Click here for a complete list. Here is a sampling of recent relevant publications:

Dao TD, Yang Y, Presti MF, Cosgrove MS, Hopkins MS, Ma W, Loh SN, Castañeda CA*. (2022) Mechanistic insights into enhancement or inhibition of phase separation by different polyubiquitin chains. EMBO Reports. e55056.

Zheng T, Galagedera SKK, Castañeda CA*. (2021) Previously uncharacterized interactions between the folded and intrinsically disordered domains impart asymmetric effects on UBQLN2 phase separation. Protein Sci. 30:1467–1481.

Riley JF, Fioramonti PJ, Rusnock AK, Hehnly H, Castañeda CA*. (2021) ALS-linked mutations impair UBQLN2 stress-induced biomolecular condensate assembly in cells. J. Neurochem. 159:145–155.

Namitz KEW, Zheng T, Canning AJ, Alicea-Velazquez NL, Castañeda CA*, Cosgrove MS*, Hanes SD*. (2021) Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism. Commun Biol. 4(1): 398.

Zheng T, Yang Y, Castañeda CA*. (2020) Structure, dynamics, and functions of UBQLNs: at the crossroads of protein quality control machinery. Biochemical Journal 477: 3471-3497.

Dao TP, Castañeda CA*. (2020) Ubiquitin-Modulated Phase Separation of Shuttle Proteins: Does Condensate Formation Promote Protein Degradation? BioEssays 42: 2000036.

Yang Y, Jones HB, Dao TP, Castañeda CA*. (2019) Single Amino Acid Substitutions in Stickers, but Not Spacers, Substantially Alter UBQLN2 Phase Transitions and Dense Phase Material Properties. J Phys Chem B 123: 3618-3629.

Selected as an ACS Editors’ Choice article

Dao TP, Martyniak B, Canning AJ, Lei Y, Colicino EG, Cosgrove MS, Hehnly H, Castañeda CA*. (2019) ALS-Linked Mutations Affect UBQLN2 Oligomerization and Phase Separation in a Position and Amino Acid-Dependent Manner. Structure 27: 937-951.

        Featured commentary: Higgins N, Lin B, Monteiro MJ. (2019) Lou Gehrig’s Disease (ALS): UBQLN2 Mutations Strike Out of Phase. Structure 27:879-881.

Riley JF, Dao TP, Castañeda CA*. (2018) Cancer mutations in SPOP put a stop to its intercompartmental hops. Molecular Cell 72: 1-3.

Dao TP, Kolaitis R-M, Kim HJ, O’Donovan K,  Martyniak B, Colicino E, Hehnly H, Taylor JP, Castañeda CA*. (2018) Ubiquitin modulates liquid-liquid phase separation of UBQLN2 via disruption of multivalent interactions. Molecular Cell 69: 965-978.

Featured commentary: Subudhi I, Shorter J. (2018) Ubiquilin 2: Shuttling clients out of phase? Molecular Cell. 69: 919-921.

Featured News & Views: Mittag T, Fawzi N. (2018) Protein quality and miRNA slicing get into phase. Nature Cell Biology. 20: 635-637.

Castañeda CA*, Dixon EK, Walker O, Chaturvedi A, Nakasone M, Curtis J, Reed M, Krueger S, Cropp TA, Fushman D. (2016) Linkage via K27 bestows ubiquitin chains with unique properties among polyubiquitins. Structure 24: 423-436.

Featured commentary: Di Lello P, Hymowitz SG. (2016) Unveiling the Structural and Dynamical Nature of the Ubiquitin Code. Structure. 24: 498-499.

Castañeda CA*, Chaturvedi A, Camara C, Curtis J, Krueger S, Fushman D. (2016) Linkage-specific conformational ensembles of non-canonical polyubiquitin chains. Phys. Chem. Chem. Phys. 18: 5771-5788.

Castañeda CA, Kashyap TR, Nakasone MA, Krueger S, Fushman D. (2013) Unique structural, dynamical, and functional properties of K11-linked polyubiquitin chains. Structure. 21: 1168-1181.

Featured commentary: Cunningham CN, Corn JE. (2013) Decoding a Chain Letter for Degradation. Structure. 21: 1068-1070.

Berlin K, Castañeda CA, Schneidman-Duhovny D, Sali A, Nava-Tudela A, Fushman D. (2013) Recovering a representative conformational ensemble from underdetermined macromolecular structural data, J. Am. Chem. Soc. 135: 16595-16609.

Castañeda CA, Liu J, Chaturvedi A, Nowicka U, Cropp TA, Fushman D. (2011) Nonenzymatic assembly of natural polyubiquitin chains of any linkage composition and isotopic labeling scheme. J. Am. Chem. Soc. 133: 17855-17868.

Castañeda CA, Spasser L, Bavikar SN, Brik A, Fushman D. (2011) Segmental isotopic labeling of ubiquitin chains to unravel monomer-specific molecular behavior. Angew Chem. Int. Ed. Engl. 50: 11210-11214.

Castañeda CA, Liu J, Kashyap TR, Singh RK, Fushman D, Cropp TA. (2011) Controlled enzymatic synthesis of natural-linkage, defined-length polyubiquitin chains using lysines with removable protecting groups. Chem Commum (Camb) 47: 2026-2028.


  • Ha JH, Karchin, JM, Walker-Kopp, N, Castañeda, CA & Loh, SN.  (2015)  Engineered domain swapping as an on/off switch for protein function.  Chemistry & Biology, 22:1384-93.