MRI axial sequential T2 views of patient 1.

<p>Pre-treatment MRI scans of patient 1 (A [sequential image: 3/16], C [4/16], and E [5/16]) show retro-patellar signal changes (arrow) consistent with chondromalacia patellae (upper bone). At three months, post-treatment MRI scans of patient 1 (B [6/20], D [7/20], and F [8/20]) show changes (arrowhead) consistent with probable cartilage restoration on the patellae-femoral joint.</p

Pain measurements of patients 1 (A), 2 (B), and 3 (C).

<p>VAS is visual analog scale and T bars indicate standard deviations.</p

MRI axial sequential T2 views patient 3.

<p>Pre-treatment MRI scans of patient 3 (A [4/19], C [5/19], and E [6/19]) show retro-patellar signal changes (arrow) consistent with chondromalacia patellae along with medial meniscal maceration and cartilage thinning consistent with osteoarthritis. Post-treatment MRI scans at three months (B [5/20], D [6/20], and F [7/20]) show changes (arrowhead) consistent with probable cartilage restoration.</p

MRI axial sequential T2 views of patient 2.

<p>Pre-treatment MRI scans of patient 2 (A [16/24], C [17/24], E [18/24]) show retro-patellar signal changes (arrow) consistent with chondromalacia patellae (upper bone). At three months, post-treatment MRI scans of patient 2 (B [right; 4/20], D [5/20], and F [6/20]) show changes (arrowhead) consistent with probable cartilage restoration on the patellae-femoral joint.</p

Epidemiology and characteristics of class C extended-spectrum β-lactamases (cESBLs)

*<p>Crystallographic structures from distinct GC1 (Protein Data Bank [PDB] code 1GCE) and CMY-10 (PDB code 1ZKJ) only have been resolved. Ser^R is the in vitro site-directed mutant of SLS73 (Ser^S). All enzymes except plasmid-encoded CMY-10 and CMY-19 are chromosomal cESBLs. All enzymes except several enzymes (Ser^R, Ser^S, AmpC^R, AmpC1 [in vitro Leu-293-Pro mutant of P99], seven mutants of CMY-2, MHN-7.6, and 520R) are the naturally (clinically) occurring cESBLs produced by clinical isolates. AmpC^D is the only inhibitor-(tazobactam and sulbactam)sensitive cESBL.</p>†<p>CAZ, ceftazidime; CTX, cefotaxime; CMX, cefmenoxime; CRO, ceftriaxone; FEP, cefepime; FPI, cefpirome; IMP, imipenem; ATM, aztreonam. Each cESBL has extended its substrate specificity in comparison with each parent enzyme (non-cESBL).</p>‡<p>Ω-loop lays from residues 189 to 226 in P99 β-lactamase. R2-loop lays from residues 289 to 307 in CMY-10 β-lactamase. The position of the N-terminal amino acid of the mature enzyme (without the respective signal peptide) is designated as position 1 of the amino acid sequence. The tripeptide deletion of AmpC^D is located just before the R2-loop but causes a structural change in the R2-loop. Glu₂₁₃ → Lys, the substitution of glutamic acid (Glu) by lysine (Lys) at residue 213.</p

Ribbon diagram of crystallographic structure of CMY-10 (a cESBL).

<p>The image was rendered with PyMOL, available on the Internet (<a href="http://sourceforge.net/projects/pymol" target="_blank">http://sourceforge.net/projects/pymol</a>). The R2-loop is represented as red, while the Ω-loop, H-2 helix, and H-11 helix are depicted in violet, blue, and cyan, respectively. The R1 active site (central upper region) is surrounded by the Ω-loop and the R2 active site (central lower region) by the R2-loop and H-11 helix. The nucleophile (Ser65), attacking the carbonyl carbon of β-lactam ring, is present in the H-2 helix.</p

Microscopic and nPCR-based diagnosis of <i>Plasmodium</i> infections in clinical isolates showing different number of patients infected by <i>P</i>. <i>vivax</i>, <i>P</i>. <i>falciparum</i>, and mixed species (double infections with <i>P</i>. <i>falciparum</i> and <i>P</i>. <i>vivax</i>).

<p><i>P</i>. <i>vivax</i> was found to be the most prevalent species.</p

Graphical summary of attributable fractions of malarial infections caused by <i>P</i>. <i>vivax</i> (A) and <i>P</i>. <i>falciparum</i> (B) in different age groups of malarial patients.

<p>Data are presented as histograms (left panel with curve showing the pattern of <i>Plasmodium</i> infection incidence in different age groups), and box and whisker plots (right panel) showing median (□), lower quartile, upper quartile, outliers (○), and extreme score (*) of their respective sample distributions.</p

Geographical location of sample collection site (Orakzai Agency: black area) in FATA, Pakistan.

<p>FATA (gray): Federally Administered Tribal Areas, KPK: Khyber Pakhtunkhwa, AK: Azad Kashmir.</p

n‑MoS₂/p-Si Solar Cells with Al₂O₃ Passivation for Enhanced Photogeneration

Molybdenum disulfide (MoS₂) has recently emerged as a promising candidate for fabricating ultrathin-film photovoltaic devices. These devices exhibit excellent photovoltaic performance, superior flexibility, and low production cost. Layered MoS₂ deposited on p-Si establishes a built-in electric field at MoS₂/Si interface that helps in photogenerated carrier separation for photovoltaic operation. We propose an Al₂O₃-based passivation at the MoS₂ surface to improve the photovoltaic performance of bulklike MoS₂/Si solar cells. Interestingly, it was observed that Al₂O₃ passivation enhances the built-in field by reduction of interface trap density at surface. Our device exhibits an improved power conversion efficiency (PCE) of 5.6%, which to our knowledge is the highest efficiency among all bulklike MoS₂-based photovoltaic cells. The demonstrated results hold the promise for integration of bulklike MoS₂ films with Si-based electronics to develop highly efficient photovoltaic cells