Results 331 to 340 of about 244,605 (365)
Endocytosis restricts dendrite branching via removing ectopically localized branching ligands. [PDF]
Fang J+8 more
europepmc +1 more source
The use of race and ethnicity in sickle cell disease research. [PDF]
Kidane Gebremeskel AS+7 more
europepmc +1 more source
Movement of the endoplasmic reticulum is driven by multiple classes of vesicles marked by Rab-GTPases. [PDF]
Langley A+3 more
europepmc +1 more source
Identification of Ser71Arg mutation in RAB32 gene in familial Parkinson's disease from Southern Italy. [PDF]
Gagliardi M+6 more
europepmc +1 more source
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Biochemical Society Transactions, 2018
Leucine-rich repeat kinase 2 (LRRK2) is mutated in familial Parkinson's disease, and pathogenic mutations activate the kinase activity. A tour de force screen by Mann and Alessi and co-workers identified a subset of Rab GTPases as bona fide LRRK2 substrates.
S. Pfeffer
openaire +3 more sources
Leucine-rich repeat kinase 2 (LRRK2) is mutated in familial Parkinson's disease, and pathogenic mutations activate the kinase activity. A tour de force screen by Mann and Alessi and co-workers identified a subset of Rab GTPases as bona fide LRRK2 substrates.
S. Pfeffer
openaire +3 more sources
RAB: Provable Robustness Against Backdoor Attacks
IEEE Symposium on Security and Privacy, 2020Recent studies have shown that deep neural net-works (DNNs) are vulnerable to adversarial attacks, including evasion and backdoor (poisoning) attacks.
Maurice Weber+4 more
semanticscholar +1 more source
The multiple roles of RAB GTPases in female and male meiosis.
Human Reproduction Update, 2021BACKGROUND RAB GTPases constitute the largest family of small GTPases and are found in all eukaryotes. RAB GTPases regulate components of the endomembrane system, the nucleus and the plasma membrane, and are involved in intracellular actin/tubulin ...
Meng-Meng Shan, Shao‐Chen Sun
semanticscholar +1 more source
Functional Properties of the Rab‐Binding Domain of Rab Coupling Protein
2005Rab-Coupling Protein (RCP) is an approximately 80-kDa, hydrophilic protein that belongs to a recently identified family of proteins that is characterized by its ability to interact with Rab11 via a highly homologous Rab-binding domain positioned at its carboxy-termini.
Lindsay, Andrew+2 more
openaire +6 more sources