The Antiviral Activity of the Cellular Glycoprotein LGALS3BP/90K Is Species Specific

Autor: Aparna Ponnurangam, Thomas Krey, George Ssebyatika, Veronika Lodermeyer, Margalida Rotger, Vânia Passos, Angelina Malassa, Ellen Ewald, Amalio Telenti, Christine S. Falk, Christina M. Stürzel, Christine Goffinet, Frank Kirchhoff

Publikováno v: Journal of virology
Journal of Virology
Journal of virology, vol. 92, no. 14, pp. 1

Cellular antiviral proteins interfere with distinct steps of replication cycles of viruses. The galectin 3 binding protein (LGALS3BP, also known as 90K) was previously shown to lower the infectivity of nascent human immunodeficiency virus type 1 (HIV

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3eead4ffd8307f20fbf21abaf24c5bbb
https://doi.org/10.1128/jvi.00226-18

BCL11A Haploinsufficiency Causes an Intellectual Disability Syndrome and Dysregulates Transcription

Autor: Gabriela Sánchez-Andrade, Susan E. Holder, Jeremy F. McRae, Stephen J. Sawiak, Song-Choon Lee, Pelagia Deriziotis, Shelagh Joss, Tjitske Kleefstra, Julien Thevenon, Jenny Morton, Simon E. Fisher, Cristina Dias, Mathew E. Hurles, Sara Busquets Estruch, Kelly Mellul, Claire L. S. Turner, Darren W. Logan, Sarah A. Graham, Rui Santos, Ximena Ibarra-Soria, Laurence Faivre, Jane A. Hurst, Pentao Liu

Publikováno v: The American Journal of Human Genetics
American Journal of Human Genetics
American Journal of Human Genetics, Elsevier (Cell Press), 2016, 99 (2), pp.253-274. ⟨10.1016/j.ajhg.2016.05.030⟩
American Journal of Human Genetics, 99, 2, pp. 253-274
American Journal of Human Genetics, 99, 253-274
Dias, C, Estruch, S B, Graham, S A, McRae, J, Sawiak, S J, Hurst, J A, Joss, S K, Holder, S E, Morton, J E V, Turner, C, Thevenon, J, Mellul, K, Sánchez-Andrade, G, Ibarra-Soria, X, Deriziotis, P, Santos, R F, Lee, S-C, Faivre, L, Kleefstra, T, Liu, P, Hurles, M E & Fisher, S E & Logan, D W 2016, ' BCL11A Haploinsufficiency Causes an Intellectual Disability Syndrome and Dysregulates Transcription ', American Journal of Human Genetics, vol. 99, no. 2, pp. 253-274 . https://doi.org/10.1016/j.ajhg.2016.05.030

Contains fulltext : 167380.pdf (Publisher’s version ) (Open Access) Intellectual disability (ID) is a common condition with considerable genetic heterogeneity. Next-generation sequencing of large cohorts has identified an increasing number of genes

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e2b0c5321656ea6915dd869874775e1
https://pubmed.ncbi.nlm.nih.gov/27453576

Bonds between Fibronectin and Fibronectin-Binding Proteins on Staphylococcus aureus and Lactococcus lactis

Autor: Andrew Buck, Steven K. Lower, Alex C. DiBartola, Jie Liu, Philippe Moreillon, Vance G. Fowler, Yok-Ai Que, Ruchirej Yongsunthon

Publikováno v: Langmuir
Langmuir, vol. 26, no. 13, pp. 10764-10770

Bacterial cell-wall-associated fibronectin binding proteins A and B (FnBPA and FnBPB) form bonds with host fibronectin. This binding reaction is often the initial step in prosthetic device infections. Atomic force microscopy was used to evaluate bind

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56ca3f2ab8af67f04972126c8bc40e41
https://doi.org/10.1021/la100549u

Structure and Characterization of AAT-1 Isoforms

Autor: Ray Ishizaki, Sanae M.M. Iguchi-Ariga, Takahiro Taira, Eiko Matsuda, Hiroyoshi Ariga

Publikováno v: Biological and Pharmaceutical Bulletin. 28:898-901

A novel protein, AAT-1, was identified as a AMY-1-binding protein and three splicing variants of AAT-1, AAT-1alpha, -beta and -gamma were identified. The function of AAT-1 is thought to be related to spermatogenesis. In this study, we further identif

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c117b647c9b9c1673a69e6a4391fa4b1
https://doi.org/10.1248/bpb.28.898

Conserved residues R420 and Q428 in a cytoplasmic loop of the citrate/malate transporter CimH of Bacillus subtilis are accessible from the external face of the membrane

Autor: Bastiaan P. Krom, Juke S. Lolkema

Publikováno v: Biochemistry, 42(2), 467-474. AMER CHEMICAL SOC
Krom, B P & Lolkema, J S 2003, ' Conserved residues R420 and Q428 in a cytoplasmic loop of the citrate/malate transporter CimH of Bacillus subtilis are accessible from the external face of the membrane ', Biochemistry, vol. 42, no. 2, pp. 467-74 . https://doi.org/10.1021/bi026874a
Biochemistry, 42(2), 467-74. American Chemical Society

CimH of Bacillus subtilis is a secondary transporter for citrate and malate that belongs to the 2-hydroxycarboxylate transporter (2HCT) family. Conserved residues R143, R420, and Q428.. located in putative cytoplasmic loops and R432, located at the c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0845dcc60b1779a4fcac5fbae112cd76
https://research.rug.nl/en/publications/42cafbcf-e1ce-46e6-b792-d5ccb77a7b92