Sarah Connolly (PER-119)
Sarah Connolly is a faculty member and director at DePaul University in College of Science and Health / Health Sciences and Biological Sciences. Documented areas of work include genomics and virology.
Summary ✓
- Primary affiliation: College of Science and Health / Health Sciences and Biological Sciences
- Role types: faculty, director
- Last reviewed: 2026-06-14
Access (availability): 🟢 Green — open or routine · 🟡 Yellow — appointment or affiliation · 🔴 Red — restricted · ⚪/⚫ White/Black — not yet classified
Verification: ✓ confirmed · ~ likely · ? needs review · ✕ archived
Profile & contact
- Email: sarah.connolly@depaul.edu
- Faculty profile: www.depaul.edu/faculty/sarah-connolly
Description
Sarah Connolly is a faculty member and director at DePaul University in College of Science and Health / Health Sciences and Biological Sciences. Documented areas of work include genomics and virology.
Linked resources
- Connolly Lab (Faculty lead)
Linked grants
Linked courses
None documented.
Linked publications
- Herpes Simplex Virus Glycoprotein B Mutations Define Structural Sites in Domain I, the Membrane Proximal Region, and Domain V That Regulate Entry (Author) — DOI
- Substitution of Herpes Simplex Virus 1 Entry Glycoproteins with Those of Saimiriine Herpesvirus 1 Reveals a gD-gH/gL Functional Interaction and a Region within the gD Profusion Domain That Is Critical for Fusion (Author) — DOI
- A Functional Interaction between Herpes Simplex Virus 1 Glycoprotein gH/gL Domains I and II and gD Is Defined by Using Alphaherpesvirus gH and gL Chimeras (Author) — DOI
- Species-specific gB ectodomain interactions and cytoplasmic domain stability regulate herpes simplex virus fusion. (Author) — DOI
- Multiple Sites on Glycoprotein H (gH) Functionally Interact with the gB Fusion Protein to Promote Fusion during Herpes Simplex Virus (HSV) Entry. (Author) — DOI
- The structural basis of herpesvirus entry. (Author) — DOI
- Structure-Based Mutations in the Herpes Simplex Virus 1 Glycoprotein B Ectodomain Arm Impart a Slow-Entry Phenotype. (Author) — DOI
- Using proximity biotinylation to detect herpesvirus entry glycoprotein interactions: Limitations for integral membrane glycoproteins. (Author) — DOI
- The structural basis of herpesvirus entry (Author) — DOI
- Structure-Based Mutations in the Herpes Simplex Virus 1 Glycoprotein B Ectodomain Arm Impart a Slow-Entry Phenotype (Author) — DOI
- Natural Selection of Glycoprotein B Mutations That Rescue the Small-Plaque Phenotype of a Fusion-Impaired Herpes Simplex Virus Mutant (Author) — DOI
- Multiple Sites on Glycoprotein H (gH) Functionally Interact with the gB Fusion Protein to Promote Fusion during Herpes Simplex Virus (HSV) Entry (Author) — DOI
- Species-specific gB ectodomain interactions and cytoplasmic domain stability regulate herpes simplex virus fusion (Author) — DOI
- PUB-642 (Author) — DOI
- PUB-643 (Author) — DOI
- PUB-644 (Author) — DOI
- PUB-705 (Author) — DOI
- PUB-776 (Author) — DOI
Linked outputs
None documented.
Verification
- Status: ✓ Listed in the map and on a DePaul page
- Last reviewed: 2026-06-14
- ORCID verification: unresolved (source: n/a)
Source URLs
Notes
Person listing on the Resource Map. Open linked places, grants, courses, and publications from this page.