Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Maria K. Janowska"'
Autor:
Christopher N Woods, Lindsey D Ulmer, Maria K Janowska, Natalie L Stone, Ellie I James, Miklos Guttman, Matthew F Bush, Rachel E Klevit
Small heat shock proteins (sHSPs) are chaperones whose importance in protein homeostasis is exemplified by dozens of missense mutations associated with tissue-specific disease states. Despite decades of studies, the structure, dynamics, and mechanism
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::27f957b193fd5e65cd4d4016255409c6
https://doi.org/10.1101/2022.05.30.493970
https://doi.org/10.1101/2022.05.30.493970
Autor:
Katherine H. Reiter, Alex Zelter, Maria K. Janowska, Michael Riffle, Nicholas Shulman, Brendan X. MacLean, Kaipo Tamura, Matthew C. Chambers, Michael J. MacCoss, Trisha N. Davis, Miklos Guttman, Peter S. Brzovic, Rachel E. Klevit
Publikováno v:
Structure (London, England : 1993). 30(9)
RING-between-RING (RBR) E3 ligases mediate ubiquitin transfer through an obligate E3-ubiquitin thioester intermediate prior to substrate ubiquitination. Although RBRs share a conserved catalytic module, substrate recruitment mechanisms remain enigmat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b07bbd68205e8a993347b5e51c5115f3
https://pubmed.ncbi.nlm.nih.gov/36055221
https://pubmed.ncbi.nlm.nih.gov/36055221
Publikováno v:
PLoS ONE, Vol 8, Iss 9, p e75018 (2013)
Aggregation of α-synuclein (αSyn), the primary protein component in Lewy body inclusions of patients with Parkinson's disease, arises when the normally soluble intrinsically disordered protein converts to amyloid fibrils. In this work, we provide a
Externí odkaz:
https://doaj.org/article/f6c0a68b63674a28bee798bdd689acee
Autor:
Christian, Lips, Tobias, Ritterhoff, Annika, Weber, Maria K, Janowska, Mandy, Mustroph, Thomas, Sommer, Rachel E, Klevit
Publikováno v:
The EMBO Journal
Protein modification with poly‐ubiquitin chains is a crucial process involved in a myriad of cellular pathways. Chain synthesis requires two steps: substrate modification with ubiquitin (priming) followed by repetitive ubiquitin‐to‐ubiquitin at
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3fcd73a01e0b60c390c8163fbbe2c9f0
https://pubmed.ncbi.nlm.nih.gov/33015833
https://pubmed.ncbi.nlm.nih.gov/33015833
Publikováno v:
Cold Spring Harb Perspect Biol
Small heat shock proteins (sHSPs) are ATP-independent chaperones that delay formation of harmful protein aggregates. sHSPs' role in protein homeostasis has been appreciated for decades, but their mechanisms of action remain poorly understood. This ga
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a207931b65fbe3223b3f5bc2ecf64408
https://pubmed.ncbi.nlm.nih.gov/30833458
https://pubmed.ncbi.nlm.nih.gov/30833458
Autor:
Jean Baum, Maria K. Janowska
Publikováno v:
Protein Science. 25:286-294
β-synuclein (βS) is a homologue of α-synuclein (αS), the major protein component of Lewy bodies in patients with Parkinson's disease. In contrast to αS, βS does not form fibrils, mitigates αS toxicity in vivo and inhibits αS fibril formation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::208bca47d7bc2e47ea40dc5596b26bfd
https://doi.org/10.1002/pro.2798
https://doi.org/10.1002/pro.2798
Autor:
Sagar D. Khare, Gina M. Moriarty, Jean Baum, Maria K. Janowska, Tamr B. Atieh, Michael P. Olson
Publikováno v:
The Journal of biological chemistry. 292(39)
α-Synuclein (αS) is the primary protein associated with Parkinson's disease, and it undergoes aggregation from its intrinsically disordered monomeric form to a cross-β fibrillar form. The closely related homolog β-synuclein (βS) is essentially f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b442b72f88c88359510f60793726045c
https://pubmed.ncbi.nlm.nih.gov/28963338
https://pubmed.ncbi.nlm.nih.gov/28963338
Autor:
Jean Baum, Maria K. Janowska
Publikováno v:
Methods in Molecular Biology ISBN: 9781493929771
NMR interchain paramagnetic relaxation enhancement (PRE) techniques are a very powerful approach for detecting transient interchain interactions between intrinsically disordered proteins. These experiments, requiring a mixed sample containing a 1:1 r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::359163e1c86a3c72003ac3b1438549e5
https://doi.org/10.1007/978-1-4939-2978-8_3
https://doi.org/10.1007/978-1-4939-2978-8_3
Publikováno v:
Scientific Reports
Pathology in Parkinson’s disease is linked to self-association of α-Synuclein (αS) into pathogenic oligomeric species and highly ordered amyloid fibrils. Developing effective therapeutic strategies against this debilitating disease is critical an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd39b27262211a0ea49b8763ea8a0697
Autor:
Maria K, Janowska, Jean, Baum
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1345
NMR interchain paramagnetic relaxation enhancement (PRE) techniques are a very powerful approach for detecting transient interchain interactions between intrinsically disordered proteins. These experiments, requiring a mixed sample containing a 1:1 r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ece55cfcd90cddfa5a413d4ab6cc4567
https://pubmed.ncbi.nlm.nih.gov/26453204
https://pubmed.ncbi.nlm.nih.gov/26453204