Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Goran Malojčić"'
Autor:
Marcin Grabowicz, Dorothee Andres, Matthew D Lebar, Goran Malojčić, Daniel Kahne, Thomas J Silhavy
Publikováno v:
eLife, Vol 3 (2014)
The lipopolysaccharide (LPS) forms the surface-exposed leaflet of the outer membrane (OM) of Gram-negative bacteria, an organelle that shields the underlying peptidoglycan (PG) cell wall. Both LPS and PG are essential cell envelope components that ar
Externí odkaz:
https://doaj.org/article/3f87990e42e34d8e8767d7d185821ac9
Autor:
Ashraf Wilsily, Robert Zahler, Nan Ke, Claudio Chuaqui, Michael J. Bradley, Jason J. Marineau, Goran Malojčić, Stephane Ciblat, Anneli Savinainen, Darby Schmidt, Nigel J. Waters, Kristin B. Hamman, Sydney Alnemy, Stephanie Roy, Dana K. Winter, Anzhelika Kabro, Kenneth Matthew Whitmore, Shanhu Hu, Janessa Mihalich
Publikováno v:
Journal of medicinal chemistry. 65(2)
CDK7 has emerged as an exciting target in oncology due to its roles in two important processes that are misregulated in cancer cells: cell cycle and transcription. This report describes the discovery of SY-5609, a highly potent (sub-nM CDK7 Kd) and s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a002487d311de55b839be03137541dfe
https://pubmed.ncbi.nlm.nih.gov/34726887
https://pubmed.ncbi.nlm.nih.gov/34726887
Autor:
Goran Malojčić, Georg Nagel, Felipe Merino, D. Vinayagam, Mark W. Ledeboer, Oliver Hofnagel, Oleg Sitsel, Maolin Yu, Markus Stabrin, Dennis Quentin, Jing Yu-Strzelczyk, Stefan Raunser
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7ee9bc0f49a7243aa1e0c61733d9994d
https://doi.org/10.7554/elife.60603.sa2
https://doi.org/10.7554/elife.60603.sa2
Autor:
Oliver Hofnagel, Georg Nagel, D. Vinayagam, Felipe Merino, Jing Yu-Strzelczyk, Markus Stabrin, Dennis Quentin, Goran Malojčić, Oleg Sitsel, Maolin Yu, Stefan Raunser, Mark W. Ledeboer
Publikováno v:
eLife, Vol 9 (2020)
eLife
eLife
Canonical transient receptor potential channels (TRPC) are involved in receptor-operated and/or store-operated Ca2+ signaling. Inhibition of TRPCs by small molecules was shown to be promising in treating renal diseases. In cells, the channels are reg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::669b023a3300a5e9d45db634dba01af5
https://elifesciences.org/articles/60603
https://elifesciences.org/articles/60603
Autor:
D. Vinayagam, Oleg Sitsel, Oliver Hofnagel, Mark W. Ledeboer, Goran Malojčić, Felipe Merino, Markus Stabrin, Stefan Raunser, Maolin Yu, Dennis Quentin
Canonical transient receptor potential channels (TRPC) are involved in receptor-operated and/or store-operated Ca2+ signaling. Inhibition of TRPCs by small molecules was shown to be promising in treating renal diseases. In cells, the channels are reg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::090a18312945f21baa014f677dcab16b
https://doi.org/10.1101/2020.06.30.180778
https://doi.org/10.1101/2020.06.30.180778
Autor:
Goran Malojčić, Martine Brault, Ines H. Kaltheuner, Lewis C. Cantley, Patrick Deroy, Heeyoun Bunch, Shanhu Hu, Janet Iwasa, Robin D. Dowell, Michael J. Bradley, Christian Clavette, Limei Tao, Peter W. White, Matthias Geyer, Zachary C. Poss, William M. Old, Zachary L. Maas, Shraddha Nayak, Tim-Michael Decker, Christopher C. Ebmeier, Benjamin Erickson, Leah J. Damon, David Bentley, Jenna K. Rimel, Tomer M. Yaron, Jason J. Marineau, Jared L. Johnson, Kristin B. Hamman, Dylan J. Taatjes
Publikováno v:
Genes Dev
CDK7 associates with the 10-subunit TFIIH complex and regulates transcription by phosphorylating the C-terminal domain (CTD) of RNA polymerase II (RNAPII). Few additional CDK7 substrates are known. Here, using the covalent inhibitor SY-351 and quanti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec82b692d03b26dca0e48986e06f8ae7
https://pubmed.ncbi.nlm.nih.gov/33060135
https://pubmed.ncbi.nlm.nih.gov/33060135
Autor:
Goran Malojčić, Jessica Steinmann, Kerstin Moehle, John A. Robinson, Milon Mondal, Katja Zerbe, Bernd Wollscheid, Jens Sobek, Harsha Kocherla, Maik Müller, László-Csaba Bencze, Gloria Andolina
Publikováno v:
ACS Chemical Biology, 13 (3)
The outer membrane (OM) in Gram-negative bacteria is an asymmetric bilayer with mostly lipopolysaccharide (LPS) molecules in the outer leaflet. During OM biogenesis, new LPS molecules are transported from their site of assembly on the inner membrane
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c38b6206b708d5286fadeae5b05f3b39
https://hdl.handle.net/20.500.11850/323600
https://hdl.handle.net/20.500.11850/323600
Structural disulfide bonds are a typical feature of secretory proteins that are often required for protein folding and stability. Formation of a disulfide bond from a cysteine pair in a newly synthesized protein is a redox reaction that requires the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3c344318e9f9f86c0d280ea0c1bb2a69
https://doi.org/10.1039/9781788013253-00175
https://doi.org/10.1039/9781788013253-00175
Autor:
Goran Malojčić, Markus Aebi, Robin L. Owen, Rudi Glockshuber, Maurice S. Brozzo, Elisabeth Mohorko
Publikováno v:
Structure. 22(4):590-601
N-linked glycosylation of proteins in the endoplasmic reticulum (ER) is essential in eukaryotes and catalyzed by oligosaccharyl transferase (OST). Human OST is a hetero-oligomer of seven subunits. The subunit N33/Tusc3 is a tumor suppressor candidate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74186a9da8976e7ef1a1c47e6a58bec7
Publikováno v:
Biochemistry. 53:1870-1877
Bacterial aryl sulfotransferases (ASSTs) catalyze sulfotransfer from a phenolic sulfate to a phenol. These enzymes are frequently found in pathogens and upregulated during infection. Their mechanistic understanding is very limited, and their natural
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72c40d9eac6fd49be683a7ac1ca12015
https://doi.org/10.1021/bi401725j
https://doi.org/10.1021/bi401725j