Michael S. Spilman
University of Alabama at Birmingham
27 Papers
29 Citations
Michael S. Spilman is an academic researcher from University of Alabama at Birmingham. The author has contributed to research in topics: Capsid & Bacteriophage. The author has an hindex of 13, co-authored 21 publications. Previous affiliations of Michael S. Spilman include Florida State University.
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Papers
Structural heterogeneity and protein composition of exosome-like vesicles (prostasomes) in human semen.
TL;DR: Human seminal fluid contains small exosome‐like vesicles called prostasomes, which play an important role in the process of fertilization by boosting survivability and motility of spermatozoa, in addition to modulating acrosomal reactivity.
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Structure of an RNA silencing complex of the CRISPR-Cas immune system.
Michael S. Spilman,Alexis I. Cocozaki,Caryn Hale,Yaming Shao,Nancy F. Ramia,Rebeca Terns,Michael P. Terns,Hong Li,Scott M. Stagg +8 more
TL;DR: Cryoelectron microscopy reconstruction of a functional Cmr complex bound with a target RNA at ~12 Å reveals a remarkably conserved architecture among very distantly related CRISPR-Cas complexes.
142
Cryo-electron Tomography of Porcine Reproductive and Respiratory Syndrome Virus: Organization of the Nucleocapsid
TL;DR: Cryo-electron microscopy and tomographic reconstruction of virions grown in MARC-145 cells suggest that the three-dimensional structure suggests that the core is composed of a double-layered chain of nucleocapsid proteins bundled into a hollow ball.
101
ResLog plots as an empirical metric of the quality of cryo-EM reconstructions.
TL;DR: An empirical procedure is presented for differentiating between a reconstruction with well-aligned particles and a Reconstruction with grossly misclassified particles.
90
Essential Structural and Functional Roles of the Cmr4 Subunit in RNA Cleavage by the Cmr CRISPR-Cas Complex
Nancy F. Ramia,Michael S. Spilman,Li Tang,Yaming Shao,Joshua R. Elmore,Caryn Hale,Alexis I. Cocozaki,Nilakshee Bhattacharya,Rebecca M. Terns,Michael P. Terns,Hong Li,Scott M. Stagg +11 more
TL;DR: The findings reveal that four helically packed Cmr4 subunits, which make up the backbone of the Cmr complex, act as a platform to support crRNA binding and target RNA cleavage.
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