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Additional file 2.

Additional file 3.

Additional file 4.

Supplemental material, sj-docx-1-jet-10.1177_15266028221079772 for Early Clinical Outcomes of Initial Launch of the Zenith Alpha Abdominal Endovascular Graft in Japan by Naoki Fujimura, Shigeo Ichihashi, Hideaki Obara, Toshihisa Asakura, Masatoshi Komooka, Seiji Onitsuka, Yoshihiko Kurimoto, Hiroaki Kato and Takao Ohki in Journal of Endovascular Therapy

Additional file 1. Supplemental figures.

Additional file 1: Figure S1. Fission yeast Hsp70 proteins and their homologs. (A) Phylogenic tree of Hsp70 proteins. Scale-bar unit indicates the number of amino acid substitutions per site. Names of proteins are associated with two-letter abbreviations and color-coded to indicate the species: “sp” for Schizosaccharomyces pombe (red), “sc” for Saccharomyces cerevisiae (black), and “dm” for Drosophila melanogaster (blue). (B) Domain structure of Hsp70 proteins. Protein names are depicted as in (A) and their amino acid lengths are shown. Protein domains are drawn as boxes according to the CATH-Gene3D classification. The N-terminal ATPase domains (ATPase) are composed of three internal domains that belong to the CATH superfamilies 3.30.420.40, 3.30.30.30, and 3.90.640.10. Substrate-binding domains (SB) belong to the 2.60.34.10 superfamily. The C-terminal lid domains (Lid) belong to the 1.20.1270.10 superfamily. Predicted localization signals for mitochondria (TargetP-M) and for the endoplasmic reticulum or beyond (TargetP-S) are shown as shaded boxes. Locations of the proteins in the cell are indicated. For clarity, D. melanogaster Hsp70 proteins other than Hsc70-4 are omitted. Figure S2. Hsp40 family proteins in fission yeast. Domain structure of all 26 fission yeast Hsp40 proteins are shown. Protein names and amino acid lengths are indicated. Protein domains are drawn as boxes according to the CATH-Gene3D, Pfam, and Prosite classifications. Predicted localization signals are shown as in Additional file 1: Figure S1. Predicted trans-membrane helix regions (TMhelix) are indicated as gray boxes. The DnaJ domains belong to the CATH superfamily 1.10.287.110. Type-I Hsp40 proteins are characterized by C-terminal (purple) and central (pink) domains that belong to the CATH superfamilies 2.60.260.20 and 2.10.230.10, respectively. The type-II Hsp40 protein Psi1 also contains the C-terminal domain but lacks the central domain. The other proteins are classified as the type-III Hsp40 proteins. Figure S3. Fission yeast type-I and -II Hsp40 proteins and their homologs. (A) Phylogenic tree of Hsp40 proteins. Scale-bar unit indicates the number of amino acid substitutions per site. Names of proteins are depicted as in Additional file 1: Figure S1. (B) Domain structure of Hsp40 proteins. Protein names are depicted as in (A) and amino acid lengths are shown. Protein domains and predicted localization signals are drawn as in Additional file 1: Figure S2. Locations of proteins in the cell are indicated. For clarity, D. melanogaster Hsp40 proteins other than Droj2 are omitted. Figure S4. Schematic representation of marker integration sites. The ade6+ and ura4+ marker genes were located in the SphI site of otr1R (otr1R(SphI)::ade6+) and in the NcoI site of imr1L (imr1L(NcoI)::ura4+), respectively. Figure S5. Hsp90 and Mas5 are dispensable for red pigment formation. Cells were spotted on normal YES plates (YES) and YES containing limited amount of adenine (Low adenine), and incubated at 30°C for six days. Figure S6. Derepression of marker genes inserted in the pericentromere. (A) Cells were serially diluted, spotted on normal EMMS plates and EMMS lacking adenine (EMMS - adenine) or uracil (EMMS - uracil), and incubated at 30°C for 6 days. (B) Strand-specific RT-qPCR for the ura4 marker gene. Values are normalized to that of the sense strand of ribosomal 28S RNA, and are presented as means + SD (n = 3). (C) Strand-specific RT-qPCR for the ade6 and ura4 genes located in the endogenous loci (ade6+ and ura4+) and in the pericentromere (otr1R::ade6+ and imr1L::ura4+). Values are normalized to that of the sense strand of ribosomal 28S RNA, and are presented as means + SD (n = 3). **P

A new and sensitive method for the determination of the molecular species of phosphatidic acid was developed. The developmental profiles of the structural heterogeneity of phosphatidic acid in rat lung and liver are presented. The individual molecular species of phosphatidic acid at different stages of development were analyzed as [14C]dimethylphosphatidates. The content of phosphatidic acid gradually increased from 20 to 40 nmol/g wet tissue during development of both lung and liver. The relative distribution of the disaturated species of lung phosphatidic acid accounted for 10.1 +/- 2.4% at -2 days of gestation and slightly decreased at -1 day and 1 day after birth (8.4 +/- 1.1%), then increased significantly to the adult level of 14.6 +/- 3.2%. The developmental pattern of the disaturated species of phosphatidic acid was not similar to that of diacylglycerol or phosphatidylcholine. On the other hand, the relative distribution of the disaturated species of liver phosphatidic acid did not change (4.1-6.0%) during development. The level of the disaturated species of phosphatidic acid was significantly higher in lung than in liver at any stage of development. The overall results strongly suggest that disaturated phosphatidic acid could be effectively formed via the de novo pathway in fetal as well as in adult lung.

For some scenarios and situations, successful localization of the sound is vital for the hearing experience. One aspect of this is the natural limits of the human localization capacity, incl. dependence on e.g. direction and distance. When addressed in laboratory experiments, the significance of other modalities are controlled in different ways, yet figures will inherently reflect properties of the test situation as well as the capacity of the individual. The present paper will review some contemporary localization experiments, with a specific view to the "absolute" acuity, the measures used to describe performance, and other methodological considerations.