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Article: Dorsal spanning plate fixation in perilunate injuries: a case report.

Jain, Neil / Harder, Justin / Rounds, Alexis / Gottlich, Caleb / Flores, Bryant / Bourland, Bryan

Case reports in plastic surgery & hand surgery

2024 Volume 11, Issue 1, Page(s) 2332223

Abstract: A 63-year-old male presented with a trans-scaphoid lunate dislocation after a ten-foot fall. Internal fixation included placement of a dorsal spanning plate (DSP). One-year follow-up yielded a satisfactory outcome. A rigid DSP is a useful tool in acute ... ...

Abstract	A 63-year-old male presented with a trans-scaphoid lunate dislocation after a ten-foot fall. Internal fixation included placement of a dorsal spanning plate (DSP). One-year follow-up yielded a satisfactory outcome. A rigid DSP is a useful tool in acute perilunate injuries to protect internal fixation constructs and help with injury rehabilitation.
Language	English
Publishing date	2024-03-20
Publishing country	United States
Document type	Case Reports
ISSN	2332-0885
ISSN	2332-0885
DOI	10.1080/23320885.2024.2332223
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Article ; Online: The Effect of Body Mass Index on Open Carpal Tunnel Release Recovery.

Allen, Jack G / Harder, Justin / Hernandez, Evan / Bourland, Bryan / MacKay, Brendan J

Journal of hand surgery global online

2023 Volume 5, Issue 6, Page(s) 799–803

Abstract: Purpose: The purpose of this study was to determine whether a relationship exists between body mass index (BMI), specifically obesity, and surgical outcomes for open carpal tunnel release. Obesity is correlated with increased incidence of carpal tunnel ... ...

Abstract	Purpose: The purpose of this study was to determine whether a relationship exists between body mass index (BMI), specifically obesity, and surgical outcomes for open carpal tunnel release. Obesity is correlated with increased incidence of carpal tunnel syndrome; however, the effect of obesity on after release recovery has not been examined. Methods: This study used a retrospective review of patient charts (n = 142). BMI was calculated based on height and weight measurements, and patients were grouped based on their BMI into the following categories: healthy BMI (18.5-24.9 kg/m Results: Age at the time of release was found to be inversely correlated with BMI. Healthy BMI patients (n = 19) underwent release at an average age of 59.1 years, whereas OB3 (n = 30) underwent release at an average age of 46.9 years. The odds of improvement in pain were significantly lower in all three obesity groups when compared with healthy BMI at both 2 and 6 weeks after operation. Conclusions: Our results indicate that obesity may be positively correlated with earlier incidence of carpal tunnel syndrome requiring surgical intervention. These data also indicate the increased rates of postoperative complications in obese patients, particularly patients with OB3. Patients with OB3 need to understand these risks before undergoing open release. Further study should examine the impact of type 2 diabetes on carpal tunnel release recovery. Clinical relevance: The information included in this study may be used to guide surgeons and patients when considering the effect and potential improvement in outcomes that may come from addressing patient BMI before open carpal tunnel surgery.
Language	English
Publishing date	2023-08-30
Publishing country	United States
Document type	Journal Article
ISSN	2589-5141
ISSN (online)	2589-5141
DOI	10.1016/j.jhsg.2023.07.012
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Article ; Online: The effect of smoking on open carpal tunnel release recovery.

Allen, Jack G / Harder, Justin / Hernandez, Evan / Bourland, Bryan / MacKay, Brendan

Hand surgery & rehabilitation

2023 Volume 43, Issue 1, Page(s) 101626

Abstract: Introduction: This study examines the relationship between smoking status and surgical outcomes in open carpal tunnel release. Smoking status has previously been correlated with orthopedic surgical complications unless smoking cessation occurs at least ... ...

Abstract	Introduction: This study examines the relationship between smoking status and surgical outcomes in open carpal tunnel release. Smoking status has previously been correlated with orthopedic surgical complications unless smoking cessation occurs at least 4 weeks prior to surgery; however, the effect of smoking on open carpal tunnel release has not been specifically examined. Methods: This study is a retrospective review of patient charts over the last 5 years (n = 131). Smoking status was determined at the time of carpal tunnel release from the patients' charts. Patients were dichotomized as smokers (n = 58) or non-smokers (n = 73). Data comprised preoperative pain, postoperative pain at 2 and 6 weeks, postoperative wrist stiffness, wound healing time, and infection status. Data were compared on chi square, Fisher exact, and one-sided Fisher exact tests. Results: Infection rates were significantly higher in smokers. Postoperative numbness and wrist stiffness were also significantly higher in smokers. Smokers reported higher postoperative pain scores at 2 and 6 weeks. Non-smokers were also significantly more likely to report complete pain resolution at 6 weeks. Discussion: In the present study smoking was associated with surgical outcome complications in open carpal tunnel release. This could be attributed to immune system suppression or to poor wound healing, both of which are known side-effects of smoking. Pain scores 6 weeks post-surgery were significantly higher in smokers than in non-smokers. Smokers undergoing open carpal tunnel release need to understand the risk of surgical complications and should consider smoking cessation to optimize their chances of successful surgery. Conclusion: Patients who were active smokers showed poorer recovery from open carpal tunnel surgery than non-smoking patients.
MeSH term(s)	Humans ; Treatment Outcome ; Smoking/adverse effects ; Carpal Tunnel Syndrome/surgery ; Retrospective Studies ; Pain, Postoperative
Language	English
Publishing date	2023-12-14
Publishing country	France
Document type	Journal Article
ZDB-ID	2848776-X
ISSN	2468-1210
ISSN (online)	2468-1210
DOI	10.1016/j.hansur.2023.11.011
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Zs.A 1791: Show issues

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Article ; Online: A 3D printable alloy designed for extreme environments.

Smith, Timothy M / Kantzos, Christopher A / Zarkevich, Nikolai A / Harder, Bryan J / Heczko, Milan / Gradl, Paul R / Thompson, Aaron C / Mills, Michael J / Gabb, Timothy P / Lawson, John W

Nature

2023 Volume 617, Issue 7961, Page(s) 513–518

Abstract: Multiprincipal-element alloys are an enabling class of materials owing to their impressive mechanical and oxidation-resistant properties, especially in extreme ... ...

Abstract	Multiprincipal-element alloys are an enabling class of materials owing to their impressive mechanical and oxidation-resistant properties, especially in extreme environments
Language	English
Publishing date	2023-04-19
Publishing country	England
Document type	Journal Article
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/s41586-023-05893-0
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Zs.A 26: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Pacritinib is a potent ACVR1 inhibitor with significant anemia benefit in patients with myelofibrosis.

Oh, Stephen T / Mesa, Ruben A / Harrison, Claire N / Bose, Prithviraj / Gerds, Aaron T / Gupta, Vikas / Scott, Bart L / Kiladjian, Jean-Jacques / Lucchesi, Alessandro / Kong, Tim / Buckley, Sarah A / Tyavanagimatt, Shanthakumar / Harder, Bryan G / Roman-Torres, Karisse / Smith, Jennifer / Craig, Adam R / Mascarenhas, John / Verstovsek, Srdan

Blood advances

2023 Volume 7, Issue 19, Page(s) 5835–5842

Abstract: In patients with cytopenic myelofibrosis, treatment with the JAK2/IRAK1 inhibitor pacritinib was associated with anemia benefit in the phase 3 PERSIST-2 study. The impact of pacritinib on transfusion independence (TI) has not been previously described, ... ...

Abstract	In patients with cytopenic myelofibrosis, treatment with the JAK2/IRAK1 inhibitor pacritinib was associated with anemia benefit in the phase 3 PERSIST-2 study. The impact of pacritinib on transfusion independence (TI) has not been previously described, nor has the mechanism by which pacritinib improves anemia been elucidated. Because it has been previously postulated that inhibition of activin A receptor, type 1 (ACVR1)/activin receptor-like kinase-2 improves anemia in patients with myelofibrosis via suppression of hepcidin production, we assessed the relative inhibitory potency of pacritinib compared with other JAK2 inhibitors against ACVR1. Pacritinib inhibited ACVR1 with greater potency (half-maximal inhibitory concentration [IC50] = 16.7 nM; Cmax:IC50 = 12.7) than momelotinib (IC50 = 52.5 nM; Cmax:IC50 = 3.2), fedratinib (IC50 = 273 nM; Cmax:IC50 = 1.0), or ruxolitinib (IC50 > 1000; Cmax:IC50 < 0.01). Pacritinib's inhibitory activity against ACVR1 was corroborated via inhibition of downstream SMAD signaling in conjunction with marked suppression of hepcidin production. Among patients on PERSIST-2 who were not transfusion independent at baseline based on Gale criteria, a significantly greater proportion achieved TI on pacritinib compared with those treated on best available therapy (37% vs 7%, P = .001), and significantly more had a ≥50% reduction in transfusion burden (49% vs 9%, P < .0001). These data indicate that the anemia benefit of the JAK2/IRAK1 inhibitor pacritinib may be a function of potent ACVR1 inhibition.
MeSH term(s)	Humans ; Primary Myelofibrosis/complications ; Primary Myelofibrosis/drug therapy ; Hepcidins ; Janus Kinase 2 ; Anemia/etiology ; Anemia/complications ; Janus Kinase Inhibitors ; Activin Receptors, Type I
Chemical Substances	Hepcidins ; activin A ; 11-(2-pyrrolidin-1-ylethoxy)-14,19-dioxa-5,7,26-triazatetracyclo(19.3.1.1(2,6).1(8,12))heptacosa-1(25),2(26),3,5,8,10,12(27),16,21,23-decaene ; Janus Kinase 2 (EC 2.7.10.2) ; Janus Kinase Inhibitors ; ACVR1 protein, human (EC 2.7.11.30) ; Activin Receptors, Type I (EC 2.7.11.30)
Language	English
Publishing date	2023-08-13
Publishing country	United States
Document type	Journal Article
ZDB-ID	2915908-8
ISSN	2473-9537 ; 2473-9529
ISSN (online)	2473-9537
ISSN	2473-9529
DOI	10.1182/bloodadvances.2023010151
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Zs.A 7153: Show issues

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Article ; Online: Inhibition of phosphatidylinositol 3-kinase by PX-866 suppresses temozolomide-induced autophagy and promotes apoptosis in glioblastoma cells.

Harder, Bryan G / Peng, Sen / Sereduk, Christopher P / Sodoma, Andrej M / Kitange, Gaspar J / Loftus, Joseph C / Sarkaria, Jann N / Tran, Nhan L

Molecular medicine (Cambridge, Mass.)

2019 Volume 25, Issue 1, Page(s) 49

Abstract: Background: Temozolomide (TMZ) is the most commonly used chemotherapeutic agent used to treat glioblastoma (GBM), which causes significant DNA damage to highly proliferative cells. Our observations have added to accumulating evidence that TMZ induces ... ...

Abstract	Background: Temozolomide (TMZ) is the most commonly used chemotherapeutic agent used to treat glioblastoma (GBM), which causes significant DNA damage to highly proliferative cells. Our observations have added to accumulating evidence that TMZ induces stress-responsive cellular programs known to promote cell survival, including autophagy. As such, targeting these survival pathways may represent new vulnerabilities of GBM after treatment with TMZ. Methods: Using the T98G human glioma cell line, we assessed the molecular signaling associated with TMZ treatment, the cellular consequences of using the pan-PI3K inhibitor PX-866, and performed clonogenic assays to determine the effect sequential treatment of TMZ and PX-866 had on colony formation. Additionally, we also use subcutaneous GBM patient derived xenograft (PDX) tumors to show relative LC3 protein expression and correlations between survival pathways and molecular markers which dictate clinical responsiveness to TMZ. Results: Here, we report that TMZ can induce autophagic flux in T98G glioma cells. GBM patient-derived xenograft (PDX) tumors treated with TMZ also display an increase in the autophagosome marker LC3 II. Additionally, O Conclusions: The understanding of how TMZ induces survival pathways, such as autophagy, may offer new therapeutic vulnerabilities and opportunities to use sequential inhibition of alternate pro-survival pathways that regulate autophagy. As such, identification of additional ways to inhibit TMZ-induced autophagy could enhance the efficacy of TMZ.
MeSH term(s)	Apoptosis/drug effects ; Autophagy/drug effects ; Brain Neoplasms/metabolism ; Cell Line, Tumor ; Glioblastoma/metabolism ; Gonanes/pharmacology ; Humans ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphoinositide-3 Kinase Inhibitors/pharmacology ; Signal Transduction/drug effects ; Temozolomide/pharmacology
Chemical Substances	Gonanes ; PX-866 ; Phosphoinositide-3 Kinase Inhibitors ; Temozolomide (YF1K15M17Y)
Language	English
Publishing date	2019-11-14
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1283676-x
ISSN	1528-3658 ; 1076-1551
ISSN (online)	1528-3658
ISSN	1076-1551
DOI	10.1186/s10020-019-0116-z
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Zs.A 4456: Show issues

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Article: Developments in Blood-Brain Barrier Penetrance and Drug Repurposing for Improved Treatment of Glioblastoma.

Harder, Bryan G / Blomquist, Mylan R / Wang, Junwen / Kim, Anthony J / Woodworth, Graeme F / Winkles, Jeffrey A / Loftus, Joseph C / Tran, Nhan L

Frontiers in oncology

2018 Volume 8, Page(s) 462

Abstract: Glioblastoma (GBM) is one of the most common, deadly, and difficult-to-treat adult brain tumors. Surgical removal of the tumor, followed by radiotherapy (RT) and temozolomide (TMZ) administration, is the current treatment modality, but this regimen only ... ...

Abstract	Glioblastoma (GBM) is one of the most common, deadly, and difficult-to-treat adult brain tumors. Surgical removal of the tumor, followed by radiotherapy (RT) and temozolomide (TMZ) administration, is the current treatment modality, but this regimen only modestly improves overall patient survival. Invasion of cells into the surrounding healthy brain tissue prevents complete surgical resection and complicates treatment strategies with the goal of preserving neurological function. Despite significant efforts to increase our understanding of GBM, there have been relatively few therapeutic advances since 2005 and even fewer treatments designed to effectively treat recurrent tumors that are resistant to therapy. Thus, while there is a pressing need to move new treatments into the clinic, emerging evidence suggests that key features unique to GBM location and biology, the blood-brain barrier (BBB) and intratumoral molecular heterogeneity, respectively, stand as critical unresolved hurdles to effective therapy. Notably, genomic analyses of GBM tissues has led to the identification of numerous gene alterations that govern cell growth, invasion and survival signaling pathways; however, the drugs that show pre-clinical potential against signaling pathways mediated by these gene alterations cannot achieve effective concentrations at the tumor site. As a result, identifying BBB-penetrating drugs and utilizing new and safer methods to enhance drug delivery past the BBB has become an area of intensive research. Repurposing and combining FDA-approved drugs with evidence of penetration into the central nervous system (CNS) has also seen new interest for the treatment of both primary and recurrent GBM. In this review, we discuss emerging methods to strategically enhance drug delivery to GBM and repurpose currently-approved and previously-studied drugs using rational combination strategies.
Language	English
Publishing date	2018-10-23
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2649216-7
ISSN	2234-943X
ISSN	2234-943X
DOI	10.3389/fonc.2018.00462
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Article ; Online: Phosphotyrosine-dependent in vitro reconstitution of recombinant LAT-nucleated multiprotein signalling complexes on liposomes.

Sangani, Dhaval / Venien-Bryan, Catherine / Harder, Thomas

Molecular membrane biology

2009 Volume 26, Issue 3, Page(s) 159–170

Abstract: Numerous cell surface receptors propagate activation signals to the interior of the cell via tyrosine phosphorylation of transmembrane proteins. This leads to the phosphotyrosine (PiY)-mediated recruitment of cytoplasmic signalling protein complexes ... ...

Abstract	Numerous cell surface receptors propagate activation signals to the interior of the cell via tyrosine phosphorylation of transmembrane proteins. This leads to the phosphotyrosine (PiY)-mediated recruitment of cytoplasmic signalling protein complexes which catalyze crucial biochemical signalling reactions. Here we describe the first in vitro reconstitution of such PiY-nucleated protein complexes on an artificial lipid membrane. A tyrosine phosphorylated recombinant variant of the transmembrane adaptor protein Linker for Activation of T cells (PiYLAT) was anchored in liposomes. These PiYLAT proteoliposomes specifically recruited cooperative high avidity signalling protein complexes from Jurkat cytosol. Nucleation of signalling protein assemblies readily occurred on PiYLAT liposomes composed of phosphatidylserine, but not on PiYLAT liposomes composed of phosphatidylcholine. Purified recombinant grb2 alone did not stably associate with tyrosine phosphorylated LAT proteoliposomes. However, when grb2 was presented to the PiYLAT proteoliposomes in the context of Jurkat cytosol it was incorporated into multiprotein signalling complexes. Together the data suggest that these reconstituted high-avidity signalling protein complexes represent a cooperative protein network. This novel in vitro approach offers a novel technology permitting biochemical, structural, and pharmacological analyses of plasma membrane receptor signalling complexes.
MeSH term(s)	Adaptor Proteins, Signal Transducing/chemistry ; Cytosol ; Humans ; Jurkat Cells ; Liposomes/chemistry ; Membrane Proteins/chemistry ; Models, Biological ; Multiprotein Complexes/chemistry ; Phosphotyrosine ; Protein Binding ; Recombinant Proteins ; Signal Transduction
Chemical Substances	Adaptor Proteins, Signal Transducing ; LAT protein, human ; Liposomes ; Membrane Proteins ; Multiprotein Complexes ; Recombinant Proteins ; Phosphotyrosine (21820-51-9)
Language	English
Publishing date	2009-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1186324-9
ISSN	1464-5203 ; 0968-7688
ISSN (online)	1464-5203
ISSN	0968-7688
DOI	10.1080/09687680802637660
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Zs.A 1504: Show issues

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Article ; Online: Arsenic Compromises Both p97 and Proteasome Functions.

Tillotson, Joseph / Zerio, Christopher J / Harder, Bryan / Ambrose, Andrew J / Jung, Kevin S / Kang, MinJin / Zhang, Donna D / Chapman, Eli

Chemical research in toxicology

2017 Volume 30, Issue 7, Page(s) 1508–1514

Abstract: Exposure to arsenic is a worldwide problem that affects more than 200 million people. The underlying mechanisms of arsenic toxicity have been difficult to ascertain due to arsenic's pleotropic effects. A number of recent investigations have shown that ... ...

Abstract	Exposure to arsenic is a worldwide problem that affects more than 200 million people. The underlying mechanisms of arsenic toxicity have been difficult to ascertain due to arsenic's pleotropic effects. A number of recent investigations have shown that arsenic can compromise protein quality control through the ubiquitin proteasome system (UPS) or the endoplasmic reticulum associated protein degradation (ERAD) pathway. In this article, a link between arsenic and protein quality control is reported. Biochemical and cellular data demonstrate a misregulation of the ATPase cycle of the ATPase associated with various cellular activities (AAA+) chaperone, p97. Interestingly, the loss of p97 activity is due to the increased rate of ATP hydrolysis, which mimics a collection of pathogenic genetic p97 lesions. Cellular studies, using a well characterized reporter of both the proteasome and p97, show the proteasome to also be compromised. This loss of both p97 and proteasome functions can explain the catastrophic protein quality control issues observed in acute, high level arsenic exposures.
MeSH term(s)	Adenosine Triphosphatases/antagonists & inhibitors ; Adenosine Triphosphatases/metabolism ; Animals ; Arsenic/toxicity ; Cells, Cultured ; Hydrolysis ; Mice ; NIH 3T3 Cells ; Proteasome Endopeptidase Complex/metabolism
Chemical Substances	Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Adenosine Triphosphatases (EC 3.6.1.-) ; Arsenic (N712M78A8G)
Language	English
Publishing date	2017-07-07
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	639353-6
ISSN	1520-5010 ; 0893-228X
ISSN (online)	1520-5010
ISSN	0893-228X
DOI	10.1021/acs.chemrestox.7b00158
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Zs.A 2320: Show issues

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Article ; Online: Brusatol overcomes chemoresistance through inhibition of protein translation.

Harder, Bryan / Tian, Wang / La Clair, James J / Tan, Aik-Choon / Ooi, Aikseng / Chapman, Eli / Zhang, Donna D

Molecular carcinogenesis

2017 Volume 56, Issue 5, Page(s) 1493–1500

Abstract: The NRF2 pathway activates a cell survival response when cells are exposed to xenobiotics or are under oxidative stress. Therapeutic activation of NRF2 can also be used prior to insult as a means of disease prevention. However, prolonged expression of ... ...

Abstract	The NRF2 pathway activates a cell survival response when cells are exposed to xenobiotics or are under oxidative stress. Therapeutic activation of NRF2 can also be used prior to insult as a means of disease prevention. However, prolonged expression of NRF2 has been shown to protect cancer cells by inducing the metabolism and efflux of chemotherapeutics, leading to both intrinsic and acquired chemoresistance to cancer drugs. This effect has been termed the "dark side" of NRF2. In an effort to combat this chemoresistance, our group discovered the first NRF2 inhibitor, the natural product brusatol, however the mechanism of inhibition was previously unknown. In this report, we show that brusatol's mode of action is not through direct inhibition of the NRF2 pathway, but through the inhibition of both cap-dependent and cap-independent protein translation, which has an impact on many short-lived proteins, including NRF2. Therefore, there is still a need to develop a new generation of specific NRF2 inhibitors with limited toxicity and off-target effects that could be used as adjuvant therapies to sensitize cancers with high expression of NRF2.
MeSH term(s)	Cell Line, Tumor ; Drug Resistance, Neoplasm/drug effects ; Drug Resistance, Neoplasm/genetics ; Endoplasmic Reticulum/drug effects ; Gene Expression Regulation, Neoplastic ; Humans ; NF-E2-Related Factor 2/antagonists & inhibitors ; NF-E2-Related Factor 2/genetics ; NF-E2-Related Factor 2/metabolism ; Protein Biosynthesis/drug effects ; Quassins/pharmacokinetics ; Quassins/pharmacology ; Sequence Analysis, RNA
Chemical Substances	NF-E2-Related Factor 2 ; NFE2L2 protein, human ; Quassins ; brusatol (14907-98-3)
Language	English
Publishing date	2017-02-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1004029-8
ISSN	1098-2744 ; 0899-1987
ISSN (online)	1098-2744
ISSN	0899-1987
DOI	10.1002/mc.22609
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