Sort by:

• Highly Influential Citations
• Citations
• Acceleration
• Velocity
• Recency

Learn More

The BCL-2 family reunion.

• Jerry Edward Chipuk, Tudor Moldoveanu, Fabien Llambi, Melissa J Parsons, Douglas R Green
• Molecular cell
• 2010

B cell CLL/lymphoma-2 (BCL-2) and its relatives comprise the BCL-2 family of proteins, which were originally characterized with respect to their roles in controlling outer mitochondrial membrane… (More)

A unified model of mammalian BCL-2 protein family interactions at the mitochondria.

• Fabien Llambi, Tudor Moldoveanu, +5 authors Douglas R Green
• Molecular cell
• 2011

During apoptosis, the BCL-2 protein family controls mitochondrial outer membrane permeabilization (MOMP), but the dynamics of this regulation remain controversial. We employed chimeric proteins… (More)

Many players in BCL-2 family affairs.

• Tudor Moldoveanu, Ariele Viacava Follis, Richard W. Kriwacki, Douglas R Green
• Trends in biochemical sciences
• 2014

During apoptotic cell death, cellular stress signals converge at the mitochondria to induce mitochondrial outer-membrane permeabilization (MOMP) through B cell lymphoma-2 (BCL-2) family proteins and… (More)

A Ca2+ Switch Aligns the Active Site of Calpain

• Tudor Moldoveanu, Christopher M. Hosfield, Daniel Lim, John S. Elce, Zongchao Jia, Peter Leslie Davies
• Cell
• 2002

Ca(2+) signaling by calpains leads to controlled proteolysis during processes ranging from cytoskeleton remodeling in mammals to sex determination in nematodes. Deregulated Ca(2+) levels result in… (More)

The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site.

• Tudor Moldoveanu, Qian Liu, Ante Tocilj, Mark Watson, Gordon Shore, Kalle Gehring
• Molecular cell
• 2006

BAK/BAX-mediated mitochondrial outer-membrane permeabilization (MOMP) drives cell death during development and tissue homeostasis from zebrafish to humans. In most cancers, this pathway is inhibited… (More)

BID-induced structural changes in BAK promote apoptosis

• Tudor Moldoveanu, Christy R. Grace, +5 authors Douglas R Green
• Nature Structural &Molecular Biology
• 2013

The BCL-2–family protein BAK is responsible for mitochondrial outer-membrane permeabilization (MOMP), which leads to apoptosis. The BCL-2 homology 3 (BH3)-only protein BID activates BAK to perform… (More)

BOK Is a Non-canonical BCL-2 Family Effector of Apoptosis Regulated by ER-Associated Degradation

• Fabien Llambi, Yue-ming Wang, +10 authors Douglas R Green
• Cell
• 2016

The mitochondrial pathway of apoptosis is initiated by mitochondrial outer membrane permeabilization (MOMP). The BCL-2 family effectors BAX and BAK are thought to be absolutely required for this… (More)

Apoptotic regulation by MCL-1 through heterodimerization.

• Qian Liu, Tudor Moldoveanu, Tara Sprules, Edna Matta-Camacho, Nura Mansur-Azzam, Kalle Gehring
• The Journal of biological chemistry
• 2010

Myeloid cell leukemia 1 (MCL-1), an anti-apoptotic BCL-2 family member active in the preservation of mitochondrial integrity during apoptosis, has fundamental roles in development and hematopoiesis… (More)

Structural model of the BCL-w-BID peptide complex and its interactions with phospholipid micelles.

• Alexey Yu Denisov, Gang Chen, Tara Sprules, Tudor Moldoveanu, Pierre Beauparlant, Kalle Gehring
• Biochemistry
• 2006

A peptide corresponding to the BH3 region of the proapoptotic protein, BID, could be bound in the cleft of the antiapoptotic protein, BCL-w. This binding induced major conformational rearrangements… (More)

Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains.

• Tudor Moldoveanu, Kalle Gehring, Douglas R Green
• Nature
• 2008

The Ca(2+)-dependent cysteine proteases, calpains, regulate cell migration, cell death, insulin secretion, synaptic function and muscle homeostasis. Their endogenous inhibitor, calpastatin, consists… (More)

• ‹
• 1
• 2
• 3
• ›