Menelaos Voulgaris

发表

Transport of DNA within cohesin involves clamping on top of engaged heads by Scc2 and entrapment within the ring by Scc3

K. Nasmyth, J. Löwe, Jean Metson, 2020, eLife.

Formation of the clamped state by Scc2 and DNA overcomes the constraints imposed by zipping-up of the SMC coiled coils on cohesin’s ATPase

K. Nasmyth, Menelaos Voulgaris, Madhusudhan Srinivasan, 2022, bioRxiv.

Formation of the clamped state by Scc2 and DNA overcomes the constraints imposed by zipping-up of the SMC coiled coils on cohesin’s ATPase

K. Nasmyth, Menelaos Voulgaris, Madhusudhan Srinivasan, 2022, bioRxiv.

Scc2 Is a Potent Activator of Cohesin’s ATPase that Promotes Loading by Binding Scc1 without Pds5

K. Nasmyth, J. Löwe, Hongtao Yu, 2018, Molecular cell.

Folding of cohesin’s coiled coil is important for Scc2/4-induced association with chromosomes

K. Nasmyth, B. Oh, J. Löwe, 2021, eLife.

Scc2 and Scc3 promote distinct modes of topological association between cohesin and DNA

K. Nasmyth, J. Löwe, Jean Metson, 2020 .

ATP dependent DNA transport within cohesin: Scc2 clamps DNA on top of engaged heads while Scc3 promotes entrapment within the SMC-kleisin ring

K. Nasmyth, J. Löwe, A. G. Llamazares, 2020, bioRxiv.

The Cohesin Ring Uses Its Hinge to Organize DNA Using Non-topological as well as Topological Mechanisms

K. Nasmyth, V. Costanzo, Sugako Ogushi, 2017, Cell.

Scc2 Is a Potent Activator of Cohesin’s ATPase that Promotes Loading by Binding Scc1 without Pds5

K. Nasmyth, J. Löwe, Hongtao Yu, 2018, Molecular cell.

Multiple interactions between Scc1 and Scc2 activate cohesin’s DNA dependent ATPase and replace Pds5 during loading

K. Nasmyth, J. Löwe, Hongtao Yu, 2017, bioRxiv.

Conformational dynamics of cohesin/Scc2 loading complex are regulated by Smc3 acetylation and ATP binding

K. Nasmyth, J. Rafferty, Naomi J Petela, 2022, bioRxiv.

Scc2 counteracts a Wapl-independent mechanism that releases cohesin from chromosomes during G1

K. Nasmyth, Johanna C. Scheinost, Naomi J Petela, 2019, bioRxiv.