R
Ramesh Rijal
Researcher at Texas A&M University
Publications - 16
Citations - 115
Ramesh Rijal is an academic researcher from Texas A&M University. The author has contributed to research in topics: Dictyostelium discoideum & Polyphosphate. The author has an hindex of 6, co-authored 10 publications receiving 61 citations. Previous affiliations of Ramesh Rijal include University of Cologne.
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Journal ArticleDOI
Polyphosphate is an extracellular signal that can facilitate bacterial survival in eukaryotic cells.
TL;DR: The results suggest that bacterial polyphosphate potentiates pathogenicity by acting as an extracellular signal that inhibits phagosome maturation.
Journal ArticleDOI
An endogenous chemorepellent directs cell movement by inhibiting pseudopods at one side of cells.
TL;DR: It is found that AprA uses a subset of chemoattraction signal transduction pathways including Ras, protein kinase A, target of rapamycin (TOR), phospholipases A, and ERK1, but does not require the PI3 kinase/Akt/PKB and guanylyl cyclase pathways to induce chemorepulsion.
Journal ArticleDOI
Functional Characterisation of the Autophagy ATG12~5/16 Complex in Dictyostelium discoideum.
Malte A. Karow,Sarah Fischer,Susanne Meßling,Roman Konertz,Jana Riehl,Qiuhong Xiong,Ramesh Rijal,Prerana Wagle,Christoph S. Clemen,Christoph S. Clemen,Christoph S. Clemen,Ludwig Eichinger +11 more
TL;DR: The results confirm the essential function of the ATG12~5/16 complex in canonical autophagy, and furthermore are consistent with autophophagy-independent functions of the complex and its individual components.
Journal ArticleDOI
Functional Characterization of Ubiquitin-Like Core Autophagy Protein ATG12 in Dictyostelium discoideum
Sarah Fischer,Ramesh Rijal,Peter Frommolt,Prerana Wagle,Roman Konertz,Jan Faix,Susanne Meßling,Ludwig Eichinger +7 more
TL;DR: It is shown that ATG12 and ATG16 fulfil autophagy-independent functions in addition to their role in canonical Autophagy, indicating that both proteins also have cellular functions independent of each other.
Journal ArticleDOI
Mutant p97 exhibits species-specific changes of its ATPase activity and compromises the UBXD9-mediated monomerisation of p97 hexamers.
Ramesh Rijal,Khalid Arhzaouy,Karl-Heinz Strucksberg,Megan Cross,Andreas Hofmann,Andreas Hofmann,Rolf Schröder,Christoph S. Clemen,Ludwig Eichinger +8 more
TL;DR: These results are consistent with a scenario in which p97 point mutations lead to differences in enzymatic activities and molecular interactions, which in the long-term result in a late-onset and progressive multisystem disease.