Associate Professor, Medicine, UCSF School of Medicine
Endocrinology
Dr. Feroz R. Papa, MD
Feroz R. Papa, MD works in the field of Endocrinology. He went to medical school at University of Chicago Pritzker School of Medicine. University of Chicago Pritzker School of Medicine has a rank of 10 in research and a 19 in primary care He received 1 awards: "Elected Member". Feroz Papa is also published. He has 27 publications published. The lastest publication: "An evolutionarily conserved gene on human chromosome 5q33-q34, UBH1, encodes a novel deubiquitinating enzyme.'
Publications
- The Role of Endoplasmic Reticulum Stress in Human Pathology.
- Druggable sensors of the unfolded protein response.
- Allosteric Inhibition of the IRE1α RNase Preserves Cell Viability and Function during Endoplasmic Reticulum Stress.
- Establishment of a system for monitoring endoplasmic reticulum redox state in mammalian cells.
- X-Box Binding Protein 1 (XBP1s) Is a Critical Determinant of Pseudomonas aeruginosa Homoserine Lactone-Mediated Apoptosis.
- Divergent allosteric control of the IRE1α endoribonuclease using kinase inhibitors.
- IRE1α Cleaves Select microRNAs during ER Stress to Derepress Translation of Proapoptotic Caspase-2.
- IRE1α Induces Thioredoxin-Interacting Protein to Activate the NLRP3 Inflammasome and Promote Programmed Cell Death under Irremediable ER Stress.
- IRE1-Dependent Activation of AMPK in Response to Nitric Oxide.
- Spontaneous development of endoplasmic reticulum stress that can lead to diabetes mellitus is associated with higher calcium-independent phospholipase A2 expression: a...
- IRE1alpha kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates.
- Rationalizing translation attenuation in the network architecture of the unfolded protein response.
- Real-time redox measurements during endoplasmic reticulum stress reveal interlinked protein folding functions.
- Caspase-2 cleavage of BID is a critical apoptotic signal downstream of endoplasmic reticulum stress.
- A kinase inhibitor activates the IRE1alpha RNase to confer cytoprotection against ER stress.
- Intracellular signaling by the unfolded protein response.
- On the mechanism of sensing unfolded protein in the endoplasmic reticulum.
- Bypassing a kinase activity with an ATP-competitive drug.
- Mutation in the NDUFS4 gene of complex I abolishes cAMP-dependent activation of the complex in a child with fatal neurological syndrome.
- An evolutionarily conserved gene on human chromosome 5q33-q34, UBH1, encodes a novel deubiquitinating enzyme.
- Interaction of the Doa4 deubiquitinating enzyme with the yeast 26S proteasome.
- DUB-1, a deubiquitinating enzyme with growth-suppressing activity.
- The DOA pathway: studies on the functions and mechanisms of ubiquitin-dependent protein degradation in the yeast Saccharomyces cerevisiae.
- The yeast SEN3 gene encodes a regulatory subunit of the 26S proteasome complex required for ubiquitin-dependent protein degradation in vivo.
- Signaling cell death from the endoplasmic reticulum stress response.
- The UPR and cell fate at a glance.
Schools
U Of Chgo Div Of Bio Sci Pritzker Sch Of Med
Doctors Specialties
- Internal Medicine
- Endocrinology
Accepted Insurances
Awards
- Elected Member
Education
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UCSF -
University of Chicago Pritzker School of Medicine
Hospital
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UCSF Medical Center
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