Author

S. Katti

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· 2 Biophysics· 1 Immunology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Assay:protein structure· 4 Research Focus:cell signaling & trafficking· 2 Research Focus:protein folding & dynamics· 2 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Approach:statistical model· 1

Frequent Co-Authors

T. I. Igumenova· 3 shared B. Her· 2 shared A. B. Taylor· 1 shared A. K. Srivastava· 1 shared A. Kamp· 1 shared D. S. Cafiso· 1 shared G. Dekkers· 1 shared G. van Mierlo· 1 shared

Activity by Year

2018-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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3 shared papersBiochemistry

T. I. Igumenova

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Unravelling the effect of a potentiating anti-Factor H antibody on atypical hemolytic uremic syndrome associated factor H variants

G. Dekkers, M. Brouwer, J. Jeremiasse, A. Kamp, R. M. Biggs, G. van Mierlo, S. Lauder, S. Katti, T. W. Kuijpers, T. Rispens, I. Jongerius

This study investigates how a potentiating anti-FH antibody enhances the function of wild-type and aHUS-associated FH variants.

bioRxiv · Apr 8, 2020 · PreprintImmunology

Interference of pH buffer with Pb2+-peripheral domain interactions: obstacle or opportunity?

S. Katti, T. I. Igumenova

The paper shows that using Bis-Tris buffer helps identify high-affinity Pb2+ binding sites in Syt1's Ca2+-sensing domains, revealing differences in membrane-binding responses between C2A and C2B domains.

bioRxiv · Dec 31, 2019Biochemistry

Partial metal ion saturation of C2 domains primes Syt1-membrane interactions

S. Katti, S. B. Nyenhuis, B. Her, D. S. Cafiso, T. I. Igumenova

This study shows that partial metal ion saturation of Syt1's C2 domains primes its membrane interactions by restricting conformational plasticity and positioning for full activation.

bioRxiv · Oct 18, 2019Biochemistry

High affinity interactions of Pb2+ with Synaptotagmin I

S. Katti, B. Her, A. K. Srivastava, A. B. Taylor, S. W. Lockless, T. I. Igumenova

This study identifies two high-affinity Pb2+ binding sites in Synaptotagmin I and shows Pb2+ can act as a kinetic and thermodynamic trap, interfering with Ca2+-dependent function.

bioRxiv · Jun 16, 2018Biophysics