Disease relevance of PHF12

• This structure has tightly interwound phosphate backbones and exposed bases in common with Pauling's early DNA structure [Pauling, L. & Corey, R. B. (1953), Proc. Natl. Acad. Sci. USA 39, 84-97] and an unusual structure proposed for the Pf1 bacteriophage [Liu, D. J. & Day, L. A. (1994) Science 265, 671-674] [1].
• When tested in vivo in a 3-day-established human squamous carcinoma nude mouse xenograft model, the PF1/D-DAVLBHYD conjugate eliminated tumor growth with three injections (days 3, 6, and 9) at 2 mg/kg Vinca content [2].
• Group 1 antibodies are also reactive with some lung adenocarcinomas and, with the exception of PF1/E, stain certain differentiated strata within normal adult plantar and fetal epidermis [3].
• The relations between the protein coats and DNAs of the four filamentous bacteriophages fd, Xf, Pf1, and Pf3 are considered [4].
• In an application to the Pf1 filamentous bacterial virus, it is shown that the Raman amide I band contains no component other than that due to alpha-helix, indicating the virtual 100% helicity of coat proteins in the native virion [5].

High impact information on PHF12

• Two factors, termed PF1 and PF2, are required for specific polyadenylation of the cleaved RNA [6].
• In vitro footprinting and quantitative gel shift analyses showed that PF1 binds preferentially to the PE1 element but also at lower affinity to two other AT-rich regions upstream of PE1 [7].
• PF1: an A-T hook-containing DNA binding protein from rice that interacts with a functionally defined d(AT)-rich element in the oat phytochrome A3 gene promoter [7].
• We identified a novel mSin3A-interacting protein that has two plant homeodomain (PHD) zinc fingers we term Pf1, for PHD factor one [8].
• These findings establish the Pf1 polybasic region as a phosphoinositide-binding module and suggest that the PHD domains function down-stream of phosphoinositide signaling triggered by the interaction between polybasic regions and phosphoinositides [9].

Biological context of PHF12

• Each of the three antibodies used was specific for one fragment and peptide mapping of PF1 and PF2 showed that there was no significant amino acid sequence overlap [10].
• The evidence indicates therefore that PF1 and GT-2 do not perform functionally equivalent roles in positively regulating oat and rice PHYA gene expression [11].
• The ROA spectra of Pf1 at temperatures above and below that at which a structural transition is known to occur (approximately 10 degrees C) reveal little difference in the protein conformation between the two forms, but there are indications of changes in DNA structure [12].
• We suggest, therefore, that the pO2 clone may encode the putative nuclear factor, oat PF1, that is involved in positive regulation of PHYA3 by binding to PE1 in vivo. pO2 encodes a 170-amino-acid-long protein that contains three repeats of the 'AT-hook' DNA-binding motif found in high mobility group I-Y (HMGI-Y) proteins [13].
• Measurements are demonstrated for a 24-nt stem-loop RNA sequence, uniformly enriched in (13)C, and aligned in Pf1 [14].

Anatomical context of PHF12

• Five independent cDNA clones were isolated from preovulatory follicles (PF1, PF11, PF13, PF14, PF15) and six from the corpus luteum (CL1, CL6, CL7, CL8, CL12, CL13) [15].
• The percentage recovery of TNC and MNC in PF1 was influenced by the volume of the collected cord blood, especially with use of the filtration procedures [16].
• The primed in situ (PRINS) labeling technique has been used for the interphase cytogenetic investigation of 3 colon cancer cell lines (Caco-2, TC7 and PF1 1) derived from a same primary tumor [17].

Associations of PHF12 with chemical compounds

• Electron microscope pictures of rotary-shadowed PF1 and PF2 showed them to be short rod-shaped molecules while PF3 has a crab-like appearance and seems to be an aggregate of several fibrillin chain fragments [10].
• Prothrombin (1-3 microM) and PF1.2 (but not PF1) in the presence of CaCl2 (2 mM) were able to replace HK (45 nM) in the presence of ZnCl2 (25 microM) as a cofactor for the specific, reversible, high-affinity (Kd approximately 25 nM) binding of factor XI to 947 +/- 150 sites per platelet [18].
• High-resolution 1H and 15N NMR experiments are used to characterize the structure and dynamics of residues 30-40 in the hydrophobic midsection of Pf1 coat protein in sodium dodecyl sulfate micelles [19].
• The results of simulations of several alanine based 46 residue polypeptides with some of the charged residues present in the Pf1 coat protein sequence suggest that interactions between the Asp 14 and Asp 18 sidechains and the peptide backbone are responsible for the formation of the mobile loop.(ABSTRACT TRUNCATED AT 250 WORDS)[20]
• The role of tyrosine residues in the DNA-binding site of the Pf1 gene 5 protein [21].

Analytical, diagnostic and therapeutic context of PHF12

• Antitumor xenograft activity with a conjugate of a Vinca derivative and the squamous carcinoma-reactive monoclonal antibody PF1/D [2].
• The altered pilin gene was transferred into wild-type PAO by recombination, where it did not affect normal piliation as observed by transmission electron microscopy or change of sensitivity to f116, PO4, B9, and Pf1 pilus-specific bacteriophages [22].
• Two proteins, named Pf1 and Pf2, were eluted in 0.1 and 0.2M of salt, respectively, and submitted to reverse-phase chromatography in HPLC [23].
• RESULTS: The median PF1 percentage recovery of total nucleated cells (TNC) was comparable with both traditional methods (HES 79%, T&B 86%) and statistically reduced with both filtration procedures (filter A 58%, filter B 61%) [16].
• In the control group, both 6-keto PF1 alpha and PGE2 showed only a slight increase both during and after the operation [24].

References