PMID:1346131(https://pubmed.ncbi.nlm.nih.gov/1346131/) reconstitutes mammalian Hsp60/Hsp10 substrate folding with MgATP; PMID:25918392(https://pubmed.ncbi.nlm.nih.gov/25918392/), DOI 10.1073/pnas.1411718112, solves the human type I chaperonin complex. These establish the distinction from the cytosolic type II TRiC/CCT system, independently of an AI review or ARBA.
Horse F6Z587 has 541 residues versus 573 for human P10809, with an internal deletion of human 171–202. The N-terminal mitochondrial precursor and annotated ATP-binding positions are conserved. Broad ATP binding and mitochondrial targeting remain reasonable inferences, but full ATP-dependent folding competence is uncertain for this model. The existing horse ARBA GO:0005832 TRiC-complex annotation is wrong at family/complex level regardless of whether this deletion preserves Hsp60 activity.
PMID:17823127(https://pubmed.ncbi.nlm.nih.gov/17823127/) shows that cytosolic Hsp60 can promote death or survival in different apoptotic systems, with different caspase-3 interactions. Do not remove opposing apoptotic-direction annotations solely because they share a reference. Immune responses to extracellular preparations require their own preparation/contamination and receptor-dependence controls; those rows remain UNDECIDED rather than being accepted as a universal Hsp60 cytokine activity or rejected from localization alone.
A completed human Falcon report has been inspected. The selected horse record is unreviewed; the initial literature search did not identify a targeted horse HSPD1 mechanistic experiment warranting a separate horse Edison report.
The completed Falcon report identifies PMID:32317635(https://pubmed.ncbi.nlm.nih.gov/32317635/), DOI:10.1038/s41467-020-15698-8, which establishes active single- and double-ring human Hsp60–Hsp10 assemblies. It also identifies PMID:31444388(https://pubmed.ncbi.nlm.nih.gov/31444388/), DOI:10.1038/s41598-019-48762-5, on impaired client refolding by disease variants. These primary identities were independently verified. ATP turnover and productive folding are distinct readouts, strengthening the caution about the selected horse deletion. The earlier manual synthesis is retained as separately labeled primary-source analysis.
All 178 annotation rows were screened. The previous blanket immune UNDECIDED rationale overlooked explicit primary controls: PMID:15371451 separates endotoxin-dependent macrophage TNF effects from retained T-cell costimulation using low-endotoxin human and eukaryotically expressed Hsp60; PMID:16148103 uses human Hsp60 on mouse B cells and reports TLR4/MyD88 dependence and LPS controls; PMID:17164250 directly tests LPS binding and distinguishes LPS-associated and IFN-alpha-associated immune effects; PMID:18256040 tests endotoxin-free costimulation. These support context-specific non-core immune annotations, not a universal cytokine activity. PMID:10663613 independently supports tumor-surface immune recognition. The vertebrate IBA node PTN002900230 includes human HSPD1 experimental grounding; that is not circular support. Detailed IgG-switch and stable LPS-receptor-complex claims remain UNDECIDED where the retrieved experiments do not resolve those precise assertions.
The ISS DNA-binding donor is yeast Hsp60/P19882, with real gel-shift/crosslinking evidence in PMID:10869431; human origin-specific/nucleoid conservation remains uncertain. The cold-response donor is chicken Q5ZL72 with PMID:23636703, not an unresolved horse experiment. The human RNA HDA observation is retained as non-core; the exact HSPD1 dsRNA entry from PMID:21266579 still needs table/supplement recovery and is not rejected from a Raftlin-focused title. Hsp60-p53/survivin statements now cite their own PMID:18086682 experiment.
The inner-membrane IBA PTN000143509 remains compatible with a principal matrix pool. The import IBA PTN000143510 is separately UNDECIDED: PMID:1347713 reports antifolding/export of cytochrome b2, whereas PMID:7911803 finds stop-transfer sorting of cytochrome-b2-presequence fusion proteins without Hsp60 exposure. A neutral OpenScientist request will assess substrate/route differences and human conservation. Neither matrix localization nor a single yeast donor refutes participation. Generic protein binding is removed for informativeness without denying its interaction evidence.