Author

I. Echeverria

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 3 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:chromatin & epigenetic regulation· 2 Assay:cryo-EM· 2 Organism:human· 2 Research Focus:protein structure prediction· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

A. Sali· 4 shared N. J. Krogan· 2 shared A. Weiss· 1 shared B. Chait· 1 shared B. M. Peterlin· 1 shared C. Akey· 1 shared C. Ouch· 1 shared C. Stoneham· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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4 shared papersBiochemistry

A. Sali

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Author profile →

4 papers

Recent·Most cited

Structure and dynamics of the essential endogenous mycobacterial polyketide synthasePks13

S. K. Kim, M. S. Dickinson, J. S. Finer-Moore, Z. Guan, R. M. Kaake, I. Echeverria, J. Chen, E. H. Pulido, A. Sali, N. J. Krogan, O. S. Rosenberg, R. M. Stroud

This paper determines the structure and dynamics of the mycobacterial polyketide synthase Pks13 using cryoEM and complementary techniques, revealing intermediate states and substrate binding.

bioRxiv · Jan 27, 2023Biochemistry

Comprehensive Structure and Functional Adaptations of the Yeast Nuclear Pore Complex

C. Akey, D. Singh, C. Ouch, I. Echeverria, I. Nudelman, J. M. Varberg, Z. Yu, F. Fang, Y. Shi, J. Wang, D. Saltzberg, K. Song, C. Xu, J. Gumbart, S. Suslov, , M. Rout

This study presents the structure of the yeast nuclear pore complex using cryo-EM, revealing its functional adaptations and evolutionary links.

bioRxiv · Oct 29, 2021Biophysics

Assembly and levels of P-TEFb depend on reversiblephosphorylation of cyclinT1

F. Huang, T. N. N. Nguyen, I. Echeverria, R. Ramachandran, D. C. Cary, H. Paculova, A. Sali, A. Weiss, B. M. Peterlin, K. Fujinaga

The paper shows that P-TEFb assembly and levels depend on reversible phosphorylation of cyclinT1 by PKC and dephosphorylation by PP1, leading to P-TEFb disassembly and CycT1 degradation in quiescent and terminally differentiated cells.

bioRxiv · May 25, 2021Biochemistry

Structural Basis of CD4 Downregulation by HIV-1 Nef

Y. Kwon, R. Kaake, I. Echeverria, M. Suarez, C. Stoneham, P. W. Ramirez, J. Kress, R. Singh, A. Sali, N. J. Krogan, J. Guatelli, X. Jia

This paper presents a high-resolution crystal structure of HIV-1 Nef interacting with AP2, revealing how Nef sequesters CD4 for degradation and identifying a dual-function pocket crucial for both MHC recruitment and CD4 binding.

bioRxiv · Apr 21, 2020Biochemistry