Search results for: Pranab Maiti

Items from 1 to 8 out of 8 results

article

Novel highly selective inhibitors of ubiquitin specific protease 30 (USP30) accelerate mitophagy

Arthur F. Kluge, Bharat R. Lagu, Pranab Maiti, Mahaboobi Jaleel, more

Bioorganic & Medicinal Chemistry Letters > 2018 > 28 > 15 > 2655-2659

Mitophagy is one of the processes that cells use to maintain overall health. An E3 ligase, parkin, ubiquitinates mitochondrial proteins prior to their degradation by autophagasomes. USP30 is an enzyme that de-ubiquitinates mitochondrial proteins; therefore, inhibiting this enzyme could foster mitophagy. Herein, we disclose the structure–activity relationships (SAR) within a novel series of highly...

article

TGR5: an emerging bile acid G-protein-coupled receptor target for the potential treatment of metabolic disorders

Atul Tiwari, Pranab Maiti

Drug Discovery Today > 2009 > 14 > 9-10 > 523-530

Over the past decade, new roles for bile acids in paracrine and endocrine regulation of cholesterol homeostasis, lipid and carbohydrate metabolism and immunomodulatory functions have been discovered. Most of the early discoveries focused on the genomic actions of bile acids through the activation of families of nuclear receptors, such as the farnesoid X receptor and vitamin D receptors, until a new...

article

Small Molecule RPE65 Antagonists Limit the Visual Cycle and Prevent Lipofuscin Formation,

Pranab Maiti, Jian Kong, So Ra Kim, Janet R. Sparrow, more

Biochemistry > 2007 > 46 > 29 > 8700 - 8700

article

Small Molecule RPE65 Antagonists Limit the Visual Cycle and Prevent Lipofuscin Formation ^†

Pranab Maiti, Jian Kong, So Ra Kim, Janet R. Sparrow, more

Biochemistry > 2006 > 45 > 3 > 852 - 860

article

Specificity of Binding of all- trans -Retinyl Ester to RPE65 ^†

Pranab Maiti, Deviprasad Gollapalli, Robert R. Rando

Biochemistry > 2005 > 44 > 44 > 14463 - 14469

article

A Palmitoylation Switch Mechanism in the Regulation of the Visual Cycle

Linlong Xue, Deviprasad R. Gollapalli, Pranab Maiti, Wan Jin Jahng, more

Cell > 2004 > 117 > 6 > 761-771

RPE65 is essential for the biosynthesis of 11-cis-retinal, the chromophore of rhodopsin. Here, we show that the membrane-associated form (mRPE65) is triply palmitoylated and is a chaperone for all-trans-retinyl esters, allowing their entry into the visual cycle for processing into 11-cis-retinal. The soluble form of RPE65 (sRPE65) is not palmitoylated and is a chaperone for vitamin A, rather than...

article

RPE65 Operates in the Vertebrate Visual Cycle by Stereospecifically Binding All- trans -Retinyl Esters,

Deviprasad R. Gollapalli, Pranab Maiti, Robert R. Rando

Biochemistry > 2004 > 43 > 22 > 7226 - 7226

article

RPE65 Operates in the Vertebrate Visual Cycle by Stereospecifically Binding All- trans -Retinyl Esters ^†

Deviprasad R. Gollapalli, Pranab Maiti, Robert R. Rando

Biochemistry > 2003 > 42 > 40 > 11824 - 11830

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Search results for: Pranab Maiti

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