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1. The femora of Drepanosauromorpha ( Reptilia : Diapsida ): Implications for the functional evolution of the thigh of Sauropsida

   https://doi.org/10.1002/ar.25160  

   Pritchard, Adam C.; Irmis, Randall B.; Olori, Jennifer C.; Nesbitt, Sterling J.; Smith, Nathan D.; Stocker, Michelle R.; Turner, Alan H. (February 2023, The Anatomical Record)

   The femora of diapsids have undergone morphological changes related to shifts in postural and locomotor modes, such as the transition from plesiomorphic amniote and diapsid taxa to the apomorphic conditions related to a more erect posture within Archosauriformes. One remarkable clade of Triassic diapsids is the chameleon-like Drepanosauromorpha. This group is known from numerous articulated but heavily compressed skeletons that have the potential to further inform early reptile femoral evolution. For the first time, we describe the three-dimensional osteology of the femora of Drepanosauromorpha, based on undistorted fossils from the Upper Triassic Chinle Formation and Dockum Group of North America. We identify apomorphies and a combination of character states that link these femora to those in crushed specimens of drepanosauromorphs and compare our sample with a range of amniote taxa. Several characteristics of drepanosauromorph femora, including a hemispherical proximal articular surface, prominent asymmetry in the proximodistal length of the tibial condyles, and a deep intercondylar sulcus, are plesiomorphies shared with early diapsids. The femora contrast with those of most diapsids in lacking a crest-like, distally tapering internal trochanter. They bear a ventrolaterally positioned tuberosity on the femoral shaft, resembling the fourth trochanter in Archosauriformes. The reduction of an internal trochanter parallels independent reductions in therapsids and archosauriforms. The presence of a ventrolaterally positioned trochanter is also similar to that of chameleonid squamates. Collectively, these features demonstrate a unique femoral morphology for drepanosauromorphs, and suggest an increased capacity for femoral adduction and protraction relative to most other Permo-Triassic diapsids. 

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2. The Movement Ecology of Mutualism ( CSEE / ESA 2022, OOS17 )

   https://doi.org/10.1002/bes2.2063  

   Moore, Christopher M.; Shaw, Allison K.; Bruninga‐Socolar, Bethanne; Caves, Eleanor M.; Karnish, Alex T.; Kiesewetter, Kasey N.; Nelson, Annika S.; Pringle, Elizabeth G. (April 2023, The Bulletin of the Ecological Society of America)
3. Unwinding the roles of RNA helicase MOV10

   https://doi.org/10.1002/wrna.1682  

   Nawaz, Aatiqa; Shilikbay, Temirlan; Skariah, Geena; Ceman, Stephanie (March 2022, WIREs RNA)
4. Structural insights into the Pseudomonas aeruginosa ClpP1 • ClpP2 heterocomplex and its interactions with the AAA + ClpX unfoldase

   https://doi.org/10.1002/pro.70310  

   Ghanbarpour, Alireza; Zhang, Jia Jia; Davis, Joseph H; Baker, Tania A; Sauer, Robert T (October 2025, Protein Science)

   Abstract ClpXP and other AAA+ proteases play central roles in bacterial proteostasis by degrading misfolded and regulatory proteins. InPseudomonas aeruginosa, ClpXP consists of the ClpX unfoldase and ClpP peptidase, which influence critical adaptive processes contributing to stress resistance.P. aeruginosa^PaClpP1 and^PaClpP2 paralogs assemble into homomeric (^PaClpP1•ClpP1) and heteromeric (^PaClpP1•ClpP2) complexes.^PaClpP2 is only active in the^PaClpP1•ClpP2 heterocomplex. Here, we present a cryo‐EM structure of^PaClpX•ClpP1•ClpP2, revealing how^PaClpX binds^PaClpP1, which in turn interacts with^PaClpP2. Comparison of the active heterocomplex with an inactive^PaClpP2 crystal structure shows that^PaClpP1 binding induces conformational changes in^PaClpP2, stabilizing an active catalytic triad. Differences in^PaClpP1 and^PaClpP2 substrate‐binding residues and an unstructured ClpP2 N‐terminal segment that protrudes into the peptidase chamber likely contribute to distinct peptide‐cleavage specificities of^PaClpX•ClpP1•ClpP2 and^PaClpX•ClpP1•ClpP1. Given the role of^PaClpP1•ClpP2 in biofilm formation and virulence, these structural insights may provide a foundation for developing selective inhibitors to combatP. aeruginosainfections. 

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5. Transmission‐dynamics models for the SARS Coronavirus‐2

   https://doi.org/10.1002/ajhb.23512  

   Jones, James Holland; Hazel, Ashley; Almquist, Zack (September 2020, American Journal of Human Biology)

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