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This archive includes all raw data and R code to reproduce the analysis for the paper: 'Drought, fire and rainforest endemics: a case study of two threatened frogs impacted by Australia’s ‘Black Summer’' submitted to Ecology and Evolution, December 2022.

Supplemental material, sj-pdf-1-cjk-10.1177_20543581221103682 for Use of Guideline-Based Therapy for Diabetes, Coronary Artery Disease, and Chronic Kidney Disease After Acute Kidney Injury: A Retrospective Observational Study by Sunchit Madan, Patrick A. Norman, Ron Wald, Javier A. Neyra, Alejandro Meraz-Muñoz, Ziv Harel and Samuel A. Silver in Canadian Journal of Kidney Health and Disease

Additional file 1: Table S1. Carotid plaque variables at baseline and month 6 between arms. Table S2. Change in clinical and blood characteristics from baseline to month 6. Table S3. Stratified sub-analysis of area stenosis percent change between arms.

Supplementary Digital Content 1: Definitions of nosocomial infections. Supplementary Digital Content 2: Multivariate analysis.

Supplemental material, CJK-Supplemental_material for Polysulfonate Resins in Hyperkalemia: A Systematic Review by Sheung Wing Sherwin Wong, Grace Zhang, Patrick Norman, Hasitha Welihinda and Don Thiwanka Wijeratne in Canadian Journal of Kidney Health and Disease

Die NMR-Spektroskopie zeichnet sich bei der Charakterisierung von Proteinen besonders darin aus, dass sie es erlaubt, das Verhalten von Proteinen bei Änderungen der Umgebungsbedingungen oder Wechselwirkungen mit anderen Molekülen im atomaren Detail zu verfolgen. In der vorliegenden Arbeit wurde die Kombination von hochauflösender NMR-Spektroskopie mit der Anwendung von hohem hydrostatischen Druck dazu genutzt, Faltungsintermediate des menschlichen Prionproteins (PrP) zu stabilisieren und zu charakterisieren. Zudem wurde die Wechselwirkung von Proteinen mit anderen Proteinen und kleinen Liganden NMR-spektroskopisch charakterisiert. Es wurde die Bindung von Proteinen und Lipiden an die PDZ2-Domäne der Phosphatase PTP-Bas sowie die Wechselwirkung des Proteins HPr mit dem Enzym HPrK/P im Detail analysiert., NMR spectroscopy is a powerful tool to study protein structures, functions and dynamics in atomic detail. With NMR spectroscopy it is possible to do this even while changing physico-chemical conditions or while the protein interacts with other molecules. Here the combination of high resolution NMR spectroscopy with the application of high hydrostatic pressure is used to stabilize and characterize folding intermediates of the human prion protein (PrP). Furthermore the interactions of proteins with other proteins and small ligands are characterized by NMR spectroscopy. The binding of proteins and phosphoinositides by the PDZ2 domain of the human tyrosine phosphatase PTP-Bas as well as the interaction of the protein HPr with the enzyme HPrK/P was studied in detail.