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  • 1.
    Boutajangout, Allal
    et al.
    NYU, Ctr Cognit Neurol, Langone Hlth, New York, NY 10016 USA.;NYU, Dept Neurol, Langone Hlth, New York, NY 10016 USA.;NYU, Dept Psychiat, Langone Hlth, 550 1St Ave, New York, NY 10016 USA.;NYU, Langone Med Ctr, Dept Physiol & Neurosci, New York, NY USA..
    Lindberg, Hanna
    KTH, Skolan för kemi, bioteknologi och hälsa (CBH), Proteinvetenskap.
    Awwad, Abdulaziz
    King Abdulaziz Univ, Sch Med, Jeddah, Saudi Arabia..
    Paul, Arun
    NYU, Ctr Cognit Neurol, Langone Hlth, New York, NY 10016 USA.;NYU, Dept Neurol, Langone Hlth, New York, NY 10016 USA..
    Baitalmal, Rabaa
    NYU, Ctr Cognit Neurol, Langone Hlth, New York, NY 10016 USA.;NYU, Dept Neurol, Langone Hlth, New York, NY 10016 USA..
    Almokyad, Ismail
    NYU, Ctr Cognit Neurol, Langone Hlth, New York, NY 10016 USA.;NYU, Dept Neurol, Langone Hlth, New York, NY 10016 USA..
    Hoiden-Guthenberg, Ingmarie
    Affibody AB, Solna, Sweden..
    Gunneriusson, Elin
    Affibody AB, Solna, Sweden..
    Frejd, Fredrik Y.
    Affibody AB, Solna, Sweden..
    Hard, Torleif
    Swedish Univ Agr Sci SLU, Dept Chem & Biotechnol, Uppsala, Sweden..
    Löfblom, John
    KTH, Skolan för kemi, bioteknologi och hälsa (CBH), Proteinvetenskap.
    Ståhl, Stefan
    KTH, Skolan för kemi, bioteknologi och hälsa (CBH), Proteinvetenskap.
    Wisniewski, Thomas
    NYU, Ctr Cognit Neurol, Langone Hlth, New York, NY 10016 USA.;NYU, Dept Neurol, Langone Hlth, New York, NY 10016 USA.;NYU, Dept Psychiat, Langone Hlth, 550 1St Ave, New York, NY 10016 USA.;NYU, Sch Med, Dept Pathol, New York, NY 10016 USA..
    Affibody-Mediated Sequestration of Amyloid beta Demonstrates Preventive Efficacy in a Transgenic Alzheimer's Disease Mouse Model2019Inngår i: Frontiers in Aging Neuroscience, ISSN 1663-4365, E-ISSN 1663-4365, Vol. 11, artikkel-id 64Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    Different strategies for treatment and prevention of Alzheimer's disease (AD) are currently under investigation, including passive immunization with anti-amyloid beta (anti-A beta) monoclonal antibodies (mAbs). Here, we investigate the therapeutic potential of a novel type of A beta-targeting agent based on an affibody molecule with fundamentally different properties to mAbs. We generated a therapeutic candidate, denoted Z(SYM73)-albumin-binding domain (ABD; 16.8 kDa), by genetic linkage of the dimeric Z(SYM73) affibody for sequestering of monomeric A beta-peptides and an ABD for extension of its in vivo half-life. Amyloid precursor protein (APP)/PS1 transgenic AD mice were administered with Z(SYM73)-ABD, followed by behavioral examination and immunohistochemistry. Results demonstrated rescued cognitive functions and significantly lower amyloid burden in the treated animals compared to controls. No toxicological symptoms or immunology-related side-effects were observed. To our knowledge, this is the first reported in vivo investigation of a systemically delivered scaffold protein against monomeric A beta, demonstrating a therapeutic potential for prevention of AD.

  • 2. Gasparrini, S.
    et al.
    Cippitelli, E.
    Gambi, E.
    Spinsante, S.
    Wåhslén, Jonas
    KTH, Skolan för teknik och hälsa (STH), Medicinsk teknik, Data- och elektroteknik.
    Orhan, Ibrahim
    KTH, Skolan för teknik och hälsa (STH), Medicinsk teknik, Data- och elektroteknik.
    Lindh, Thomas
    KTH, Skolan för teknik och hälsa (STH), Medicinsk teknik, Data- och elektroteknik.
    Proposal and experimental evaluation of fall detection solution based on wearable and depth data fusion2016Inngår i: ICT Innovations 2015: Emerging Technologies For Better Living, Springer, 2016, Vol. 399, s. 99-108Konferansepaper (Fagfellevurdert)
    Abstract [en]

    Fall injury issues represent a serious problem for elderly in our society. These people want to live in their home as long as possible and technology can improve their security and independence. In this work we study the joint use of a camera based system and wearable devices, in the so called data fusion approach, to design a fall detection solution. The synchronization issues between the heterogeneous data provided by the devices are properly treated, and three different fall detection algorithms are implemented. Experimental results are also provided, to compare the proposed solutions.

  • 3. Lin, Tzung-Sheng
    et al.
    Hsieh, Chang-Hsun
    Kuo, Chin
    Juang, Yu-Pu
    Hsieh, Yves S. Y.
    KTH, Skolan för kemi, bioteknologi och hälsa (CBH), Kemi, Glykovetenskap.
    Chiang, Hongsen
    Hung, Shang-Cheng
    Jiang, Ching-Chuan
    Liang, Pi-Hui
    Sulfation pattern of chondroitin sulfate in human osteoarthritis cartilages reveals a lower level of chondroitin-4-sulfate2019Inngår i: Carbohydrate Polymers, ISSN 0144-8617, E-ISSN 1879-1344Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    Chondroitin sulfates (CS) account for more than 80% of glycosaminoglycans of articular cartilage, which imparts its physiological functions. We quantified the absolute concentration of the CS components of the full thickness cartilages from the knees of patients with terminal-phase osteoarthritis. Osteochondrol biopsies were removed from the medial femoral condyle and lateral femoral condyle of sixty female patients receiving total knee arthroplasty, aged from 58 to 83 years old. We found that total CS concentrations and chondroitin-4-sulfate disaccharide were significantly lowered in osteoarthritic samples. Microstructure analysis indicated that while chondroitin-0-sulfate was equally distributed across different zones of the osteoarthritic cartilages, chondroitin-4-sulfate is significantly less in the deep zones. Down-regulation of sulfotransferases, the enzymes responsible for CS sulfation in the lesion site of cartilage were observed. Our study suggested chondroitin-4-sulfate down-regulation may be a diagnostic marker for degraded osteoarthritis cartilage, with potential implications in cartilage regeneration.

  • 4. Sillén, Anna
    et al.
    Brohede, Jesper
    Forsell, Charlotte
    Lilius, Lena
    Andrade, Jorge
    KTH, Skolan för bioteknologi (BIO).
    Odeberg, Jacob
    KTH, Skolan för bioteknologi (BIO), Proteomik.
    Kimura, Toru
    Winblad, Bengt
    Graff, Caroline
    Linkage Analysis of Autopsy-Confirmed Familial Alzheimer Disease Supports an Alzheimer Disease Locus in 8q242011Inngår i: Dementia and Geriatric Cognitive Disorders, ISSN 1420-8008, E-ISSN 1421-9824, Vol. 31, nr 2, s. 109-118Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    Background/Aims: We have previously reported the results of an extended genome-wide scan of Swedish Alzheimer disease (AD)-affected families; in this paper, we analyzed a subset of these families with autopsy-confirmed AD. Methods: We report the fine-mapping, using both microsatellite markers and single-nucleotide polymorphisms (SNPs), in the observed maximum logarithm of the odds (LOD)-2 unit (LODmax-2) region under the identified linkage peak, linkage analysis of the fine-mapping data with additionally analyzed pedigrees, and association analysis of SNPs selected from candidate genes in the linked interval. The subset was made on the criterion of at least one autopsy-confirmed AD case per family, resulting in 24 families. Results: Linkage analysis of a family subset having at least one autopsy-confirmed AD case showed a significant nonparametric single-point LOD score of 4.4 in 8q24. Fine-mapping under the linkage peak with 10 microsatellite markers yielded an increase in the multipoint (mpt) LOD score from 2.1 to 3.0. SNP genotyping was performed on 21 selected candidate transcripts of the LODmax-2 region. Both family-based association and linkage analysis were performed on extended material from 30 families, resulting in a suggestive linkage at peak marker rs6577853 (mpt LOD score = 2.4). Conclusion: The 8q24 region has been implicated to be involved in AD etiology.

  • 5.
    Åberg, Anna Cristina
    et al.
    Swedish School of Sports and Health Sciences.
    Frykberg, Gunilla
    Uppsala University.
    Halvorsen, Kjartan
    The Swedish School of Sport and Health Sciences, Stockholm, Sweden.
    Medio-lateral stability of sit-to-walk performance in older individuals with and without fear of falling2010Inngår i: Gait & Posture, ISSN 0966-6362, E-ISSN 1879-2219, Vol. 31, nr 4, s. 438-443Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    Most falls in older people are due to loss of balance during everyday locomotion, e.g., when initiating walking from sitting; sit-to-walk (STW). It has been considered that the broader stride width in walking that is seen in many people with fear of falling (FoF) does not increase stability, but could be predictive of future falls because of increased medio-lateral (ML) velocity of the body centre of mass (CoM). This study was aimed to examine step-, velocity- and stability-related parameters, focusing on ML stability, in STW performance of people with and without FoF. Ten subjects with FoF and 10 matched controls, aged >= 70 years, were included. Kinematic and kinetic data were collected in a laboratory. Stability parameters were calculated from a formula implying that the vertical projection of the CoM extrapolated by adding its velocity times a factor root l/g (height of inverted pendulum divided by gravity) should fall within the base of support (BoS). A related spatial margin of stability (SMoS), defined as the minimum distance from the extrapolated CoM (XCoM) to the boundaries of the BoS, was also calculated. In the phase 'seat-off-second-toe-off, the FoF group had significantly (p < 0.05) shorter and broader steps, lower forward but similar ML CoM velocity, and broader CoM and XCoM widths. The FoF group therefore exhibited a disproportionately large sideways velocity compared to the controls. This indicates that STW may be a hazardous transfer for older people with FoF, which should be relevant in assessment and training aimed at preventing falls.

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