tests/data/release/n3ijnxlzzbf3tgz44ic2llutja
new file mode 100644
index 0000000..7998473
--- /dev/null
+++ b/tests/data/release/n3ijnxlzzbf3tgz44ic2llutja
@@ -0,0 +1,69 @@
+{
+  "abstracts": [
+    {
+      "content": "Extracellular matrix (ECM) turnover and remodeling are initiated, at least in part, by the regulated secretion of members of a family of matrix metalloproteinases. Human and bovine trabecular mesh-work in culture secrete interstitial collagenase, both the 72- and the 92-kD forms of type IV collagenase (gelatinases) and stromelysin, and the tissue inhibitor of metalloproteinases (TIMP). These proteinases and TIMP were identified by immunoblotting western transfers from sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) using several specific antiprotein and antipeptide polyclonal antibodies. Gelatinase and stromelysin enzymatic activities were also analyzed by substrate SDS-PAGE, in which proteinase substrates were polymerized into the gels before electrophoresis to allow subsequent activity assays. These matrix metalloproteinases and TIMP are secreted at low basal levels into trabecular culture medium; their secretion levels are increased several-fold by treatment of the cultures with the phorbol mitogen. 12-O-tetradecanoylphorbol-13-acetate (TPA). Characteristics of the trabecular matrix metalloproteinases and TIMP are similar to those secreted by numerous other tissues, including the retinal pigment epithelium. These proteinases may serve an important role in the maintenance and regulation of the trabecular extracellular matrix and, subsequently, of the aqueous humor outflow pathway in normal and glaucomatous eyes.",
+      "lang": "en",
+      "mimetype": "text/plain",
+      "sha1": "ac1d44d0940199d70ff335088dbe0136a82af1b4"
+    }
+  ],
+  "container_id": "bktgmrvaorcfle3nbaxcwpsb44",
+  "contribs": [
+    {
+      "extra": {},
+      "given_name": "J P",
+      "index": 0,
+      "raw_affiliation": "Department of Ophthalmology, School of Medicine, Oregon Health Sciences University, Portland 97201.",
+      "raw_name": "J P Alexander",
+      "role": "author",
+      "surname": "Alexander"
+    },
+    {
+      "extra": {},
+      "given_name": "J R",
+      "index": 1,
+      "raw_name": "J R Samples",
+      "role": "author",
+      "surname": "Samples"
+    },
+    {
+      "extra": {},
+      "given_name": "E M",
+      "index": 2,
+      "raw_name": "E M Van Buskirk",
+      "role": "author",
+      "surname": "Van Buskirk"
+    },
+    {
+      "extra": {},
+      "given_name": "T S",
+      "index": 3,
+      "raw_name": "T S Acott",
+      "role": "author",
+      "surname": "Acott"
+    }
+  ],
+  "ext_ids": {
+    "pmid": "1846130"
+  },
+  "extra": {
+    "pubmed": {
+      "pub_types": [
+        "Journal Article"
+      ]
+    }
+  },
+  "ident": "n3ijnxlzzbf3tgz44ic2llutja",
+  "issue": "1",
+  "language": "en",
+  "pages": "172-80",
+  "refs": [],
+  "release_stage": "published",
+  "release_type": "article-journal",
+  "release_year": 1991,
+  "revision": "1a505fdc-87a2-4848-ae60-1385eeee3eb9",
+  "state": "active",
+  "title": "Expression of matrix metalloproteinases and inhibitor by human trabecular meshwork",
+  "volume": "32",
+  "work_id": "evvvpozkofh4vbwlx7wbgpilni"
+}
diff --git a/tests/data/verify.csv b/tests/data/verify.csv
index 2480a9e..1ade260 100644
--- a/tests/data/verify.csv
+++ b/tests/data/verify.csv
@@ -250,3 +250,4 @@ bhrbuu3sijgtpbu4nsquk3ykba,vfdeyz6khrflxivy5n2byocmjy,,
 5b7dlm6ux5gppon3f2s5jj7sr4,zyv5tpidcza33kkc5dn3lxrbd4,,
 45kgugyzbzadjmkqi5l6lekxq4,dgbgkxqihjgelpdaghsnxoybmm,Status.EXACT,TITLE_AUTHOR_MATCH
 ixktsx5gmnbonl5zxubhxhfgya,q5yheygzs5fxnahqihwejepn6u,Status.STRONG,SLUG_TITLE_AUTHOR_MATCH
+n3ijnxlzzbf3tgz44ic2llutja,fy4tfzhcjnh7rj2r4v2mnyslne,Status.AMBIGUOUS,UNKNOWN