Distribution frequency of <i>CA9</i> genotypes in 221 controls and 221 patients with urothelial cell carcinoma.

<p>% confidence intervals (CIs) were estimated by logistic regression models. The adjusted odds ratios (AORs) with their 95% confidence intervals (CIs) were estimated by multiple logistic regression models after controlling for age and gender. * p value < 0.05 as statistically significant. The odds ratios (ORs) and with their 95</p

Functional implication and <i>In silico</i> profiling of ADAMTS14 SNP rs12774070.

<p><b>(A)</b> ADAMTS14 displays a significant eQTL association with rs12774070 genotypes in esophagus mucosa tissues (GTEx data set). (<b>B</b>) The altered residue is conserved throughout three procollagen aminopropeptidase subfamily of ADAMTS proteases, including ADAMTS2 (NP_055059.2), ADAMTS3 (NP_055058.2) and ADAMTS14 (NP_631894.2), as shown by alignment of the protein sequences with Crustal Omega software. Numbering is for human ADMDTS14. The arrow represents b-strands, and consensus sites for N-liked oligosaccharide attachment are marked in red (pinpointed). The disulfide bonds are marked in dark lines connecting paired cysteines. (<b>C</b>) Schematic representation of the full-length human ADMDTS14 protein, domain symbols are drawn approximately to scale. The rectangles represent the key domain structures, ZnMc superfamily (cd04273; pink), ADAM spacer1 (pfam05986; green) and four TSR1 (smart00209; yellow) by NCBI CDD server. Putative furin cleavage site is indicated by an arrowhead, and N-linked glycosylation sites are pointed by pins. (<b>D</b>) Ribbon diagram depicts the homology model of TSR1 (3) domain of ADAMTS14. The ribbon indicates the Cα carbon of the TSR1 domain characterized in this study. The blue ribbon, purple sphere, green spheres and yellow sticks indicate the b-strands structure, SNP rs12774070, potential N-linked glycosylation site and disulfide bonds, respectively. (<b>E</b>) Pathogenicity prediction of ADAMTS14 SNPs assessed in this study.</p

The distributions of demographical characteristics and clinical parameters in 708 controls and 354 patients with HCC.

<p>The distributions of demographical characteristics and clinical parameters in 708 controls and 354 patients with HCC.</p

<i>ADAMTS14</i> gene polymorphisms assessed in this study.

<p><i>ADAMTS14</i> gene polymorphisms assessed in this study.</p

Odds ratio (OR) and 95% confidence interval (CI) of clinical status and <i>WWOX</i> rs11545028 genotypic frequencies in 354 HCC patients.

<p>Odds ratio (OR) and 95% confidence interval (CI) of clinical status and <i>WWOX</i> rs11545028 genotypic frequencies in 354 HCC patients.</p

Structural characterization and SNP (rs12918952) in human WWOX protein (NP_057457.1).

<p>Alignments of conserved domain-based sequences of (A) two conserved tryptophans domain (WW; cd00201) and (C) classical-like SDR domain (human_WWOX-like_SDR_c-like; cd09809) by use of multiple sequence alignment format and numbered according to the human WWOX is shown above the sequences. Strick consensus amino acids in the putative active centers of compact structural units are shown: the key amino acids of active site and cofactor binding site are highlighted in red star and blue pound signs, respectively. The WWOX-relative sequences are as follows: human (<i>H</i>. <i>sapiens</i>, NP_057457.1); mouse (<i>M</i>. <i>musculus</i>, NP_062519.2); chicken (<i>G</i>. <i>gallus</i>, NP_001025745.1); fish (<i>D</i>. <i>rerio</i>, NP_957207.1) and fly (<i>D</i>. <i>melanogaster</i>, NP_609171.1). (B) Schematic representation of the overall human WWOX protein; domain symbols are drawn approximately to scale. The rectangle represents the WW and human_WWOX-like_SDR_c-like domain; the key residues of active site and cofactor binding site are highlighted in red and triangle sign, respectively. The N-terminal and C-terminal ends are indicated (N’ and C’, respectively). (D) Ribbon diagram showing the homologous 3D model of the SDR_c-like domain of human WWOX using the SWISSMODEL server based on <i>M</i>. <i>abscessus</i> short chain dehydrogenase or reductase crystal structure (PDB ID: 3RIH). The side chains of the amino acids characterized catalytic tetrad of Asn232-Thr266-Tyr293-Lys297 are shown as sticks and labeled which aligned well with the ‘classical’ type of short-chain dehydrogenase/reductase (SDR) enzyme. The blue spheres represent the putative coenzyme NAD (P)-binding pocket is drawn to illustrate the location of the cofactor binding site. The ribbons indicate the backbone course of human WWOX and the arrows represent b-strands, and cylinders indicate a-helices. The figure was prepared using ViewerLite^™ 5.0 software. (E) Expression quantitative trait locus association between rs12918952 genotype and WWOX expression in whole blood (GTEx data set). Numbers in parentheses indicate the number of cases.</p

Associations of combined effects of <i>ADAMTS14</i> genotypic frequencies and betel nut chewing with oral cancer among 1401 smokers.

<p>Associations of combined effects of <i>ADAMTS14</i> genotypic frequencies and betel nut chewing with oral cancer among 1401 smokers.</p

Distribution frequency of the clinical status and <i>CA9</i> rs1048638 genotype frequencies in 221 patients with urothelial cell carcinoma with non-smoker and smoker.

<p>Distribution frequency of the clinical status and <i>CA9</i> rs1048638 genotype frequencies in 221 patients with urothelial cell carcinoma with non-smoker and smoker.</p

Association of <i>WWOX</i> genotypic frequencies with HCC laboratory status.

<p>Association of <i>WWOX</i> genotypic frequencies with HCC laboratory status.</p

Distribution frequency of the clinical status and <i>CA9</i> rs1048638 genotype frequencies in 221 patients with urothelial cell carcinoma.

<p>Distribution frequency of the clinical status and <i>CA9</i> rs1048638 genotype frequencies in 221 patients with urothelial cell carcinoma.</p