Journal: Cellular and Molecular Life Sciences

Article Title: Structure of potassium channels

doi: 10.1007/s00018-015-1948-5

Figure Lengend Snippet: Structures included in this paper

Article Snippet: One noticeable interaction is a salt bridge between E139 and R149 (the sequence is based on Kir2.2, a Kir channel from Gallus gallus , PDB: 3SPI [ ] and 3JYC), which replaces the E71–D80 carboxyl–carboxylate interaction in KcsA (PDB: 1K4C).

Techniques:

Journal: Cellular and Molecular Life Sciences

Article Title: Structure of potassium channels

doi: 10.1007/s00018-015-1948-5

Figure Lengend Snippet: The transmembrane part of KcsA. a The atomic structure of KcsA in the conductive state (PDB: 1K4C) viewed along the membrane plane. The pore-forming domain consists of the outer helix ( magenta ), loop regions ( green ), pore helix ( blue ), SF ( yellow ), and inner helix ( orange ). The conducted K + ions are represented by purple balls with surrounding water molecules in red . EC is extracellular and IC is intracellular for short. The glycine hinge (Gly99) and the helical bundle are labeled. b , c The enlarged view of the boxed area in ( a ) containing the SF and the extracellular entryway. The K + ions are in two configurations, either in S2 and S4 ( b ) or S1 and S3 ( c ) during conduction. The water molecules occupy the vacant ion positions in S1 and S3 ( b ) or in S2 and S4 ( c ). Other ions are located in the extracellular entryway (either S0 ( b ) or Sext ( c )) and in the central cavity (Sc ( a )). For clarity, only two monomers opposite to each other are shown. The amino acid sequence of the SF is labeled. All figures (Figs. 1, , , , , , , ) in this paper were made using Chimera and GNU Image Manipulation Program (GIMP)

Article Snippet: One noticeable interaction is a salt bridge between E139 and R149 (the sequence is based on Kir2.2, a Kir channel from Gallus gallus , PDB: 3SPI [ ] and 3JYC), which replaces the E71–D80 carboxyl–carboxylate interaction in KcsA (PDB: 1K4C).

Techniques: Labeling, Sequencing

Journal: Cellular and Molecular Life Sciences

Article Title: Structure of potassium channels

doi: 10.1007/s00018-015-1948-5

Figure Lengend Snippet: Structural comparison of bacterial K + channels: KcsA (PDB: 1K4C, cyan ), KcsA (PDB: 3F5W , magenta ), KvAP (PDB: 1ORQ, yellow ), and MthK (PDB: 3LDC , blue ). Except for KcsA in the closed conformation ( cyan ), the others are in open conformation. All structures are viewed from the intracellular side. The glycine hinges are in a similar position in these proteins. The outer helix, inner helix, and a queue of K + ions are labeled

Article Snippet: One noticeable interaction is a salt bridge between E139 and R149 (the sequence is based on Kir2.2, a Kir channel from Gallus gallus , PDB: 3SPI [ ] and 3JYC), which replaces the E71–D80 carboxyl–carboxylate interaction in KcsA (PDB: 1K4C).

Techniques: Labeling

Journal: Cellular and Molecular Life Sciences

Article Title: Structure of potassium channels

doi: 10.1007/s00018-015-1948-5

Figure Lengend Snippet: Activated, inactivated, and flipped SF structures of KcsA, viewed along the membrane plane. a Comparison of conductive (PDB: 1K4C, black ) and nonconductive (PDB: 1K4D, 3F7V and 3F5W resemble each other and 3F7V is shown in magenta ) structures. V76 and G77 are reorientated in the nonconductive state. b Comparison of conductive (PDB: 1K4C, black ) and flipped (PDB: 2ATK and 3OGC are similar and 2ATK is shown in gray ) structures. V76 and Y78 are reorientated in the flipped conformation. The S2 and S4 binding sites are labeled

Article Snippet: One noticeable interaction is a salt bridge between E139 and R149 (the sequence is based on Kir2.2, a Kir channel from Gallus gallus , PDB: 3SPI [ ] and 3JYC), which replaces the E71–D80 carboxyl–carboxylate interaction in KcsA (PDB: 1K4C).

Techniques: Binding Assay, Labeling

Journal: Oncotarget

Article Title: Protein arginine methyltransferase 1 is a novel regulator of MYCN in neuroblastoma

doi: 10.18632/oncotarget.11556

Figure Lengend Snippet: ( A ) Alignment of MYCN (53-71) and corresponding MYC protein sequences. The consensus substrate sequence of CDK is also shown. ( B ) Western blot analysis of stably transfected HEK293 cells with V5-tagged MYCN wildtype or R65A in the presence of absence of MG132 treatment (6 hr). β-actin was used as a loading control. ( C ) V5-tagged MYCN was immunoprecipitated with anti-V5 antibody from (B) after MG132 treatment, followed by western blot with indicated antibodies. The IgG heavy-chain was also indicated. ( D ) MYCN was immunoprecipitated with anti-MYCN antibody from SHEP-TET21N cells (Tet-off, MYCN on) 3 days post-transfection with siPRMT1#1 and 6 hr of MG132 treatment, followed by western blot with indicated antibodies. Western blot analysis of whole cell lysates was also shown. β-actin was used as a loading control. ( E ) The life cycle of MYCN from synthesis to degradation is shown. PRMT1-mediated R65 methylation may prime MYCN for phosphorylation at S62 via CDK, stabilizing MYCN and further priming it for phosphorylation at T58 through GSK3β. Dephosphorylation of pS62 via protein phosphatase 2A (PP2A) sensitizes MYCN phosphorylated at T58 to bind to E3 ligase, such as F-box and WD repeat domain-containing 7 (Fbw7), for subsequent ubiquitination and degradation. Demethylation of R65 may occur through unknown demethylases.

Article Snippet: Antibodies used in this study include anti-PRMT1 (Millipore #07-404), anti-MYCN (Santa Cruz #sc-53993), anti-PRMT5 (Millipore #07-405), anti-β-actin (Sigma #A5316), anti-V5 (Invitrogen #R960-25), anti-phospho-T58 MYC (Applied Biological Material #Y011034), anti-phospho-S62 MYC (BioAcademia #E71-161) and anti-ASYM24 (Millipore #07-414).

Techniques: Sequencing, Western Blot, Stable Transfection, Transfection, Immunoprecipitation, Methylation, De-Phosphorylation Assay

Journal: Journal of Clinical Microbiology

Article Title: “Smart Diagnosis” of Parasitic Diseases by Use of Smartphones

doi: 10.1128/JCM.01469-17

Figure Lengend Snippet: A comparison of smartphone-based devices used in the diagnosis of parasites

Article Snippet: Smartphone-assisted automated microscopy , Nokia E71 or Sony Ericsson C905 + algorithms , Automated; time-saving; high specificity , Images from each device need separate validation , 20.

Techniques: Comparison, Biomarker Discovery, Microscopy, Imaging, Light Microscopy, Sample Prep, Labeling, DNA Amplification