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For: Sicking M, Lang S, Bochen F, Roos A, Drenth JPH, Zakaria M, Zimmermann R, Linxweiler M. Complexity and Specificity of Sec61-Channelopathies: Human Diseases Affecting Gating of the Sec61 Complex. Cells 2021;10:1036. [PMID: 33925740 DOI: 10.3390/cells10051036] [Cited by in Crossref: 17] [Cited by in F6Publishing: 20] [Article Influence: 17.0] [Reference Citation Analysis]
Number Citing Articles
1 Sun J, Qin F, Sun F, He P, Wei E, Wang R, Zhu F, Wang Q, Tang X, Zhang Y, Shen Z. Identification and subcellular colocalization of protein transport protein Sec61α and Sec61γ in Nosema bombycis. Gene 2023;851:146971. [DOI: 10.1016/j.gene.2022.146971] [Reference Citation Analysis]
2 Jung S, Yun M, Yim C, Hong S, Huh W, Kim H. Expression level of Sec62 modulates membrane insertion of marginally hydrophobic segments. Biochimica et Biophysica Acta (BBA) - Biomembranes 2022;1864:184051. [DOI: 10.1016/j.bbamem.2022.184051] [Reference Citation Analysis]
3 Bhadra P, Römisch K, Helms V. Effect of Sec62 on the conformation of the Sec61 channel in yeast. Biochimica et Biophysica Acta (BBA) - Biomembranes 2022;1864:184050. [DOI: 10.1016/j.bbamem.2022.184050] [Reference Citation Analysis]
4 Parys JB, Van Coppenolle F. Sec61 complex/translocon: The role of an atypical ER Ca2+-leak channel in health and disease. Front Physiol 2022;13:991149. [DOI: 10.3389/fphys.2022.991149] [Reference Citation Analysis]
5 Zimmermann JSM, Linxweiler J, Radosa JC, Linxweiler M, Zimmermann R. The endoplasmic reticulum membrane protein Sec62 as potential therapeutic target in SEC62 overexpressing tumors. Front Physiol 2022;13:1014271. [DOI: 10.3389/fphys.2022.1014271] [Reference Citation Analysis]
6 Linxweiler M, Müller CSL. Role of the SEC62 gene in dermato-oncology - impact on tumor cell biology, prognostication, and personalized therapy management. J Dtsch Dermatol Ges 2022. [PMID: 36067526 DOI: 10.1111/ddg.14817] [Reference Citation Analysis]
7 Zimmermann R. Mechanismen des Proteinimports in das humane endoplasmatische Retikulum. Biospektrum 2022;28:470-474. [DOI: 10.1007/s12268-022-1797-3] [Reference Citation Analysis]
8 Linxweiler M, Müller CSL. Rolle des SEC62-Gens in der Dermatoonkologie - Relevanz für die Tumorzellbiologie, Prognoseeinschätzung und personalisierte Therapieplanung. J Dtsch Dermatol Ges 2022;20:1187-200. [PMID: 36162019 DOI: 10.1111/ddg.14817_g] [Reference Citation Analysis]
9 Körner S, Pick T, Bochen F, Wemmert S, Körbel C, Menger MD, Cavalié A, Kühn J, Schick B, Linxweiler M. Antagonizing Sec62 function in intracellular Ca2+ homeostasis represents a novel therapeutic strategy for head and neck cancer. Front Physiol 2022;13:880004. [DOI: 10.3389/fphys.2022.880004] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
10 Lang S, Nguyen D, Bhadra P, Jung M, Helms V, Zimmermann R. Signal Peptide Features Determining the Substrate Specificities of Targeting and Translocation Components in Human ER Protein Import. Front Physiol 2022;13:833540. [DOI: 10.3389/fphys.2022.833540] [Cited by in Crossref: 3] [Cited by in F6Publishing: 2] [Article Influence: 3.0] [Reference Citation Analysis]
11 O'Keefe S, Bhadra P, Duah KB, Zong G, Tenay L, Andrews L, Schneider H, Anderson A, Hu Z, Aljewari HS, Hall BS, Simmonds RE, Helms V, High S, Shi WQ. Synthesis, Biological Evaluation and Docking Studies of Ring-Opened Analogues of Ipomoeassin F. Molecules 2022;27:4419. [PMID: 35889292 DOI: 10.3390/molecules27144419] [Reference Citation Analysis]
12 Lang S, Zimmermann R. Mechanisms of ER Protein Import. Int J Mol Sci 2022;23:5315. [PMID: 35628123 DOI: 10.3390/ijms23105315] [Reference Citation Analysis]
13 Kitamura T, Suzuki R, Inuki S, Ohno H, McPhail KL, Oishi S. Design of Coibamide A Mimetics with Improved Cellular Bioactivity. ACS Med Chem Lett 2022;13:105-10. [PMID: 35059129 DOI: 10.1021/acsmedchemlett.1c00591] [Reference Citation Analysis]
14 Tirincsi A, Sicking M, Hadzibeganovic D, Haßdenteufel S, Lang S. The Molecular Biodiversity of Protein Targeting and Protein Transport Related to the Endoplasmic Reticulum. Int J Mol Sci 2021;23:143. [PMID: 35008565 DOI: 10.3390/ijms23010143] [Cited by in Crossref: 7] [Cited by in F6Publishing: 7] [Article Influence: 7.0] [Reference Citation Analysis]
15 Zimmermann R, Lang S, Lerner M, Förster F, Nguyen D, Helms V, Schrul B. Quantitative Proteomics and Differential Protein Abundance Analysis after the Depletion of PEX3 from Human Cells Identifies Additional Aspects of Protein Targeting to the ER. Int J Mol Sci 2021;22:13028. [PMID: 34884833 DOI: 10.3390/ijms222313028] [Cited by in Crossref: 5] [Cited by in F6Publishing: 5] [Article Influence: 5.0] [Reference Citation Analysis]
16 Jung SJ, Kim H. Emerging View on the Molecular Functions of Sec62 and Sec63 in Protein Translocation. Int J Mol Sci 2021;22:12757. [PMID: 34884562 DOI: 10.3390/ijms222312757] [Cited by in Crossref: 3] [Cited by in F6Publishing: 5] [Article Influence: 3.0] [Reference Citation Analysis]
17 Pauwels E, Schülein R, Vermeire K. Inhibitors of the Sec61 Complex and Novel High Throughput Screening Strategies to Target the Protein Translocation Pathway. Int J Mol Sci 2021;22:12007. [PMID: 34769437 DOI: 10.3390/ijms222112007] [Cited by in Crossref: 8] [Cited by in F6Publishing: 9] [Article Influence: 8.0] [Reference Citation Analysis]
18 Bhadra P, Helms V. Molecular Modeling of Signal Peptide Recognition by Eukaryotic Sec Complexes. Int J Mol Sci 2021;22:10705. [PMID: 34639046 DOI: 10.3390/ijms221910705] [Cited by in Crossref: 4] [Cited by in F6Publishing: 5] [Article Influence: 4.0] [Reference Citation Analysis]
19 Perkins HT, Allan V. Intertwined and Finely Balanced: Endoplasmic Reticulum Morphology, Dynamics, Function, and Diseases. Cells 2021;10:2341. [PMID: 34571990 DOI: 10.3390/cells10092341] [Cited by in Crossref: 10] [Cited by in F6Publishing: 12] [Article Influence: 10.0] [Reference Citation Analysis]