Pubmed Search for Leschziner Lab Publications

* Equal contribution
# Co-corresponding authors

Chromatin Remodeling

Turegun B, Baker RW, Leschziner AE and Dominguez R (2018). Actin-related proteins regulate the RSC chromatin remodeler by weakening intramolecular interactions of the Sth1 ATPase. Comms. Biol. 1. (link)

Xu J*, Lahiri I*, Wang W, Wier A, Cianfrocco MA, Chong J, Hare AA, Dervan PB, DiMaio F, Leschziner AE# and Wang D# (2017). Structural basis for the initiation of eukaryotic transcription-coupled DNA repair. Nature 551: 653-7.

Nguyen VQ, Ranjan A, Stengel F, Wei D, Aebersold R, Wu C and Leschziner AE (2013). Molecular architecture of the ATP-dependent chromatin remodeling complex SWR1. Cell 154: 1220-1231. (link)

Leschziner AE (2011). Electron Microscopy studies of nucleosome remodelers. Curr. Opin. Struct. Biol. 21:709-718 [Review] {download PDF}

Leschziner AE, Saha A, Wittmeyer J, Zhang Y, Bustamante C, Cairns BR and Nogales E (2007). Conformational flexibility in the chromatin remodeler RSC observed by electron microscopy and the orthogonal tilt reconstruction method. Proc. Natl. Acad. Sci. USA 104: 4913-8. {download PDF}

Leschziner AE, Lemon B, Tjian R and Nogales E (2005). Structural studies of the human PBAF chromatin-remodeling complex. Structure (Camb) 13: 267-75. {download PDF}


DeSantis ME*, Cianfrocco MA*, Htet ZM*, Tran PT, Reck-Peterson SL# and Leschziner AE# (2017). Lis1 has two opposing modes of regulating cytoplasmic dynein. Cell 170:1197-1201. And here is the BioRxiv version. 

Cianfrocco MA*, DeSantis ME*, Leschziner AE and Reck-Peterson SL (2015). Mechanism and regulation of cytoplasmic dynein. Annu. Rev. Cell. Dev. Biol. 31:83-108

Toropova K*, Zou S*, Roberts AJ, Redwine WB, Goodman BS, Reck-Peterson SL#, Leschziner AE# (2014). Lis1 regulates dynein by sterically blocking its mechanochemical cycle. eLIFE: 03372 (link)

Cianfrocco MA, Leschziner AE (2014).Traffic control: adaptor proteins guide dynein-cargo takeoff. EMBO J 33:1845-6 [News & Views]

Derr ND*, Goodman BS*, Jungmann R, Leschziner AE, Shih WM, Reck-Peterson SL (2012). Tug-of-war in motor protein ensembles revealed with a programmable DNA origami scaffold. Science 338:662-665 {download PDF}

Redwine WB*, Hernandez-Lopez R*, Zou S, Huang J, Reck-Peterson SL, Leschziner AE (2012). Structural basis for microtubule binding and release by dynein. Science 337:1532-1536 {download PDF}{Supplemental movies}

Huang J*, Roberts A*, Leschziner AE, Reck-Peterson SL (2012). Lis1 acts as a "clutch" between the ATPase and microtubule-binding domains of the dynein motor. Cell 150:975-986 {download PDF}

EM Methods

Lahiri I, Xu J, Han BG, Oh J, Wang D, DiMaio F, Leschziner AE (2019). 3.1Å structure of yeast RNA polymerase II elongation complex stalled at a cyclobutane pyrimidine dimer lesion solved using streptavidin affinity grids. J. Struct Biol. (Epub ahead of print). And here is the BioRxiv version.

Cianfrocco MA, Lahiri I, DiMaio F, Leschziner AE (2018). cryoem-cloud-tools: A software platform to deploy and manage cryo-EM jobs in the cloud. J. Struct Biol. 203:230-5. doi: And here is the BioRxiv version.

Cianfrocco MA, Leschziner AE (2015). Low cost, high performance processing of single particle cryo-electron microscopy data in the cloud. eLIFE 06664 (link). And here is the BioRxiv version.

Chandramouli P, Hernandez-Lopez R, Wang HW, Leschziner AE (2011). Validation of the ortogonal tilt reconstruction method with a biological test sample. J. Struct Biol. 175:85-96 {download PDF}

Leschziner A E (2010). The ortogonal tilt reconstruction method. Methods in Enzymology. 2010 482:237-262 [Review]{download PDF}

Leschziner AE and Nogales E (2007). Visualizing flexibility at molecular resolution: Analysis of heterogeneity in single-particle electron microscopy reconstructions. Annu. Rev. Biophys. Biomol. Struct. Vol.36: 43-62 [Review] {download PDF}

Leschziner AE and Nogales E (2006). The Orthogonal Tilt Reconstruction method: an approach to generating single-class volumes with no missing cone for ab initio reconstruction of asymmetric particles. J. Struct Biol. 153:284-99. {download PDF}