Minhajuddin Sirajuddin
University of California, San Francisco
27 Papers
17 Citations
Minhajuddin Sirajuddin is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: Microtubule & Tubulin. The author has an hindex of 11, co-authored 16 publications. Previous affiliations of Minhajuddin Sirajuddin include Indian Institute of Science & Max Planck Society.
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Papers
Regulation of microtubule motors by tubulin isotypes and post-translational modifications
TL;DR: The results show that tubulin isotypes and PTMs can govern motor velocity, processivity and microtubule depolymerization rates, with substantial changes conferred by even single amino acid variation, and that different molecular motors recognize distinctive tubulin ‘signatures’, which supports the tubulin-code hypothesis.
Structural insight into filament formation by mammalian septins
Minhajuddin Sirajuddin,Marian Farkasovsky,Florian Hauer,Dorothee Kühlmann,Ian G. Macara,Michael Weyand,Holger Stark,Alfred Wittinghofer +7 more
TL;DR: The structures reveal a universal bipolar polymer building block, composed of an extended G domain, which forms oligomers and filaments by conserved interactions between adjacent nucleotide-binding sites and/or the amino- and carboxy-terminal extensions.
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Tyrosination of α‐tubulin controls the initiation of processive dynein–dynactin motility
TL;DR: Examination of processive motility of mammalian dynein complexed with dynactin and BicD2 on tyrosinated versus detyrosinated microtubules reveals a strong effect of the C‐terminal α‐tubulin tyrosine on dyneIn–dynactin motility and suggests that the tubulin tyosination cycle could modulate the initiation of dyne in‐driven motility in cells.
GTP-induced conformational changes in septins and implications for function
TL;DR: It is proposed that GTP binding/hydrolysis and the nature of the nucleotide influence the stability of interfaces in heterooligomeric and polymeric septins and are required for proper septin filament assembly/disassembly.
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De novo mutations in KIF1A cause progressive encephalopathy and brain atrophy.
Sahar Esmaeeli Nieh,Maura Madou,Minhajuddin Sirajuddin,Minhajuddin Sirajuddin,Brieana Fregeau,Dianalee McKnight,Katrina W. Lexa,Jonathan B. Strober,Christine G. Spaeth,Barbara Hallinan,Nizar Smaoui,John Pappas,Thomas A. Burrow,Thomas A. Burrow,Marie T. McDonald,Mariam Latibashvili,Mariam Latibashvili,Esther Leshinsky-Silver,Dorit Lev,Luba Blumkin,Ronald D. Vale,A. J. Barkovich,Elliott H. Sherr +22 more
TL;DR: To determine the cause and course of a novel syndrome with progressive encephalopathy and brain atrophy in children, an international team of scientists and clinicians are using a novel approach called “big data” to solve the mystery of “why children’s brains are mummified”.
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