Eilika Weber-Ban
Researcher
Eilika Weber-Ban's AcademicInfluence.com Rankings
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Biology
Eilika Weber-Ban's Degrees
- PhD Biochemistry University of Zurich
- Masters Biochemistry University of Zurich
Why Is Eilika Weber-Ban Influential?
(Suggest an Edit or Addition)According to Wikipedia, Eilika Weber-Ban is a German biochemist. Her research considers protein degradation pathways. She was elected to the European Molecular Biology Organization in 2021. Early life and education Weber-Ban studied biochemistry at the University of Tübingen. She then received a Fulbright Program scholarship and went to the University of California at Riverside. Here she studied the tryptophan sunthase bienzyme complex under the supervision of Michael Dunn. She completed her graduate studies in 1996, and was awarded a Jane Coffin Childs Memorial Fund for Medical Research fellowship to join Arthur Horwich at Yale University.
Eilika Weber-Ban's Published Works
Published Works
- Thermotolerance Requires Refolding of Aggregated Proteins by Substrate Translocation through the Central Pore of ClpB (2004) (455)
- Global unfolding of a substrate protein by the Hsp100 chaperone ClpA (1999) (422)
- Structural basis of enzyme encapsulation into a bacterial nanocompartment (2008) (317)
- Chaperone rings in protein folding and degradation. (1999) (191)
- Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes (2009) (181)
- ClpA mediates directional translocation of substrate proteins into the ClpP protease (2001) (145)
- Protein post-translational modifications in bacteria (2019) (140)
- Controlled destruction: AAA+ ATPases in protein degradation from bacteria to eukaryotes. (2009) (129)
- Clp chaperone-proteases: structure and function. (2009) (116)
- Pilus chaperones represent a new type of protein-folding catalyst (2004) (115)
- Targeted delivery of an ssrA-tagged substrate by the adaptor protein SspB to its cognate AAA+ protein ClpX. (2003) (115)
- The mycobacterial Mpa–proteasome unfolds and degrades pupylated substrates by engaging Pup's N‐terminus (2010) (108)
- Dop functions as a depupylase in the prokaryotic ubiquitin‐like modification pathway (2010) (88)
- A distinct structural region of the prokaryotic ubiquitin‐like protein (Pup) is recognized by the N‐terminal domain of the proteasomal ATPase Mpa (2009) (82)
- Mycobacterial Ubiquitin-like Protein Ligase PafA Follows a Two-step Reaction Pathway with a Phosphorylated Pup Intermediate* (2010) (77)
- Deletion of dop in Mycobacterium smegmatis abolishes pupylation of protein substrates in vivo (2010) (65)
- Pupylation as a signal for proteasomal degradation in bacteria. (2014) (64)
- Prokaryotic ubiquitin-like protein (Pup) is coupled to substrates via the side chain of its C-terminal glutamate. (2010) (62)
- Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification pathway (2012) (56)
- Both ATPase Domains of ClpA Are Critical for Processing of Stable Protein Structures (2009) (53)
- The Mycobacterium tuberculosis ClpP1P2 Protease Interacts Asymmetrically with Its ATPase Partners ClpX and ClpC1 (2015) (52)
- The pupylation pathway and its role in mycobacteria (2012) (50)
- The Mycobacterial LexA/RecA-Independent DNA Damage Response Is Controlled by PafBC and the Pup-Proteasome System. (2018) (47)
- An intrinsic degradation tag on the ClpA C-terminus regulates the balance of ClpAP complexes with different substrate specificity. (2008) (45)
- Assembly pathway of an AAA+ protein: tracking ClpA and ClpAP complex formation in real time. (2007) (44)
- Activity of the Mycobacterial Proteasomal ATPase Mpa Is Reversibly Regulated by Pupylation* (2011) (40)
- Investigation of allosteric linkages in the regulation of tryptophan synthase: the roles of salt bridges and monovalent cations probed by site-directed mutation, optical spectroscopy, and kinetics. (2001) (38)
- Solution structure and activation mechanism of ubiquitin-like small archaeal modifier proteins. (2011) (38)
- Optimal efficiency of ClpAP and ClpXP chaperone-proteases is achieved by architectural symmetry. (2009) (37)
- Intersubunit Cross-talk in Pyridoxal 5′-Phosphate Synthase, Coordinated by the C Terminus of the Synthase Subunit* (2009) (31)
- The Bacterial Proteasome at the Core of Diverse Degradation Pathways (2019) (29)
- Bacterial Proteasome Activator Bpa (Rv3780) Is a Novel Ring-Shaped Interactor of the Mycobacterial Proteasome (2014) (29)
- Crystal structure of the complex between prokaryotic ubiquitin-like protein and its ligase PafA. (2013) (29)
- Studying chaperone-proteases using a real-time approach based on FRET. (2009) (29)
- The flexible attachment of the N-domains to the ClpA ring body allows their use on demand. (2008) (27)
- Toxic Activation of an AAA+ Protease by the Antibacterial Drug Cyclomarin A. (2019) (25)
- Mycobacterium smegmatis PafBC is involved in regulation of DNA damage response (2017) (23)
- Structural Analysis of the Bacterial Proteasome Activator Bpa in Complex with the 20S Proteasome. (2016) (21)
- Genome‐wide interaction screen for Mycobacterium tuberculosis ClpCP protease reveals toxin–antitoxin systems as a major substrate class (2020) (20)
- Prokaryotic ubiquitin-like protein remains intrinsically disordered when covalently attached to proteasomal target proteins (2017) (17)
- Structure and functional implications of WYL domain-containing bacterial DNA damage response regulator PafBC (2019) (15)
- Cdc48-like protein of actinobacteria (Cpa) is a novel proteasome interactor in mycobacteria and related organisms (2018) (15)
- Prokaryotic Ubiquitin-Like Protein and Its Ligase/Deligase Enyzmes. (2017) (14)
- Depupylase Dop Requires Inorganic Phosphate in the Active Site for Catalysis* (2017) (13)
- Chaperone-Proteases of Mycobacteria (2014) (12)
- Pupylation-dependent and -independent proteasomal degradation in mycobacteria (2015) (12)
- FixK2, a key regulator in Bradyrhizobium japonicum, is a substrate for the protease ClpAP in vitro (2013) (10)
- Antibacterial peptide CyclomarinA creates toxicity by deregulating the Mycobacterium tuberculosis ClpC1–ClpP1P2 protease (2022) (9)
- Characterization of a new AAA+ protein from archaea. (2006) (6)
- Cdc 48-like protein of actinobacteria ( Cpa ) is a novel proteasome interactor in 1 mycobacteria and related organisms 2 (2018) (6)
- Survival in Hostile Conditions: Pupylation and the Proteasome in Actinobacterial Stress Response Pathways (2021) (6)
- The alternating power stroke of a 6-cylinder AAA protease chaperone engine. (2009) (5)
- Pupylated proteins are subject to broad proteasomal degradation specificity and differential depupylation (2019) (4)
- Transcriptional control of mycobacterial DNA damage response by sigma adaptation (2021) (3)
- Structural basis of prokaryotic ubiquitin-like protein engagement and translocation by the mycobacterial Mpa-proteasome complex (2022) (3)
- Crystal structure of Thermotoga maritima encapsulin (2008) (2)
- Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation (2021) (2)
- Targeted protein degradation: from small molecules to complex organelles—a Keystone Symposia report (2022) (1)
- The pupylation pathway and its role in mycobacteria (2012) (1)
- Mycobacterium smegmatis PafBC is involved in regulation of DNA damage response (2017) (0)
- Proteasome accessory factor B/C (PafBC) of Arthrobacter aurescens (2019) (0)
- Binding of the C-terminal GQYL motif of the bacterial proteasome activator Bpa to the 20S proteasome (2016) (0)
- Structure and functional implications of WYL-domain-containing transcription factor PafBC involved in the mycobacterial DNA damage response (2019) (0)
- Real-time functional studies of Escherichia coli ClpAP chaperone-protease complex (2005) (0)
- Structure of the Deamidase-Depupylase Dop of the Prokaryotic Ubiquitin-like Modification Pathway in Complex with ATP (2012) (0)
- Correction: The Mycobacterium tuberculosis ClpP1P2 Protease Interacts Asymmetrically with Its ATPase Partners ClpX and ClpC1 (2015) (0)
- Author response: Cdc48-like protein of actinobacteria (Cpa) is a novel proteasome interactor in mycobacteria and related organisms (2018) (0)
- Structure of the Deamidase-Depupylase Dop of the Prokaryotic Ubiquitin-like Modification Pathway in Complex with ADP and Phosphate (2017) (0)
- An emerging class of nucleic acid-sensing regulators in bacteria: WYL domain-containing proteins. (2023) (0)
- ClpC2 protects mycobacteria against a natural antibiotic targeting ClpC1-dependent protein degradation (2023) (0)
- Crystal Structure of the Bacterial Proteasome Activator Bpa of Mycobacterium tuberculosis (2016) (0)
- Structure of the Deamidase-Depupylase Dop of the Prokaryotic Ubiquitin-like Modification Pathway (2012) (0)
- Structure of the Pup Ligase PafA of the Prokaryotic Ubiquitin-like Modification Pathway in Complex with ADP (2012) (0)
- Crystal Structure of the Bacterial Proteasome Activator Bpa of Mycobacterium tuberculosis (space group P3) (2016) (0)
- Solution structure of the small archaeal modifier protein 1 (SAMP1) from Methanosarcina acetivorans (2011) (0)
- Crystal Structure of the Bacterial Proteasome Activator Bpa of Mycobacterium tuberculosis (space group P6322, SeMet) (2016) (0)
- The mycobacterial pupylation pathway (98.2) (2014) (0)
- Protein post-translational modifications in bacteria (2019) (0)
- Structural basis of prokaryotic ubiquitin-like protein engagement and translocation by the mycobacterial Mpa-proteasome complex (2022) (0)
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Eilika Weber-Ban is affiliated with the following schools: