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

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

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

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

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

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

Manipulation of Chain Conformation for Optimum Charge-Transport Pathways in Conjugated Polymers

A pair of different diketopyrrolopyrrole-based conjugated polymers (CPs) were designed and synthesized to investigate the effect of chain conformation on their molecular assembly. Conformation management was achieved by the incorporation of different linkers during polymerization. Through the use of computational calculations and UV–vis absorption measurements, the resulting CPs (PDPP-T and PDPP-BT) were found to exhibit partly modulated chain geometry. Grazing incident X-ray diffraction experiments with a two-dimensional detector revealed that PDPP-T having a planar chain conformation exhibited an edge-on type molecular arrangement, which evolved to a face-on type chain assembly when the planar geometry was altered to a slightly twisted one as in PDPP-BT. In addition, it was verified that the directional electric carrier mobility of CPs was critically distinguished by the distinctive chain arrangement in spite of their similar chemical structure. Concentration-dependent absorption measurements could provide an improved understanding of the assembly mechanism of CP chains: the planar conformation of PDPP-T facilitates the formation of preassembled chains in a concentrated solution and further directs the edge-on stacking, while the twisted dihedral angle along the benzothiophene in PDPP-BT prevents chain assembly, resulting in the face-on stacking. Because CP chain conformation is inevitably connected with the generation of preassembled chains, manipulating CP geometry could be an efficient tool for extracting an optimum chain assembly that is connected with the principal charge-transport pathway in CPs